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Conserved domains on  [gi|112789532|ref|NP_001036189|]
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nectin-2 isoform delta precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 34-158 4.90e-64

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: 204.35  E-value: 4.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDapaNHQNVAAFHPKMGPSFPSPkpgsERLSFVSAKQstg 113
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHD---EHGSVAVFHPKQGPSFPES----ERLSFVAARL--- 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112789532 114 qdtEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd20989   71 ---GAELRNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 261-346 2.31e-56

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


:

Pssm-ID: 409524  Cd Length: 86  Bit Score: 183.15  E-value: 2.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 261 PEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRA 340
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 112789532 341 EQVIFV 346
Cdd:cd20930   81 EQTIFV 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 162-258 6.76e-50

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) 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: 409500  Cd Length: 97  Bit Score: 166.42  E-value: 6.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 162 PKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVE 241
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 112789532 242 HESFEEPALIPVTLSVR 258
Cdd:cd07703   81 HETLEEPQLLPVTLSVR 97
 
Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 34-158 4.90e-64

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: 204.35  E-value: 4.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDapaNHQNVAAFHPKMGPSFPSPkpgsERLSFVSAKQstg 113
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHD---EHGSVAVFHPKQGPSFPES----ERLSFVAARL--- 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112789532 114 qdtEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd20989   71 ---GAELRNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 261-346 2.31e-56

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 183.15  E-value: 2.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 261 PEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRA 340
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 112789532 341 EQVIFV 346
Cdd:cd20930   81 EQTIFV 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 162-258 6.76e-50

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) 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: 409500  Cd Length: 97  Bit Score: 166.42  E-value: 6.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 162 PKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVE 241
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 112789532 242 HESFEEPALIPVTLSVR 258
Cdd:cd07703   81 HETLEEPQLLPVTLSVR 97
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 175-249 2.13e-15

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 71.68  E-value: 2.13e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112789532  175 QDPTTVALCISKEGRPPARISWLSSLD--WEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPA 249
Cdd:pfam08205  13 EGPEVVATCSSAGGKPAPRITWYLDGKplEAAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSYGALRGSI 89
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 37-158 5.82e-10

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: 56.70  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532   37 QVLPEVRGQLGGTVELPCHLLPPVPGlYISLVTWQR-PDAPANHQNVAAFHPKMGPSFPSPKpgserlsfVSAKQSTGQd 115
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSE-ASTSVYWYRqPPGKGPTFLIAYYSNGSEEGVKKGR--------FSGRGDPSN- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 112789532  116 teaelQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:pfam07686  71 -----GDGSLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
49-142 7.21e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 49.69  E-value: 7.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532    49 TVELPCHLLPPVPGLYIslVTWQRpDAPANHQNVAAFHPKMGPSFPSPKPgSERLSFVSAKQSTgqdteaelqDATLALH 128
Cdd:smart00406   1 SVTLSCKFSGSTFSSYY--VSWVR-QPPGKGLEWLGYIGSNGSSYYQESY-KGRFTISKDTSKN---------DVSLTIS 67

                           90
                   ....*....|....
gi 112789532   129 GLTVEDEGNYTCEF 142
Cdd:smart00406  68 NLRVEDTGTYYCAV 81
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 260-333 1.79e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.16  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  260 PPEVSISGYDDNWYLGRTdATLSCDVRSNPEPTgYDWS------TTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTN 333
Cdd:pfam13927   1 KPVITVSPSSVTVREGET-VTLTCEATGSPPPT-ITWYkngepiSSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
 
Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 34-158 4.90e-64

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: 204.35  E-value: 4.90e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDapaNHQNVAAFHPKMGPSFPSPkpgsERLSFVSAKQstg 113
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHD---EHGSVAVFHPKQGPSFPES----ERLSFVAARL--- 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112789532 114 qdtEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd20989   71 ---GAELRNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 261-346 2.31e-56

Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here are composed of the third immunoglobulin domain of Nectin-like Protein-5 (also known as Cluster of Differentiation 155 (CD155)). Nectin-like Protein-5 mediates NK (Natural Killer) cell adhesion and triggers NK cell effector functions. CD155 binds two different NK cell receptors: CD96 and CD226. These interactions accumulate at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. CD155 may also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Moreover, CD155 plays a role in mediating tumor cell invasion and migration.


