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Conserved domains on  [gi|767985480|ref|XP_011520397|]
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CD276 antigen isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
250-360 1.94e-63

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


:

Pssm-ID: 409528  Cd Length: 115  Bit Score: 202.83  E-value: 1.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 250 QVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTE----GRDQGSAYANRTALFPDLLAQGNASL 325
Cdd:cd20934    1 RVPEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDTKQLVHSFTEsqdqGRDQGSAYANRTALFPDLLAQGNASL 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767985480 326 RLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPY 360
Cdd:cd20934   81 RLQRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
32-142 1.42e-61

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


:

Pssm-ID: 409528  Cd Length: 115  Bit Score: 197.82  E-value: 1.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  32 QVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQ----DQGSAYANRTALFPDLLAQGNASL 107
Cdd:cd20934    1 RVPEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDTKQLVHSFTESQdqgrDQGSAYANRTALFPDLLAQGNASL 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767985480 108 RLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPY 142
Cdd:cd20934   81 RLQRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
144-224 1.06e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.18  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  144 KPSMTLEPNK-DLRPGDTVTITCSSyQGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFdvhSILRVVLGANGTYSCLV 222
Cdd:pfam13927   1 KPVITVSPSSvTVREGETVTLTCEA-TGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTL---TISNVTRSDAGTYTCVA 76

                  ..
gi 767985480  223 RN 224
Cdd:pfam13927  77 SN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
362-442 3.54e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.64  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  362 KPSMTLEPNK-DLRPGDTVTITCSSyRGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSVLRvvlGANGTYSCLV 440
Cdd:pfam13927   1 KPVITVSPSSvTVREGETVTLTCEA-TGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTR---SDAGTYTCVA 76

                  ..
gi 767985480  441 RN 442
Cdd:pfam13927  77 SN 78
 
Name Accession Description Interval E-value
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
250-360 1.94e-63

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 202.83  E-value: 1.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 250 QVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTE----GRDQGSAYANRTALFPDLLAQGNASL 325
Cdd:cd20934    1 RVPEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDTKQLVHSFTEsqdqGRDQGSAYANRTALFPDLLAQGNASL 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767985480 326 RLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPY 360
Cdd:cd20934   81 RLQRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
32-142 1.42e-61

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 197.82  E-value: 1.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  32 QVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQ----DQGSAYANRTALFPDLLAQGNASL 107
Cdd:cd20934    1 RVPEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDTKQLVHSFTESQdqgrDQGSAYANRTALFPDLLAQGNASL 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767985480 108 RLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPY 142
Cdd:cd20934   81 RLQRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
144-224 1.06e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.18  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  144 KPSMTLEPNK-DLRPGDTVTITCSSyQGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFdvhSILRVVLGANGTYSCLV 222
Cdd:pfam13927   1 KPVITVSPSSvTVREGETVTLTCEA-TGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTL---TISNVTRSDAGTYTCVA 76

                  ..
gi 767985480  223 RN 224
Cdd:pfam13927  77 SN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
362-442 3.54e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.64  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  362 KPSMTLEPNK-DLRPGDTVTITCSSyRGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSVLRvvlGANGTYSCLV 440
Cdd:pfam13927   1 KPVITVSPSSvTVREGETVTLTCEA-TGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTR---SDAGTYTCVA 76

                  ..
gi 767985480  441 RN 442
Cdd:pfam13927  77 SN 78
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
250-340 1.95e-06

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 46.68  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  250 QVPEDPVVALvGTDATLRCSFSPEPgfSLAQLNLIWQLTDT----KQLVHSFTEGRDQGSaYANRTALFPDLlAQGNASL 325
Cdd:pfam07686   1 QTPREVTVAL-GGSVTLPCTYSSSM--SEASTSVYWYRQPPgkgpTFLIAYYSNGSEEGV-KKGRFSGRGDP-SNGDGSL 75
                          90
                  ....*....|....*
gi 767985480  326 RLQRVRVADEGSFTC 340
Cdd:pfam07686  76 TIQNLTLSDSGTYTC 90
IgC1_PD-L2 cd20986
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ...
375-442 2.11e-06

Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients.


Pssm-ID: 409578  Cd Length: 82  Bit Score: 45.79  E-value: 2.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767985480 375 PG-DTVTITCSSyRGYPEAEVFWQDgqgVPLTGNvtTSQMANEQGLFDVHSVLRVVLGANGTYSCLVRN 442
Cdd:cd20986    8 PGtGEVQLTCQA-RGYPLAEVSWQN---VSVPAN--TSHTRTPEGLYQVTSVLRLKPQPGRNFSCMFWN 70
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
32-122 5.63e-06

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 45.14  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   32 QVPEDPVVALvGTDATLCCSFSPEPgfSLAQLNLIWQLTDT----KQLVHSFAEGQDQGSaYANRTALFPDLlAQGNASL 107
Cdd:pfam07686   1 QTPREVTVAL-GGSVTLPCTYSSSM--SEASTSVYWYRQPPgkgpTFLIAYYSNGSEEGV-KKGRFSGRGDP-SNGDGSL 75
                          90
                  ....*....|....*
gi 767985480  108 RLQRVRVADEGSFTC 122
Cdd:pfam07686  76 TIQNLTLSDSGTYTC 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
161-233 6.04e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.24  E-value: 6.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767985480 161 VTITCSsYQGYPEAEVFWQ-DGQGVPLTGNVTTSQMANEQGLfdvhSILRVVLGANGTYSCLVRNPVLQQDAHS 233
Cdd:cd00096    1 VTLTCS-ASGNPPPTITWYkNGKPLPPSSRDSRRSELGNGTL----TISNVTLEDSGTYTCVASNSAGGSASAS 69
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
156-237 6.46e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 6.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   156 RPGDTVTITCsSYQGYPEAEVFW--QDGQGVPLTGNVTTSQMANEQGLFdvhsILRVVLGANGTYSCLVRNPVLQQDAHS 233
Cdd:smart00410   7 KEGESVTLSC-EASGSPPPEVTWykQGGKLLAESGRFSVSRSGSTSTLT----ISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 767985480   234 SVTI 237
Cdd:smart00410  82 TLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
374-456 8.80e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 41.34  E-value: 8.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   374 RPGDTVTITCsSYRGYPEAEVFW--QDGQGVPLTGNVTTSQMANEQGLFdvhsVLRVVLGANGTYSCLVRNPVlqQDAHG 451
Cdd:smart00410   7 KEGESVTLSC-EASGSPPPEVTWykQGGKLLAESGRFSVSRSGSTSTLT----ISNVTPEDSGTYTCAATNSS--GSASS 79

