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Conserved domains on  [gi|1370488842|ref|XP_024301788|]
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hepatitis A virus cellular receptor 1 isoform X1 [Homo sapiens]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 34076)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 22-124 1.27e-40

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.


The actual alignment was detected with superfamily member cd20982:

Pssm-ID: 472250  Cd Length: 107  Bit Score: 139.52  E-value: 1.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  22 VKVGGEAGPSVTLPCHYS----GAVTSMCWNRGSCSLFTCQNGIVWTNGTHVTYRKDTRYKLLGDLSRRDVSLTIENTAV 97
Cdd:cd20982     1 VEYRAEVGHNAYLPCSYTtaapGNLVPVCWGKGACPVSYCGNVLLRTDERDVTYQKSSRYQLKGDFSKGDVSLTIENVTL 80

                          90       100
                  ....*....|....*....|....*..
gi 1370488842  98 SDSGVYCCRVEHRGWFNDMKITVSLEI 124
Cdd:cd20982    81 ADSGIYCCRIQIPGIMNDEKFNLKLVI 107
 
Name Accession Description Interval E-value
IgV_TIM-3_like cd20982
Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3) ...
 22-124 1.27e-40

Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and similar domains; The members here are composed of the immunoglobulin variable (IgV) domain of T cell immunoglobulin domain and mucin domain 3 (Tim-3; also known as Hepatitis A virus cellular receptor 2 (HAVcr-2) and Cluster of Differentiation 366 (CD366)) and similar proteins. TIM-3 is a checkpoint inhibitor in immune responses to tumors, as well as involved in chronic viral infections. Thus, Tim-3 has emerged as one of most promising immune checkpoint targets for cancer immunotherapy. Tim-3 is highly expressed on Th1 lymphocytes and CD11b(+) macrophages and is upregulated on activated T and myeloid cells. TIM-3 regulates macrophage, activation and inhibits Th1 mediated immune responses to promote immunological tolerance. There are three TIM family members in humans (TIM-1, TIM-3, and TIM-4) and eight members in mice (TIM-1 to TIM-8). The IgV domain of human TIM-3 has been shown to bind ligands such as carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1), high mobility group protein B1 (HMGB1)and galectin-9 (GAL9). The binding of GAL9 to TIM-3 can negatively regulate Th1 immune response, enhance immune tolerance and inhibit anti#tumor immunity. Dysregulation of the TIM-3/GAL9 pathway is implicated in numerous chronic autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus.


Pssm-ID: 409574  Cd Length: 107  Bit Score: 139.52  E-value: 1.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  22 VKVGGEAGPSVTLPCHYS----GAVTSMCWNRGSCSLFTCQNGIVWTNGTHVTYRKDTRYKLLGDLSRRDVSLTIENTAV 97
Cdd:cd20982     1 VEYRAEVGHNAYLPCSYTtaapGNLVPVCWGKGACPVSYCGNVLLRTDERDVTYQKSSRYQLKGDFSKGDVSLTIENVTL 80

                          90       100
                  ....*....|....*....|....*..
gi 1370488842  98 SDSGVYCCRVEHRGWFNDMKITVSLEI 124
Cdd:cd20982    81 ADSGIYCCRIQIPGIMNDEKFNLKLVI 107
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 21-120 4.34e-12

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: 62.48  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  21 SVKVGGeagpSVTLPCHYS----GAVTSMCWNRGSCSLFTCQNGIVWTNGTHVTYRKDtRYKLLGDLSRRDVSLTIENTA 96
Cdd:pfam07686   7 TVALGG----SVTLPCTYSssmsEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKG-RFSGRGDPSNGDGSLTIQNLT 81

                          90       100
                  ....*....|....*....|....*..
gi 1370488842  97 VSDSGVYCCRV---EHRGWFNDMKITV 120
Cdd:pfam07686  82 LSDSGTYTCAVipsGEGVFGKGTRLTV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 21-108 9.48e-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: 43.65  E-value: 9.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842   21 SVKVGGeagpSVTLPCHYSGAVTSMCWnrgscslftcqngivWTNGTHVTYRKDTRYKLLGDLSrrDVSLTIENTAVSDS 100
Cdd:smart00410   5 TVKEGE----SVTLSCEASGSPPPEVT---------------WYKQGGKLLAESGRFSVSRSGS--TSTLTISNVTPEDS 63


                   ....*...
gi 1370488842  101 GVYCCRVE 108
Cdd:smart00410  64 GTYTCAAT 71
 
Name Accession Description Interval E-value
IgV_TIM-3_like cd20982
Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3) ...
 22-124 1.27e-40

Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and similar domains; The members here are composed of the immunoglobulin variable (IgV) domain of T cell immunoglobulin domain and mucin domain 3 (Tim-3; also known as Hepatitis A virus cellular receptor 2 (HAVcr-2) and Cluster of Differentiation 366 (CD366)) and similar proteins. TIM-3 is a checkpoint inhibitor in immune responses to tumors, as well as involved in chronic viral infections. Thus, Tim-3 has emerged as one of most promising immune checkpoint targets for cancer immunotherapy. Tim-3 is highly expressed on Th1 lymphocytes and CD11b(+) macrophages and is upregulated on activated T and myeloid cells. TIM-3 regulates macrophage, activation and inhibits Th1 mediated immune responses to promote immunological tolerance. There are three TIM family members in humans (TIM-1, TIM-3, and TIM-4) and eight members in mice (TIM-1 to TIM-8). The IgV domain of human TIM-3 has been shown to bind ligands such as carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1), high mobility group protein B1 (HMGB1)and galectin-9 (GAL9). The binding of GAL9 to TIM-3 can negatively regulate Th1 immune response, enhance immune tolerance and inhibit anti#tumor immunity. Dysregulation of the TIM-3/GAL9 pathway is implicated in numerous chronic autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus.


Pssm-ID: 409574  Cd Length: 107  Bit Score: 139.52  E-value: 1.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  22 VKVGGEAGPSVTLPCHYS----GAVTSMCWNRGSCSLFTCQNGIVWTNGTHVTYRKDTRYKLLGDLSRRDVSLTIENTAV 97
Cdd:cd20982     1 VEYRAEVGHNAYLPCSYTtaapGNLVPVCWGKGACPVSYCGNVLLRTDERDVTYQKSSRYQLKGDFSKGDVSLTIENVTL 80

                          90       100
                  ....*....|....*....|....*..
gi 1370488842  98 SDSGVYCCRVEHRGWFNDMKITVSLEI 124
Cdd:cd20982    81 ADSGIYCCRIQIPGIMNDEKFNLKLVI 107
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 21-120 4.34e-12

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: 62.48  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  21 SVKVGGeagpSVTLPCHYS----GAVTSMCWNRGSCSLFTCQNGIVWTNGTHVTYRKDtRYKLLGDLSRRDVSLTIENTA 96
Cdd:pfam07686   7 TVALGG----SVTLPCTYSssmsEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKG-RFSGRGDPSNGDGSLTIQNLT 81

                          90       100
                  ....*....|....*....|....*..
gi 1370488842  97 VSDSGVYCCRV---EHRGWFNDMKITV 120
Cdd:pfam07686  82 LSDSGTYTCAVipsGEGVFGKGTRLTV 108
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 23-123 1.25e-06

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 46.62  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  23 KVGGEAGPSVTLPCHYSGAVTS----MC-WNRGSCSLFTCQNGivwtngthvtYRKDTRYKLLGDLSRRDVSLTIENTAV 97
Cdd:cd05716     6 VVTGVEGGSVTIQCPYPPKYASsrkyWCkWGSEGCQTLVSSEG----------VVPGGRISLTDDPDNGVFTVTLNQLRK 75

                          90       100
                  ....*....|....*....|....*.
gi 1370488842  98 SDSGVYCCRVEHRGWFnDMKITVSLE 123
Cdd:cd05716    76 EDAGWYWCGVGDDGDR-GLTVQVKLV 100
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 21-108 9.48e-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: 43.65  E-value: 9.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842   21 SVKVGGeagpSVTLPCHYSGAVTSMCWnrgscslftcqngivWTNGTHVTYRKDTRYKLLGDLSrrDVSLTIENTAVSDS 100
Cdd:smart00410   5 TVKEGE----SVTLSCEASGSPPPEVT---------------WYKQGGKLLAESGRFSVSRSGS--TSTLTISNVTPEDS 63


                   ....*...
gi 1370488842  101 GVYCCRVE 108
Cdd:smart00410  64 GTYTCAAT 71
IGv smart00406
Immunoglobulin V-Type;
31-105 1.83e-05

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 42.75  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842   31 SVTLPCHYSG---AVTSMCWNRgscslftcQ---NGIVW--------TNGTHVTYRkdTRYKLLGDLSRRDVSLTIENTA 96
Cdd:smart00406   1 SVTLSCKFSGstfSSYYVSWVR--------QppgKGLEWlgyigsngSSYYQESYK--GRFTISKDTSKNDVSLTISNLR 70


                   ....*....
gi 1370488842   97 VSDSGVYCC 105
Cdd:smart00406  71 VEDTGTYYC 79
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 22-124 5.51e-05

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 42.31  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  22 VKVGGEAGPSVTLPCHYsgavtsmcwNRGSCSLFTCQNGIVWTNgTHVTYRK--------DTRYKLLGDLSRR------- 86
Cdd:cd05877     5 AKVFSHRGGNVTLPCRY---------HYEPELSAPRKIRVKWTK-LEVDYAKeedvlvaiGTRHKSYGSYQGRvflrrad 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370488842  87 --DVSLTIENTAVSDSGVYCCRVEHRgwFNDMKITVSLEI 124
Cdd:cd05877    75 dlDASLVITDLRLEDYGRYRCEVIDG--LEDESVVVALRL 112
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 26-107 1.30e-04