Pssm-ID: 409524  Cd Length: 86  Bit Score: 183.15  E-value: 2.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 261 PEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRA 340
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 112789532 341 EQVIFV 346
Cdd:cd20930   81 EQTIFV 86
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 34-158 1.66e-52

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: 174.17  E-value: 1.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPgLYISLVTWQRPDApANHQNVAAFHPKMGPSFPSPKpgSERLSFVSAKQstg 113
Cdd:cd05718    1 QRVQVPTEVTGFLGGSVTLPCSLTSPGT-TKITQVTWMKIGA-GSSQNVAVFHPQYGPSVPNPY--AERVEFLAARL--- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 112789532 114 qdteaELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd05718   74 -----GLRNATLRIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 162-258 6.76e-50

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) 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: 409500  Cd Length: 97  Bit Score: 166.42  E-value: 6.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 162 PKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVE 241
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 112789532 242 HESFEEPALIPVTLSVR 258
Cdd:cd07703   81 HETLEEPQLLPVTLSVR 97
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 162-257 7.08e-41

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: 142.63  E-value: 7.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 162 PKNQAEAQKVTF-SQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTlAGTVTVTSRFTLVPSGRADGVTVTCKV 240
Cdd:cd05719    1 PTNSLEGGPALLiGGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRGS-NGTVTVTSRYRLVPSREADGQPLTCVV 79

                         90
                 ....*....|....*..
gi 112789532 241 EHESFEEPALIPVTLSV 257
Cdd:cd05719   80 EHPSLEKDQRISVTLNV 96
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 36-149 2.64e-16

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: 75.00  E-value: 2.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  36 VQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPdAPANHQNVAAFHPKMGPSFPSPKpgSERLSFVSAKqstgqd 115
Cdd:cd05886    3 VQVNDSMSGFIGTDVVLHCSFANPLPSVKITQVTWQKS-TNGSKQNVAIYNPSMGVSVLPPY--RERVTFLNPS------ 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 112789532 116 teaeLQDATLALHGLTVEDEGNYTCEFATFPKGS 149
Cdd:cd05886   74 ----FTDGTIRLSRLELEDEGVYICEFATFPTGN 103
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 175-249 2.13e-15

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 71.68  E-value: 2.13e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112789532  175 QDPTTVALCISKEGRPPARISWLSSLD--WEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPA 249
Cdd:pfam08205  13 EGPEVVATCSSAGGKPAPRITWYLDGKplEAAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSYGALRGSI 89
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 43-158 1.55e-13

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 66.98  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  43 RGQLGGTVELPCHLLPPVPglyISLVTWQRPDAPANHqNVAAFHPKMG-PSFPSPKpgsERLSFvsakqstgqdTEAELQ 121
Cdd:cd05846    9 RAVLGGNATLSCNLTLPEE---VLQVTWQKIKASSPE-NIVTYSKKYGvKIQPSYV---RRISF----------TSSGLN 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 112789532 122 DATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd05846   72 STSITIWNVTLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 175-257 1.31e-11

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: 60.99  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 175 QDPTTVALCISKEGRPPARISWlsslDWEAKETQVSGTL--AGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIP 252
Cdd:cd07704   16 GNETLAASCTAETGKPAASVTW----ETDLGGMESSRTFehNRTATVTSEYHLVPTRFANGRPLTCVVSHPALQQDIRIT 91


                 ....*
gi 112789532 253 VTLSV 257
Cdd:cd07704   92 HILDV 96
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 37-158 5.82e-10

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: 56.70  E-value: 5.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532   37 QVLPEVRGQLGGTVELPCHLLPPVPGlYISLVTWQR-PDAPANHQNVAAFHPKMGPSFPSPKpgserlsfVSAKQSTGQd 115
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSE-ASTSVYWYRqPPGKGPTFLIAYYSNGSEEGVKKGR--------FSGRGDPSN- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 112789532  116 teaelQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:pfam07686  71 -----GDGSLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IgC1_2_Nectin-1_like cd05890
Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig ...
 153-243 8.09e-10