                   ....*
gi 767985480   452 SVTIT 456
Cdd:smart00410  80 GTTLT 84
IGv smart00406
Immunoglobulin V-Type;
263-342 1.33e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 40.44  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   263 DATLRCSFSpepGFSLAQLNLIWQ-LTDTKQLVHsFTEGRDQGSAYA-----NRTALFPDLlAQGNASLRLQRVRVADEG 336
Cdd:smart00406   1 SVTLSCKFS---GSTFSSYYVSWVrQPPGKGLEW-LGYIGSNGSSYYqesykGRFTISKDT-SKNDVSLTISNLRVEDTG 75

                   ....*.
gi 767985480   337 SFTCFV 342
Cdd:smart00406  76 TYYCAV 81
IGv smart00406
Immunoglobulin V-Type;
45-124 2.12e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 40.06  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480    45 DATLCCSFSpepGFSLAQLNLIWQ-LTDTKQLVHsFAEGQDQGSAYA-----NRTALFPDLlAQGNASLRLQRVRVADEG 118
Cdd:smart00406   1 SVTLSCKFS---GSTFSSYYVSWVrQPPGKGLEW-LGYIGSNGSSYYqesykGRFTISKDT-SKNDVSLTISNLRVEDTG 75

                   ....*.
gi 767985480   119 SFTCFV 124
Cdd:smart00406  76 TYYCAV 81
 
Name Accession Description Interval E-value
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
250-360 1.94e-63

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 202.83  E-value: 1.94e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 250 QVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTE----GRDQGSAYANRTALFPDLLAQGNASL 325
Cdd:cd20934    1 RVPEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDTKQLVHSFTEsqdqGRDQGSAYANRTALFPDLLAQGNASL 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767985480 326 RLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPY 360
Cdd:cd20934   81 RLQRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
32-142 1.42e-61

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 197.82  E-value: 1.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  32 QVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQ----DQGSAYANRTALFPDLLAQGNASL 107
Cdd:cd20934    1 RVPEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDTKQLVHSFTESQdqgrDQGSAYANRTALFPDLLAQGNASL 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767985480 108 RLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPY 142
Cdd:cd20934   81 RLQRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
39-125 2.92e-21

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 88.81  E-value: 2.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  39 VALVGTDATLCCSFSPEPgfSLAQLNLIWQLTDTKQLVHSFAEGQD----QGSAYANRTALFPDLLAQGNASLRLQRVRV 114
Cdd:cd20984    8 AGNIGEDGILSCTFTPDI--KLSDIVIQWLKEGDSGLVHEFKEGKDelsrQSPMFRGRTSLFADQVHVGNASLRLKNVQL 85
                         90
                 ....*....|.
gi 767985480 115 ADEGSFTCFVS 125
Cdd:cd20984   86 TDAGTYLCIIS 96
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
34-139 3.02e-21

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 88.79  E-value: 3.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  34 PEDPVVALVGTDATLCCSFSPEpgFSLAQLNLIWQLTDTKQLVHSFAEGQDQGS----AYANRTALFPDLLAQGNASLRL 109
Cdd:cd05713    6 PTEPILALVGEDAELPCHLSPK--MSAEHMEVRWFRSQFSPVVHLYRDGQDQEEeqmpEYRGRTELLKDAIAEGSVALRI 83
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767985480 110 QRVRVADEGSFTCFVSIRDF-GSAAVSLQVA 139
Cdd:cd05713   84 HNVRPSDEGQYTCFFRSGSFyEEATLELKVA 114
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
252-357 3.85e-21

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 88.79  E-value: 3.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 252 PEDPVVALVGTDATLRCSFSPEpgFSLAQLNLIWQLTDTKQLVHSFTEGRDQGS----AYANRTALFPDLLAQGNASLRL 327
Cdd:cd05713    6 PTEPILALVGEDAELPCHLSPK--MSAEHMEVRWFRSQFSPVVHLYRDGQDQEEeqmpEYRGRTELLKDAIAEGSVALRI 83
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767985480 328 QRVRVADEGSFTCFVSIRDF-GSAAVSLQVA 357
Cdd:cd05713   84 HNVRPSDEGQYTCFFRSGSFyEEATLELKVA 114
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
257-343 7.76e-21

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 87.65  E-value: 7.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 257 VALVGTDATLRCSFSPEPgfSLAQLNLIWQLTDTKQLVHSFTEGRD----QGSAYANRTALFPDLLAQGNASLRLQRVRV 332
Cdd:cd20984    8 AGNIGEDGILSCTFTPDI--KLSDIVIQWLKEGDSGLVHEFKEGKDelsrQSPMFRGRTSLFADQVHVGNASLRLKNVQL 85
                         90
                 ....*....|.
gi 767985480 333 ADEGSFTCFVS 343
Cdd:cd20984   86 TDAGTYLCIIS 96
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
253-356 4.80e-20

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 85.13  E-value: 4.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 253 EDPVVALVGTDATLRCSFSPEPgfslaQLNLIWQLTDTKQLVHSFTEGRD----QGSAYANRTALFPDLLAQGNASLRLQ 328
Cdd:cd16091    4 EVIVVCLLSEDCILPCSFTPGS-----EVVIHWYKQDSDIKVHSYYYGKDqlesQDQRYRNRTSLFKDQISNGNASLLLR 78
                         90       100
                 ....*....|....*....|....*....
gi 767985480 329 RVRVADEGSFTCFVS-IRDFGSAAVSLQV 356
Cdd:cd16091   79 RVQLQDEGRYKCYTStIIGNQESFVNLKV 107
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
35-138 7.23e-20

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 84.75  E-value: 7.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  35 EDPVVALVGTDATLCCSFSPEPgfslaQLNLIWQLTDTKQLVHSFAEGQD----QGSAYANRTALFPDLLAQGNASLRLQ 110
Cdd:cd16091    4 EVIVVCLLSEDCILPCSFTPGS-----EVVIHWYKQDSDIKVHSYYYGKDqlesQDQRYRNRTSLFKDQISNGNASLLLR 78
                         90       100
                 ....*....|....*....|....*....
gi 767985480 111 RVRVADEGSFTCFVS-IRDFGSAAVSLQV 138
Cdd:cd16091   79 RVQLQDEGRYKCYTStIIGNQESFVNLKV 107
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
249-343 7.04e-13

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 64.95  E-value: 7.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 249 VQVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTK--QLVHSFTEGRDQGSAYANRTALFPDLLAQGNASLR 326
Cdd:cd20947    1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNiiQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80
                         90
                 ....*....|....*..
gi 767985480 327 LQRVRVADEGSFTCFVS 343
Cdd:cd20947   81 ITDVKLQDAGVYRCMIS 97
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
31-125 2.97e-12