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: 41.26  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  26 GEAGPSVTLPCHYS-----GAVTSMCWNRGSCSLFTCQNGIVWTNGTHVTyRKDTRYK----LLGDLSRRDVSLTIENTA 96
Cdd:cd05715    11 VLNGSDVRLTCTFTscytvGDAFSVTWTYQPEGGNTTESMFHYSKGKPYI-LKVGRFKdrvsWAGNPSKKDASIVISNLQ 89

                          90
                  ....*....|.
gi 1370488842  97 VSDSGVYCCRV 107
Cdd:cd05715    90 FSDNGTYTCDV 100
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 76-124 3.75e-04

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 40.07  E-value: 3.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370488842  76 RYKLLGDLSRRDVSLTIENTAVSDSGVYCCRVEHRGW--FNDMKITVSLEI 124
Cdd:cd05712    68 RFRLLGDPGKKNCSLSISDARPEDSGKYFFRVERGDSnkYSYLSNQLSLTV 118
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 18-124 4.17e-04

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 39.89  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  18 VAGSVKVGGEAGPSVTLPCHYS-----------------GAVTSMCWNRGSCSLFTCQNGIVWTNGthvTYRKDTRYKLL 80
Cdd:cd05714     1 EAESAKVFSHLGGNVTLPCKFYrdptafgsgihkirikwTKLTSDSGYLKEVDVLVAMGNVVYHKK---TYGGRVSVPLK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370488842  81 GDlSRRDVSLTIENTAVSDSGVYCCRVEhRGwFNDMKITVSLEI 124
Cdd:cd05714    78 PG-SDSDASLVITDLTASDYGLYRCEVI-EG-IEDDQDVVALDV 118
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 23-107 7.62e-04

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: 38.97  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  23 KVGGEAGPSVTLPCHYSGA----VTSMCW------NRGSCSLFTCQNGIVWTNgthvTYRKDTRYkLLGDLSRRDVSLTI 92
Cdd:cd05718     8 EVTGFLGGSVTLPCSLTSPgttkITQVTWmkigagSSQNVAVFHPQYGPSVPN----PYAERVEF-LAARLGLRNATLRI 82

                          90
                  ....*....|....*
gi 1370488842  93 ENTAVSDSGVYCCRV 107
Cdd:cd05718    83 RNLRVEDEGNYICEF 97
IgV_1_CD4 cd07690
First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of ...
 24-124 2.31e-03

First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of IgSF domains; The members here are composed of the first immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4. CD4 and CD8 are the two primary co-receptor proteins found on the surface of T cells, and the presence of either CD4 or CD8 determines the function of the T cell. CD4 is found on helper T cells, where it is required for the binding of MHC (major histocompatibility complex) class II molecules, while CD8 is found on cytotoxic T cells, where it is required for the binding of MHC class I molecules. CD4 contains four immunoglobulin domains, with the first three included in this hierarchy. The fourth domain has a general Ig architecture, but has slight topological changes in the arrangement of beta strands relative to the other structures in this family and is not specifically included in the hierarchy.


Pssm-ID: 409487  Cd Length: 97  Bit Score: 37.14  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  24 VGGEAGPSVTLPCHYSGAVT-SMCWNRGSCSLFTCQNGIVWTNGTHVTY-RKDTRYKLLgdlSRRDVSLTIENTAVSDSG 101
Cdd:cd07690     4 VLGKKGDTAELPCTASQKKSiQFHWKNSNQIKILGNQGSFLTKGPSKLNdRADSRRNLW---DQGSFPLIIKNLKIEDSD 80

                          90       100
                  ....*....|....*....|...
gi 1370488842 102 VYCCRVEhrgwfnDMKITVSLEI 124
Cdd:cd07690    81 TYICEVE------DKKEEVELLV 97
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 23-105 4.17e-03

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: 36.79  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  23 KVGGEAGPSVTLPCHYSGA-----VTSMCWNR----GSCSLFTCQNGIVWTNGTHVTYrkdTRYKLLGDLsrRDVSLTIE 93
Cdd:cd20989     8 EVRGFLGGSVTLPCHLLPPnmvthVSQVTWQRhdehGSVAVFHPKQGPSFPESERLSF---VAARLGAEL--RNASLAMF 82

                          90
                  ....*....|..
gi 1370488842  94 NTAVSDSGVYCC 105
Cdd:cd20989    83 GLRVEDEGNYTC 94
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 32-109 7.07e-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: 35.00  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370488842  32 VTLPCHYSGavtsmcwnrgscslftcqngivwTNGTHVTYRKDTRYKLLGDLSRRDV-----SLTIENTAVSDSGVYCCR 106
Cdd:cd00096     1 VTLTCSASG-----------------------NPPPTITWYKNGKPLPPSSRDSRRSelgngTLTISNVTLEDSGTYTCV 57


                  ...
gi 1370488842 107 VEH 109
Cdd:cd00096    58 ASN 60
 
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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