Second immunoglobulin (Ig) domain of nectin-1, 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-1 (also known as poliovirus receptor related protein 1, or cluster of differentiation (CD) 111). Nectin-1 belongs 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. Nectins also 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: 143298  Cd Length: 98  Bit Score: 56.15  E-value: 8.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 153 MTWLRVIAKPKNQAEAQKvtfsqDPTTVALCISKEGRPPARISWLSSLDWEAkETQVSGTLAGTVTVTSRFTLVPSGRAD 232
Cdd:cd05890    2 TNRMEGTTAVLRAKKGQD-----DKVLVATCTSANGKPPSVVSWDTRLKGEA-EFQEIRNPNGTVTVISRYRLVPSREAH 75

                         90
                 ....*....|.
gi 112789532 233 GVTVTCKVEHE 243
Cdd:cd05890   76 QQSLACIVNYH 86
IGv smart00406
Immunoglobulin V-Type;
49-142 7.21e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 49.69  E-value: 7.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532    49 TVELPCHLLPPVPGLYIslVTWQRpDAPANHQNVAAFHPKMGPSFPSPKPgSERLSFVSAKQSTgqdteaelqDATLALH 128
Cdd:smart00406   1 SVTLSCKFSGSTFSSYY--VSWVR-QPPGKGLEWLGYIGSNGSSYYQESY-KGRFTISKDTSKN---------DVSLTIS 67

                           90
                   ....*....|....
gi 112789532   129 GLTVEDEGNYTCEF 142
Cdd:smart00406  68 NLRVEDTGTYYCAV 81
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 38-159 7.25e-08

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family 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, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 50.70  E-value: 7.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  38 VLPEVRGQLGGTVELPCHLLPPVPglyISLVTWQRPdAPANHQNVAAFHPKMGPSFPSPKPGseRLSFVSAkqstgqdte 117
Cdd:cd05887    5 VEPHVTAVWGKNVSLKCLIEVNET---ITQISWEKI-HGKSSQTVAVHHPQYGISIQGEYQG--RVSFKNY--------- 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 112789532 118 aELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVI 159
Cdd:cd05887   70 -SLNDATITLHNVGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 40-158 8.48e-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: 44.03  E-value: 8.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532    40 PEVRGQLGGTVELPCHllppVPGLYISLVTWQRPDapanhqnvaafhpkmgpsfPSPKPGSERLSFVSakqstgqdteaE 119
Cdd:smart00410   2 PSVTVKEGESVTLSCE----ASGSPPPEVTWYKQG-------------------GKLLAESGRFSVSR-----------S 47

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 112789532   120 LQDATLALHGLTVEDEGNYTCEfATFPKGSVRGMTWLRV 158
Cdd:smart00410  48 GSTSTLTISNVTPEDSGTYTCA-ATNSSGSASSGTTLTV 85
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 37-159 1.28e-05

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes.


Pssm-ID: 409472  Cd Length: 111  Bit Score: 44.47  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  37 QVLPEVRGQLGGTVELPChlLPPVPGLyISLVTWQRpdAPANHQNVAAFHPKMGPSFPSPKPGseRLSFvsakqstgQDT 116
Cdd:cd05889    4 EVLWDTSVPLSENMSLEC--VYPSTGI-LTQVEWTK--IGGQKDNIAVYHPTHGMHIRKPYAG--RVYF--------LNS 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 112789532 117 EAELQDATLALHGLTVEDEGNYTCEFATFPKGSvrgmtWLRVI 159
Cdd:cd05889   69 TMASNNMSLSFRNASEDDVGYYSCSLYTYPQGS-----WEKVI 106
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 174-253 3.65e-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: 42.45  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 174 SQDPTTVaLCISKEGRPP-ARISWL---SSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPA 249
Cdd:cd00098   13 GGGKVTL-VCLVSGFYPKdITVTWLkngVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTHESLKSPL 91


                 ....
gi 112789532 250 LIPV 253
Cdd:cd00098   92 SKTW 95
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 183-244 8.57e-05

Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 or CADM3), Necl-2 (also known as CADM1), Necl-3 (also known as CADM2) and Necl-4 (also known as CADM4). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues, and is a putative tumour suppressor gene, which is downregulated in aggressive neuroblastoma. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system, where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Necl-4 is expressed on Schwann cells, and plays a key part in initiating peripheral nervous system (PNS) myelination. Necl-4 participates in cell-cell adhesion and is proposed to play a role in tumor suppression.