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 63.41  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  31 VQVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTK--QLVHSFAEGQDQGSAYANRTALFPDLLAQGNASLR 108
Cdd:cd20947    1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNiiQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80
                         90
                 ....*....|....*..
gi 767985480 109 LQRVRVADEGSFTCFVS 125
Cdd:cd20947   81 ITDVKLQDAGVYRCMIS 97
IgV_B7-H2 cd20935
Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of ...
256-357 3.05e-11

Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of the immunoglobulin variable (IgV) domain of B7-H2 (B7 homolog 2 also known as ICOSL (inducible T cell costimulator ligand) or CD275). B7-H2 is a ligand for the T-cell-specific cell surface receptor ICOS and acts as a costimulatory signal for T-cell proliferation and cytokine secretion. The interaction of ICOS with ICOSL (B7-H2) regulates T cell activation and expansion, is involved in T cell dependent B cell activation, and T-helper cell differentiation. It is a member of the B7 family of immune regulatory proteins and shares homology with other B7 ligands, such as B7-1, B7-2, B7-H1 (PD-L1), PD-L2, and B7-H3. The extracellular domains of B7 proteins contain two Ig-like domains and all members have short cytoplasmic domains. These ligands are typically expressed on antigen presenting cells (such as macrophages, B cells and dendritic cells) and have the ability to regulate T-cell proliferation and function. Tumor cells are also capable of expressing the B7 family members in order to evade immune surveillance.


Pssm-ID: 409529  Cd Length: 113  Bit Score: 60.65  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 256 VVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRDQG----SAYANRTALFPDLLAQGNASLRLQRVR 331
Cdd:cd20935    3 VRAMVGSDVELSCICPEGSRFDLNDLYVYWQISESETVVTYHLPQNSSLenvdSHYRNRALLSLDSMKQGDFSLRLFNVT 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767985480 332 VADEGSFTCFVSIRDFG-----SAAVSLQVA 357
Cdd:cd20935   83 PQDEQKFHCLVFSQSLElqkvlEVVVTLHVA 113
IgV_B7-H2 cd20935
Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of ...
38-139 1.56e-10

Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of the immunoglobulin variable (IgV) domain of B7-H2 (B7 homolog 2 also known as ICOSL (inducible T cell costimulator ligand) or CD275). B7-H2 is a ligand for the T-cell-specific cell surface receptor ICOS and acts as a costimulatory signal for T-cell proliferation and cytokine secretion. The interaction of ICOS with ICOSL (B7-H2) regulates T cell activation and expansion, is involved in T cell dependent B cell activation, and T-helper cell differentiation. It is a member of the B7 family of immune regulatory proteins and shares homology with other B7 ligands, such as B7-1, B7-2, B7-H1 (PD-L1), PD-L2, and B7-H3. The extracellular domains of B7 proteins contain two Ig-like domains and all members have short cytoplasmic domains. These ligands are typically expressed on antigen presenting cells (such as macrophages, B cells and dendritic cells) and have the ability to regulate T-cell proliferation and function. Tumor cells are also capable of expressing the B7 family members in order to evade immune surveillance.


Pssm-ID: 409529  Cd Length: 113  Bit Score: 58.34  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  38 VVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQDQG----SAYANRTALFPDLLAQGNASLRLQRVR 113
Cdd:cd20935    3 VRAMVGSDVELSCICPEGSRFDLNDLYVYWQISESETVVTYHLPQNSSLenvdSHYRNRALLSLDSMKQGDFSLRLFNVT 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767985480 114 VADEGSFTCFVSIRDFG-----SAAVSLQVA 139
Cdd:cd20935   83 PQDEQKFHCLVFSQSLElqkvlEVVVTLHVA 113
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
144-224 1.06e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.18  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  144 KPSMTLEPNK-DLRPGDTVTITCSSyQGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFdvhSILRVVLGANGTYSCLV 222
Cdd:pfam13927   1 KPVITVSPSSvTVREGETVTLTCEA-TGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTL---TISNVTRSDAGTYTCVA 76

                  ..
gi 767985480  223 RN 224
Cdd:pfam13927  77 SN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
362-442 3.54e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 50.64  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  362 KPSMTLEPNK-DLRPGDTVTITCSSyRGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSVLRvvlGANGTYSCLV 440
Cdd:pfam13927   1 KPVITVSPSSvTVREGETVTLTCEA-TGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTR---SDAGTYTCVA 76

                  ..
gi 767985480  441 RN 442
Cdd:pfam13927  77 SN 78
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
247-356 5.03e-08

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 51.29  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 247 VEVQVPEDpVVALVGTDATLRCSFSPEPGFSLAQLNliWQLTDTKQ----LVHSFTEGRDQGSAYANRTALFPDLLAQGN 322
Cdd:cd05718    1 QRVQVPTE-VTGFLGGSVTLPCSLTSPGTTKITQVT--WMKIGAGSsqnvAVFHPQYGPSVPNPYAERVEFLAARLGLRN 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767985480 323 ASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQV 356
Cdd:cd05718   78 ATLRIRNLRVEDEGNYICEFATFPQGNRQGTTWL 111
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
366-449 5.62e-07

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 47.41  E-value: 5.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  366 TLEPNKDLRPGD--TVTITCSSYRGYPEAEVFWQdGQGVPLTGNVTTSQMANEQGLFDVHSVLRVVL--GANG-TYSCLV 440
Cdd:pfam08205   2 TIEPPASLLEGEgpEVVATCSSAGGKPAPRITWY-LDGKPLEAAETSSEQDPESGLVTVTSELKLVPsrSDHGqSLTCQV 80

                  ....*....
gi 767985480  441 RNPVLQQDA 449
Cdd:pfam08205  81 SYGALRGSI 89
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
256-342 1.34e-06

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 46.94  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 256 VVALVGTDATLRCSFSPEPGFSLAQLNLIWQlTDTKQLVHSFTEGRDQ----GSAYANRTALfpdllAQGNASLRLQRVR 331
Cdd:cd16087    3 IQAYFNETAYLPCQFKNPQNISLSELVVFWQ-DQKKLVLYELYLGKEKldnvNSKYIGRTSF-----DQENWTLQLHNVQ 76
                         90
                 ....*....|.
gi 767985480 332 VADEGSFTCFV 342
Cdd:cd16087   77 IKDQGTYQCFI 87
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
148-231 1.48e-06

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 400489  Cd Length: 89  Bit Score: 46.26  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  148 TLEPNKDLRPGD--TVTITCSSYQGYPEAEVFWQdGQGVPLTGNVTTSQMANEQGLFDVHSILRVVL--GANG-TYSCLV 222
Cdd:pfam08205   2 TIEPPASLLEGEgpEVVATCSSAGGKPAPRITWY-LDGKPLEAAETSSEQDPESGLVTVTSELKLVPsrSDHGqSLTCQV 80

                  ....*....
gi 767985480  223 RNPVLQQDA 231
Cdd:pfam08205  81 SYGALRGSI 89
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
151-231 1.57e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 46.42  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  151 PNKDLRPGDTVTITCSSYQGYPEAEVFWQDGQGVPLTGNvTTSQMANEQGLFDVHsILRVVLGANGTYSCLVRNPVLQQD 230
Cdd:pfam00047   4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESL-KVKHDNGRTTQSSLL-ISNVTKEDAGTYTCVVNNPGGSAT 81

                  .
gi 767985480  231 A 231
Cdd:pfam00047  82 L 82
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
250-340 1.95e-06

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 46.68  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  250 QVPEDPVVALvGTDATLRCSFSPEPgfSLAQLNLIWQLTDT----KQLVHSFTEGRDQGSaYANRTALFPDLlAQGNASL 325
Cdd:pfam07686   1 QTPREVTVAL-GGSVTLPCTYSSSM--SEASTSVYWYRQPPgkgpTFLIAYYSNGSEEGV-KKGRFSGRGDP-SNGDGSL 75
                          90
                  ....*....|....*
gi 767985480  326 RLQRVRVADEGSFTC 340
Cdd:pfam07686  76 TIQNLTLSDSGTYTC 90
IgC1_PD-L2 cd20986
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ...
375-442 2.11e-06

Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients.


Pssm-ID: 409578  Cd Length: 82  Bit Score: 45.79  E-value: 2.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767985480 375 PG-DTVTITCSSyRGYPEAEVFWQDgqgVPLTGNvtTSQMANEQGLFDVHSVLRVVLGANGTYSCLVRN 442
Cdd:cd20986    8 PGtGEVQLTCQA-RGYPLAEVSWQN---VSVPAN--TSHTRTPEGLYQVTSVLRLKPQPGRNFSCMFWN 70
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
369-449 3.23e-06

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 45.26  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  369 PNKDLRPGDTVTITCSSYRGYPEAEVFWQDGQGVPLTGNvTTSQMANEQGLFDVHsVLRVVLGANGTYSCLVRNPVLQQD 448
Cdd:pfam00047   4 PTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESL-KVKHDNGRTTQSSLL-ISNVTKEDAGTYTCVVNNPGGSAT 81

                  .
gi 767985480  449 A 449
Cdd:pfam00047  82 L 82
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
30-138 3.63e-06

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 45.90  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  30 EVQVPEDpVVALVGTDATLCCSFSPEPGFSLAQLNliWQLTDTKQ----LVHSFAEGQDQGSAYANRTALFPDLLAQGNA 105
Cdd:cd05718    2 RVQVPTE-VTGFLGGSVTLPCSLTSPGTTKITQVT--WMKIGAGSsqnvAVFHPQYGPSVPNPYAERVEFLAARLGLRNA 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767985480 106 SLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQV 138
Cdd:cd05718   79 TLRIRNLRVEDEGNYICEFATFPQGNRQGTTWL 111
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
38-124 5.17e-06

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 45.39  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  38 VVALVGTDATLCCSFSPEPGFSLAQLNLIWQlTDTKQLVHSFAEGQDQ----GSAYANRTALfpdllAQGNASLRLQRVR 113
Cdd:cd16087    3 IQAYFNETAYLPCQFKNPQNISLSELVVFWQ-DQKKLVLYELYLGKEKldnvNSKYIGRTSF-----DQENWTLQLHNVQ 76
                         90
                 ....*....|.
gi 767985480 114 VADEGSFTCFV 124
Cdd:cd16087   77 IKDQGTYQCFI 87
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
32-122 5.63e-06

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 45.14  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   32 QVPEDPVVALvGTDATLCCSFSPEPgfSLAQLNLIWQLTDT----KQLVHSFAEGQDQGSaYANRTALFPDLlAQGNASL 107
Cdd:pfam07686   1 QTPREVTVAL-GGSVTLPCTYSSSM--SEASTSVYWYRQPPgkgpTFLIAYYSNGSEEGV-KKGRFSGRGDP-SNGDGSL 75
                          90
                  ....*....|....*
gi 767985480  108 RLQRVRVADEGSFTC 122
Cdd:pfam07686  76 TIQNLTLSDSGTYTC 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
161-233 6.04e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 44.24  E-value: 6.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767985480 161 VTITCSsYQGYPEAEVFWQ-DGQGVPLTGNVTTSQMANEQGLfdvhSILRVVLGANGTYSCLVRNPVLQQDAHS 233
Cdd:cd00096    1 VTLTCS-ASGNPPPTITWYkNGKPLPPSSRDSRRSELGNGTL----TISNVTLEDSGTYTCVASNSAGGSASAS 69
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
156-237 6.46e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 6.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   156 RPGDTVTITCsSYQGYPEAEVFW--QDGQGVPLTGNVTTSQMANEQGLFdvhsILRVVLGANGTYSCLVRNPVLQQDAHS 233
Cdd:smart00410   7 KEGESVTLSC-EASGSPPPEVTWykQGGKLLAESGRFSVSRSGSTSTLT----ISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 767985480   234 SVTI 237
Cdd:smart00410  82 TLTV 85
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
247-340 1.06e-05

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 44.49  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 247 VEVQVPEDpVVALVGTDATLRCSF-SPEPGFSLAQLNliWQLTDTKQLVHSFTEgrDQGSAYAN-------RTALFPDLL 318
Cdd:cd20989    1 VRVQVPPE-VRGFLGGSVTLPCHLlPPNMVTHVSQVT--WQRHDEHGSVAVFHP--KQGPSFPEserlsfvAARLGAELR 75
                         90       100
                 ....*....|....*....|..
gi 767985480 319 aqgNASLRLQRVRVADEGSFTC 340
Cdd:cd20989   76 ---NASLAMFGLRVEDEGNYTC 94
IgC1_PD-L2 cd20986
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ...
157-224 1.07e-05

Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients.


Pssm-ID: 409578  Cd Length: 82  Bit Score: 43.87  E-value: 1.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767985480 157 PG-DTVTITCSSyQGYPEAEVFWQDgqgVPLTGNvtTSQMANEQGLFDVHSILRVVLGANGTYSCLVRN 224
Cdd:cd20986    8 PGtGEVQLTCQA-RGYPLAEVSWQN---VSVPAN--TSHTRTPEGLYQVTSVLRLKPQPGRNFSCMFWN 70
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
31-122 1.55e-05

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 44.11  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  31 VQVPEDpVVALVGTDATLCCSF-SPEPGFSLAQLNliWQLTDTKQLVHSFAegQDQGSAYAN-------RTALFPDLLaq 102
Cdd:cd20989    3 VQVPPE-VRGFLGGSVTLPCHLlPPNMVTHVSQVT--WQRHDEHGSVAVFH--PKQGPSFPEserlsfvAARLGAELR-- 75
                         90       100
                 ....*....|....*....|
gi 767985480 103 gNASLRLQRVRVADEGSFTC 122
Cdd:cd20989   76 -NASLAMFGLRVEDEGNYTC 94
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
151-222 2.25e-05

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, and delta chains, and CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, epsilon, and mu chains; member of the C1-set of I; The members here are composed of the third and fourth immunoglobulin constant domain (IgC) of alpha, delta, gamma and alpha, epsilon, and mu heavy chains, respectively. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.


Pssm-ID: 409425  Cd Length: 105  Bit Score: 43.48  E-value: 2.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767985480 151 PNKDLRPGDTVTITCSSYQGYPEaEVF--W-QDGQGVPLTGNVTTSQMANEQGLFDVHSILRVVLGA--NG-TYSCLV 222
Cdd:cd05768    9 PEEELSLNETVTLTCLVKGFYPE-DIFvsWlQNGEPLPSADYKTTAPVPESDGSFFVYSKLNVSTADwnSGdVFSCVV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
251-353 2.92e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 42.57  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  251 VPEDPVVALVGTDATLRCSFSPEPGFslaqLNLIWQLTDtKQLVHSFTEGRDQGSayanrtalfpdllaQGNASLRLQRV 330
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPG----PDVTWSKEG-GTLIESLKVKHDNGR--------------TTQSSLLISNV 61
                          90       100
                  ....*....|....*....|...
gi 767985480  331 RVADEGSFTCFVSIRDFGSAAVS 353
Cdd:pfam00047  62 TKEDAGTYTCVVNNPGGSATLST 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
379-450 6.49e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 41.16  E-value: 6.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767985480 379 VTITCSsYRGYPEAEVFWQ-DGQGVPLTGNVTTSQMANEQGLfdvhSVLRVVLGANGTYSCLVRNPVLQQDAH 450
Cdd:cd00096    1 VTLTCS-ASGNPPPTITWYkNGKPLPPSSRDSRRSELGNGTL----TISNVTLEDSGTYTCVASNSAGGSASA 68
IgC1_CH3_IgAGD_CH4_IgAEM cd05768
CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, ...
369-440 6.63e-05

CH3 domain (third constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, gamma, and delta chains, and CH4 domain (fourth constant Ig domain of the heavy chain) in immunoglobulin heavy alpha, epsilon, and mu chains; member of the C1-set of I; The members here are composed of the third and fourth immunoglobulin constant domain (IgC) of alpha, delta, gamma and alpha, epsilon, and mu heavy chains, respectively. This domain is found on the Fc fragment. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda; each is composed of a constant domain and a variable domain. There are five types of heavy chains: alpha, delta, epsilon, gamma, and mu, all consisting of a variable domain (VH) with three (alpha, delta and gamma) or four (epsilon and mu) constant domains (CH1 to CH4). Ig molecules are modular proteins, in which the variable and constant domains have clear, conserved sequence patterns.


Pssm-ID: 409425  Cd Length: 105  Bit Score: 41.94  E-value: 6.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767985480 369 PNKDLRPGDTVTITCSSYRGYPEaEVF--W-QDGQGVPLTGNVTTSQMANEQGLFDVHSVLRVVLGA--NG-TYSCLV 440
Cdd:cd05768    9 PEEELSLNETVTLTCLVKGFYPE-DIFvsWlQNGEPLPSADYKTTAPVPESDGSFFVYSKLNVSTADwnSGdVFSCVV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
374-456 8.80e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 41.34  E-value: 8.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   374 RPGDTVTITCsSYRGYPEAEVFW--QDGQGVPLTGNVTTSQMANEQGLFdvhsVLRVVLGANGTYSCLVRNPVlqQDAHG 451
Cdd:smart00410   7 KEGESVTLSC-EASGSPPPEVTWykQGGKLLAESGRFSVSRSGSTSTLT----ISNVTPEDSGTYTCAATNSS--GSASS 79

                   ....*
gi 767985480   452 SVTIT 456
Cdd:smart00410  80 GTTLT 84
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
372-447 9.71e-05

Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other strands by G, F, C, and C'.


Pssm-ID: 409354  Cd Length: 95  Bit Score: 41.29  E-value: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 372 DLRPGDTVTITCSSYRGYPE-AEVFW-QDGQGVPlTGNVTTSQMANEQGLFDVHSVLRVVLG---ANGTYSCLVRNPVLQ 446
Cdd:cd00098   10 EEKGGGKVTLVCLVSGFYPKdITVTWlKNGVPLT-SGVSTSSPVEPNDGTYSVTSSLTVPPSdwdEGATYTCVVTHESLK 88

                 .
gi 767985480 447 Q 447
Cdd:cd00098   89 S 89
IGv smart00406
Immunoglobulin V-Type;
263-342 1.33e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 40.44  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   263 DATLRCSFSpepGFSLAQLNLIWQ-LTDTKQLVHsFTEGRDQGSAYA-----NRTALFPDLlAQGNASLRLQRVRVADEG 336
Cdd:smart00406   1 SVTLSCKFS---GSTFSSYYVSWVrQPPGKGLEW-LGYIGSNGSSYYqesykGRFTISKDT-SKNDVSLTISNLRVEDTG 75

                   ....*.
gi 767985480   337 SFTCFV 342
Cdd:smart00406  76 TYYCAV 81
IGv smart00406
Immunoglobulin V-Type;
45-124 2.12e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 40.06  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480    45 DATLCCSFSpepGFSLAQLNLIWQ-LTDTKQLVHsFAEGQDQGSAYA-----NRTALFPDLlAQGNASLRLQRVRVADEG 118
Cdd:smart00406   1 SVTLSCKFS---GSTFSSYYVSWVrQPPGKGLEW-LGYIGSNGSSYYqesykGRFTISKDT-SKNDVSLTISNLRVEDTG 75

                   ....*.
gi 767985480   119 SFTCFV 124
Cdd:smart00406  76 TYYCAV 81
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
144-226 2.33e-04

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 40.07  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 144 KPSMTLEPNKDLRPGDTVTITCSSYQgyPEAEVFW-QDGQGVPLTGNVTTSQmANEQglfdvHSILRVVLGANGTYSCLV 222
Cdd:cd05740    1 KPFISSNNSNPVEDKDAVTLTCEPET--QNTSYLWwFNGQSLPVTPRLTLSN-GNRT-----LTLLNVTREDAGAYQCEI 72

                 ....
gi 767985480 223 RNPV 226
Cdd:cd05740   73 SNPV 76
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
376-456 3.22e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 39.86  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 376 GDTVTITCSsYRGYPEAEVFWQ-DGQGVPLTGNvttsQMANEQGLFDVHSVLRVVlgANGTYSCLVRNPVlQQDAHGSVT 454
Cdd:cd20958   15 GQTLRLHCP-VAGYPISSITWEkDGRRLPLNHR----QRVFPNGTLVIENVQRSS--DEGEYTCTARNQQ-GQSASRSVF 86

                 ..
gi 767985480 455 IT 456
Cdd:cd20958   87 VK 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
255-356 4.60e-04

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.03  E-value: 4.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   255 PVVALVGTDATLRCSFSpepGFSLAQLNLIWQltdtkQLVHSFTEGRDQGSAYANrtalfpdllaqgNASLRLQRVRVAD 334
Cdd:smart00410   3 SVTVKEGESVTLSCEAS---GSPPPEVTWYKQ-----GGKLLAESGRFSVSRSGS------------TSTLTISNVTPED 62
                           90       100
                   ....*....|....*....|...
gi 767985480   335 EGSFTCFVSIRDF-GSAAVSLQV 356
Cdd:smart00410  63 SGTYTCAATNSSGsASSGTTLTV 85
I-set pfam07679
Immunoglobulin I-set domain;
145-237 4.71e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.16  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  145 PSMTLEP-NKDLRPGDTVTITCSSyQGYPEAEVFWQ-DGQGVPLTGNVTTSQMANEQGLFdvhsILRVVLGANGTYSCLV 222
Cdd:pfam07679   1 PKFTQKPkDVEVQEGESARFTCTV-TGTPDPEVSWFkDGQPLRSSDRFKVTYEGGTYTLT----ISNVQPDDSGKYTCVA 75
                          90
                  ....*....|....*
gi 767985480  223 RNPVLQQDAHSSVTI 237
Cdd:pfam07679  76 TNSAGEAEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
264-354 5.31e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 38.46  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 264 ATLRCSFSPEPgfslaQLNLIWQLTDTKQLVHSFTEGRDQgsayanrtalfpdllaQGNASLRLQRVRVADEGSFTCFVS 343
Cdd:cd00096    1 VTLTCSASGNP-----PPTITWYKNGKPLPPSSRDSRRSE----------------LGNGTLTISNVTLEDSGTYTCVAS 59
                         90
                 ....*....|.
gi 767985480 344 IRDFGSAAVSL 354
Cdd:cd00096   60 NSAGGSASASV 70
IgC1_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of ...
144-229 5.86e-04

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II beta chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes and they are also expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain has two globular domains (N- and C-terminal) and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.


Pssm-ID: 409423  Cd Length: 96  Bit Score: 39.24  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 144 KPSMTLEPNKDLRPGDTVTITCSSYQGYP-EAEVFW-QDGQGVPlTGNVTTSQMANEQGLFDVHSILRVVLGANGTYSCL 221
Cdd:cd05766    3 QPSVKVSPTKTGPLEHPNLLVCSVTGFYPaEIEVKWfRNGQEET-AGVVSTELIPNGDWTFQILVMLETTPRRGDVYTCQ 81

                 ....*...
gi 767985480 222 VRNPVLQQ 229
Cdd:cd05766   82 VEHSSLQS 89
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
362-444 6.89e-04

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 38.91  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 362 KPSMTLEPNKDLRPGDTVTITCSSYRgyPEAEVFW-QDGQGVPLTGNVTTSQmANEQglfdvHSVLRVVLGANGTYSCLV 440
Cdd:cd05740    1 KPFISSNNSNPVEDKDAVTLTCEPET--QNTSYLWwFNGQSLPVTPRLTLSN-GNRT-----LTLLNVTREDAGAYQCEI 72

                 ....
gi 767985480 441 RNPV 444
Cdd:cd05740   73 SNPV 76
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
145-238 6.90e-04

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 39.01  E-value: 6.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 145 PSMTLEPNKDLRPGD--TVTITCSSYQGYPEAEVFWqDGQgvpLTGNVTTSQMANEQGLFDVHSILRVVLG--ANG-TYS 219
Cdd:cd05719    1 PTNSLEGGPALLIGGepTLVATCISANGKPPASVTW-ETD---LKGEASTTQVRGSNGTVTVTSRYRLVPSreADGqPLT 76
                         90
                 ....*....|....*....
gi 767985480 220 CLVRNPVLQQDAHSSVTIT 238
Cdd:cd05719   77 CVVEHPSLEKDQRISVTLN 95
C1-set pfam07654
Immunoglobulin C1-set domain;
158-227 7.08e-04

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 38.77  E-value: 7.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767985480  158 GDTVTITCSSYQGYPEA-EVFW-QDGQgvPLTGNVTTSQ-MANEQGLFDVHSILRVVLGANG---TYSCLVRNPVL 227
Cdd:pfam07654  12 GKPNTLTCLVTGFYPPDiTVTWlKNGQ--EVTEGVKTTPpSPNSDWTYQLSSYLTVTPSDWEsgdEYTCRVEHEGL 85
IgC1_MHC_II_beta cd05766
Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of ...
362-447 7.86e-04

Class II major histocompatibility complex (MHC) beta chain immunoglobulin domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class II beta chain. MHC class II molecules play a key role in the initiation of the antigen-specific immune reponse. These molecules have been shown to be expressed constitutively on the cell surface of professional antigen-presenting cells (APCs), including B-lymphocytes, monocytes, and macrophages in both humans and mice. The expression of these molecules has been shown to be induced in nonprofessional APCs such as keratinocyctes and they are also expressed on the surface of activated human T cells and on T cells from other species. The MHC II molecules present antigenic peptides to CD4(+) T-lymphocytes. These peptides derive mostly from proteolytic processing via the endocytic pathway of antigens internalized by the APC. These peptides bind to the MHC class II molecules in the endosome before they are transported to the cell surface. MHC class II molecules are heterodimers, comprised of two similarly-sized membrane-spanning chains, alpha and beta. Each chain has two globular domains (N- and C-terminal) and a membrane-anchoring transmembrane segment. The two chains form a compact four-domain structure. The peptide-binding site is a cleft in the structure.


Pssm-ID: 409423  Cd Length: 96  Bit Score: 38.85  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 362 KPSMTLEPNKDLRPGDTVTITCSSYRGYP-EAEVFW-QDGQGVPlTGNVTTSQMANEQGLFDVHSVLRVVLGANGTYSCL 439
Cdd:cd05766    3 QPSVKVSPTKTGPLEHPNLLVCSVTGFYPaEIEVKWfRNGQEET-AGVVSTELIPNGDWTFQILVMLETTPRRGDVYTCQ 81

                 ....*...
gi 767985480 440 VRNPVLQQ 447
Cdd:cd05766   82 VEHSSLQS 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
248-343 8.36e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.32  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  248 EVQVPEDPVVALVGTDATLRC--SFSPEPgfslaqlNLIWQLtDTKQLVHSFTEGRDQGSayanrtalfpdllaqGNASL 325
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCeaTGSPPP-------TITWYK-NGEPISSGSTRSRSLSG---------------SNSTL 59
                          90
                  ....*....|....*...
gi 767985480  326 RLQRVRVADEGSFTCFVS 343
Cdd:pfam13927  60 TISNVTRSDAGTYTCVAS 77
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
154-229 8.81e-04

Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, classical Ig-like domains resembling the antibody constant domain. Members of the IgC1 family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and major histocompatibility complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, while the IgC domain is involved in oligomerization and molecular interactions. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other strands by G, F, C, and C'.


Pssm-ID: 409354  Cd Length: 95  Bit Score: 38.59  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 154 DLRPGDTVTITCSSYQGYPE-AEVFW-QDGQGVPlTGNVTTSQMANEQGLFDVHSILRVVLG---ANGTYSCLVRNPVLQ 228
Cdd:cd00098   10 EEKGGGKVTLVCLVSGFYPKdITVTWlKNGVPLT-SGVSTSSPVEPNDGTYSVTSSLTVPPSdwdEGATYTCVVTHESLK 88

                 .
gi 767985480 229 Q 229
Cdd:cd00098   89 S 89
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
29-124 1.32e-03

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 38.56  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  29 LEVQVPEDpVVALVGTDATLCCSF-SPEPGFSLAQLNLIWQLTDTKQLVHSFAegQDQGSAYANRTALFPDL------LA 101
Cdd:cd05715    1 MEVYTPRE-LNVLNGSDVRLTCTFtSCYTVGDAFSVTWTYQPEGGNTTESMFH--YSKGKPYILKVGRFKDRvswagnPS 77
                         90       100
                 ....*....|....*....|...
gi 767985480 102 QGNASLRLQRVRVADEGSFTCFV 124
Cdd:cd05715   78 KKDASIVISNLQFSDNGTYTCDV 100
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
152-226 1.40e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 37.87  E-value: 1.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767985480 152 NKDLRPGDTVTITCSSYqGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLfdvhSILRVVLGANGTYSCLVRNPV 226
Cdd:cd20970   11 TVTAREGENATFMCRAE-GSPEPEISWTRNGNLIIEFNTRYIVRENGTTL----TIRNIRRSDMGIYLCIASNGV 80
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
363-456 1.41e-03

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 38.24  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 363 PSMTLEPNKDLRPGD--TVTITCSSYRGYPEAEVFWqDGQgvpLTGNVTTSQMANEQGLFDVHSVLRVVLG--ANG-TYS 437
Cdd:cd05719    1 PTNSLEGGPALLIGGepTLVATCISANGKPPASVTW-ETD---LKGEASTTQVRGSNGTVTVTSRYRLVPSreADGqPLT 76
                         90
                 ....*....|....*....
gi 767985480 438 CLVRNPVLQQDAHGSVTIT 456
Cdd:cd05719   77 CVVEHPSLEKDQRISVTLN 95
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
247-342 1.43e-03

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 38.56  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 247 VEVQVPEDpVVALVGTDATLRCSF-SPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRdqGSAYANRTALFPDL------LA 319
Cdd:cd05715    1 MEVYTPRE-LNVLNGSDVRLTCTFtSCYTVGDAFSVTWTYQPEGGNTTESMFHYSK--GKPYILKVGRFKDRvswagnPS 77
                         90       100
                 ....*....|....*....|...
gi 767985480 320 QGNASLRLQRVRVADEGSFTCFV 342
Cdd:cd05715   78 KKDASIVISNLQFSDNGTYTCDV 100
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
33-135 1.61e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 37.56  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   33 VPEDPVVALVGTDATLCCSFSPEPGFslaqLNLIWQLTDtKQLVHSFAEGQDQGSayanrtalfpdllaQGNASLRLQRV 112
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPG----PDVTWSKEG-GTLIESLKVKHDNGR--------------TTQSSLLISNV 61
                          90       100
                  ....*....|....*....|...
gi 767985480  113 RVADEGSFTCFVSIRDFGSAAVS 135
Cdd:pfam00047  62 TKEDAGTYTCVVNNPGGSATLST 84
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
30-125 1.63e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.55  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480   30 EVQVPEDPVVALVGTDATLCC--SFSPEPgfslaqlNLIWQLTDTKQLVHSFAEGQDQGsayanrtalfpdllaqGNASL 107
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCeaTGSPPP-------TITWYKNGEPISSGSTRSRSLSG----------------SNSTL 59
                          90
                  ....*....|....*...
gi 767985480  108 RLQRVRVADEGSFTCFVS 125
Cdd:pfam13927  60 TISNVTRSDAGTYTCVAS 77
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
36-138 1.88e-03

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain


Pssm-ID: 409471  Cd Length: 108  Bit Score: 37.96  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  36 DPVVALVGTDATLCCSFSPEPGFSLAQlnLIWQLTDTKQ------LVHsFAEGQDQGSAYANRTAlFPDLLAQGNASLRL 109
Cdd:cd05888    1 DVVTVVLGQDAKLPCFYRGDSGEQVGQ--VAWARVDAGEgaqeiaLLH-SKYGLHVFPAYEGRVE-QPPPPRPADGSVLL 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767985480 110 QRVRVADEGSFTCFVSIRDFGS--AAVSLQV 138
Cdd:cd05888   77 RNAVQADEGEYECRVSTFPAGNfqAELRLRV 107
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
158-238 2.19e-03

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 37.16  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 158 GDTVTITCSsYQGYPEAEVFWQ-DGQGVPLTGNvttsQMANEQGLFDVHSILRVVlgANGTYSCLVRNPVlQQDAHSSVT 236
Cdd:cd20958   15 GQTLRLHCP-VAGYPISSITWEkDGRRLPLNHR----QRVFPNGTLVIENVQRSS--DEGEYTCTARNQQ-GQSASRSVF 86

                 ..
gi 767985480 237 IT 238
Cdd:cd20958   87 VK 88
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
249-340 2.22e-03

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 409469  Cd Length: 113  Bit Score: 38.02  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 249 VQVpEDPVVALVGTDATLRCSF-SPEPGFSLAQLNliWQ--LTDTKQLVHSFTE--GRDQGSAYANRTALFPDLLAQGna 323
Cdd:cd05886    3 VQV-NDSMSGFIGTDVVLHCSFaNPLPSVKITQVT--WQksTNGSKQNVAIYNPsmGVSVLPPYRERVTFLNPSFTDG-- 77
                         90
                 ....*....|....*..
gi 767985480 324 SLRLQRVRVADEGSFTC 340
Cdd:cd05886   78 TIRLSRLELEDEGVYIC 94
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
144-238 2.45e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 36.99  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  144 KPSMTLEPnKDLRPGDTVTITCSSYqGYPEAEVFWQdGQGVPLTGNvttsqmaneQGLFdvhsILRVVLGANGTYSCLVR 223
Cdd:pfam13895   1 KPVLTPSP-TVVTEGEPVTLTCSAP-GNPPPSYTWY-KDGSAISSS---------PNFF----TLSVSAEDSGTYTCVAR 64
                          90
                  ....*....|....*
gi 767985480  224 NPVLQQDAhSSVTIT 238
Cdd:pfam13895  65 NGRGGKVS-NPVELT 78
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
370-444 2.76e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 37.10  E-value: 2.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767985480 370 NKDLRPGDTVTITCSSYrGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLfdvhSVLRVVLGANGTYSCLVRNPV 444
Cdd:cd20970   11 TVTAREGENATFMCRAE-GSPEPEISWTRNGNLIIEFNTRYIVRENGTTL----TIRNIRRSDMGIYLCIASNGV 80
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
363-448 4.30e-03

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


Pssm-ID: 409501  Cd Length: 96  Bit Score: 36.72  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 363 PSMTLEPNKDLRP---GDTVTITCSSYRGYPEAEVFWQDGQGvplTGNVTTSQMANEQGLFDVHSVLRVVLGANG-TYSC 438
Cdd:cd07704    1 PLVSLNPGPALLIdggNETLAASCTAETGKPAASVTWETDLG---GMESSRTFEHNRTATVTSEYHLVPTRFANGrPLTC 77
                         90
                 ....*....|
gi 767985480 439 LVRNPVLQQD 448
Cdd:cd07704   78 VVSHPALQQD 87
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
362-456 4.45e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 36.22  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  362 KPSMTLEPnKDLRPGDTVTITCSSYrGYPEAEVFWQdGQGVPLTGNvttsqmaneQGLFdvhsVLRVVLGANGTYSCLVR 441
Cdd:pfam13895   1 KPVLTPSP-TVVTEGEPVTLTCSAP-GNPPPSYTWY-KDGSAISSS---------PNFF----TLSVSAEDSGTYTCVAR 64
                          90
                  ....*....|....*
gi 767985480  442 NPVLQQDAHgSVTIT 456
Cdd:pfam13895  65 NGRGGKVSN-PVELT 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
46-136 4.66e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 35.77  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  46 ATLCCSFSPEPgfslaQLNLIWQLtDTKQLVHSfaegqdqgsayanrtALFPDLLAQGNASLRLQRVRVADEGSFTCFVS 125
Cdd:cd00096    1 VTLTCSASGNP-----PPTITWYK-NGKPLPPS---------------SRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
                         90
                 ....*....|.
gi 767985480 126 IRDFGSAAVSL 136
Cdd:cd00096   60 NSAGGSASASV 70
IGc1 smart00407
Immunoglobulin C-Type;
160-229 4.82e-03

Immunoglobulin C-Type;


Pssm-ID: 214651  Cd Length: 75  Bit Score: 36.14  E-value: 4.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767985480   160 TVTITCSSYQGYP-EAEVFWQ-DGQGVPLtGNVTTSQMANEQGLFDVHSILRV---VLGANGTYSCLVRNPVLQQ 229
Cdd:smart00407   1 KATLVCLVSGFYPpDITVTWLrNGQEVTE-GVSTTDPLKNSDGTYFLSSYLTVpasTWESGDVYTCQVTHEGLKE 74
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
145-230 5.23e-03

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


Pssm-ID: 409501  Cd Length: 96  Bit Score: 36.34  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 145 PSMTLEPNKDLRP---GDTVTITCSSYQGYPEAEVFWQDGQGvplTGNVTTSQMANEQGLFDVHSILRVVLGANG-TYSC 220
Cdd:cd07704    1 PLVSLNPGPALLIdggNETLAASCTAETGKPAASVTWETDLG---GMESSRTFEHNRTATVTSEYHLVPTRFANGrPLTC 77
                         90
                 ....*....|
gi 767985480 221 LVRNPVLQQD 230
Cdd:cd07704   78 VVSHPALQQD 87
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
46-131 5.89e-03

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 80). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as cluster of differentiation 152/CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. CD80 contains two Ig-like domains, an amino-terminal immunoglobulin variable (IgV)-like domain characteristic of adhesion molecules and a membrane proximal immunoglobulin constant (IgC)-like domain similar to the constant domains of antigen receptors. Members of the Ig family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and Major Histocompatibility Complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 319335  Cd Length: 105  Bit Score: 36.66  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480  46 ATLCC--SFSPEpgfSLAQLNLIWQLTDtkQLVHSFAEGQ-DQGSAYANRTalFPDLLaqGNASLRLQRVRVADEGSFTC 122
Cdd:cd16086   12 ALLSCdyNVSVD---ELAQVRIYWQKDD--KMVLTIISGDvKVWPEYKNRT--LFDIT--NNLSIVILALRLSDRGTYTC 82

                 ....*....
gi 767985480 123 FVSIRDFGS 131
Cdd:cd16086   83 VVQKKERGA 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
37-138 6.86e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 35.94  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480    37 PVVALVGTDATLCCSFSPEPgfslaQLNLIWQLTDTKQLVHSfaegqdqgsayaNRTALFPDllaQGNASLRLQRVRVAD 116
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSP-----PPEVTWYKQGGKLLAES------------GRFSVSRS---GSTSTLTISNVTPED 62
                           90       100
                   ....*....|....*....|...
gi 767985480   117 EGSFTCFVSIRDF-GSAAVSLQV 138
Cdd:smart00410  63 SGTYTCAATNSSGsASSGTTLTV 85
IgV_PD-L2 cd20983
Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here ...
249-342 8.70e-03

Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). Receptor-binding domain of PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients.


Pssm-ID: 409575  Cd Length: 100  Bit Score: 36.01  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985480 249 VQVPEDPVVALVGTDATLRCSFSPEpgfslaqlnliwQLTDTKQLVHSFTEGRDQGSAYANRTALFPDLLAQGNASLRLQ 328
Cdd:cd20983    4 VTVPKELYTVDHGSNVTLECDFDTG------------EHVELGAIRASLQKVENDTSLHSERATLLEEQLPLGKALFHIP 71
                         90
                 ....*....|....
gi 767985480 329 RVRVADEGSFTCFV 342
Cdd:cd20983   72 SVQVRDAGQYRCLI 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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