Pssm-ID: 409418  Cd Length: 102  Bit Score: 41.65  E-value: 8.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112789532 183 CISKEGRPPARISWLSSlDWE---AKETQVSGTlAGTVTVTSRFTLVPSGRADGVTVTCKVEHES 244
Cdd:cd05761   26 CTTSGSKPAADIRWFKN-DKElkgVKEVQESGA-GKTFTVTSTLRFRVDRDDDGVAVICRVDHES 88
IgI_2_Necl-1 cd07705
Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set ...
 163-249 8.71e-05

Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1; also known as cell adhesion molecule3 (CADM3)). These nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains is essential to cell-cell adhesion and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 and Necl-2 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 409502  Cd Length: 103  Bit Score: 41.88  E-value: 8.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532 163 KNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSS-LDWEAKETQVSGTLAG-TVTVTSRFTLVPSGRADGVTVTCKV 240
Cdd:cd07705    6 KPQITGYESAFKEKDKAKLRCTSSGSKPAANIKWRKGdQELEGAPTSVQEDGNGkTFTVSSSVEFQVTREDDGAEITCSV 85


                 ....*....
gi 112789532 241 EHESFEEPA 249
Cdd:cd07705   86 GHESLHDSD 94
IgI_2_Necl-3 cd05884
Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set ...
 183-244 1.52e-04

Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3; also known as cell adhesion molecule 2 (CADM2)). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Necl-3 has been shown to accumulate in tissues of the central and peripheral nervous system where it is expressed in ependymal cells and myelinated axons. It is observed at the interface between the axon shaft and the myelin sheath. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 409467  Cd Length: 104  Bit Score: 41.07  E-value: 1.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112789532 183 CISKEGRPPARISWLSSlDWE---AKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHES 244
Cdd:cd05884   27 CKTSGSKPAADIRWFKN-DKEvkdVKYLKAEDANRKTFTVSSSLDFHVDRDDDGVAITCRVDHES 90
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 46-159 1.66e-04

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: 41.04  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  46 LGGTVELPCHLLPPvPGLYISLVTWQRPDAPANHQNVAAFHPKMGPSfpspkpgserlSFVSAKQSTGQDTEAELQDATL 125
Cdd:cd05888    7 LGQDAKLPCFYRGD-SGEQVGQVAWARVDAGEGAQEIALLHSKYGLH-----------VFPAYEGRVEQPPPPRPADGSV 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 112789532 126 ALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVI 159
Cdd:cd05888   75 LLRNAVQADEGEYECRVSTFPAGNFQAELRLRVL 108
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 214-248 7.07e-04

Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain on Tapasin-R. Tapasin is a V-C1 (variable-constant) immunoglobulin superfamily molecule present in the endoplasmic reticulum (ER), where it links MHC class I molecules to the transporter associated with antigen processing (TAP). Tapasin-R is a tapasin-related protein that contains similar structural motifs to Tapasin, with some marked differences, especially in the V domain, transmembrane and cytoplasmic regions. The majority of Tapasin-R is located within the ER; however, there may be some expression of Tapasin-R at the cell surface. Tapasin-R lacks an obvious ER retention signal.


Pssm-ID: 409428  Cd Length: 100  Bit Score: 39.02  E-value: 7.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 112789532 214 AGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEP 248
Cdd:cd05771   62 DGTYSISSYLTLEPGTENRGATYTCRVTHVSLEEP 96
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 279-343 7.47e-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: 38.08  E-value: 7.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112789532 279 ATLSCDVRSNPEPTgYDWS------TTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQV 343
Cdd:cd00096    1 VTLTCSASGNPPPT-ITWYkngkplPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 260-333 1.79e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.16  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  260 PPEVSISGYDDNWYLGRTdATLSCDVRSNPEPTgYDWS------TTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTN 333
Cdd:pfam13927   1 KPVITVSPSSVTVREGET-VTLTCEATGSPPPT-ITWYkngepiSSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_Necl-2 cd05883
Second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2); member of the I-set ...
 167-242 4.43e-03

Second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2); member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin (Ig)-like domain of nectin-like molecule 2 (Necl-2; also known as cell adhesion molecule 1 (CADM1)). Nectin-like molecules (Necls) have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 through Necl-5). These have an extracellular region containing three Ig-like domains, one transmembrane region, and one cytoplasmic region. Necl-2 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Ig domains are likely to participate in ligand binding and recognition.


Pssm-ID: 409466  Cd Length: 99  Bit Score: 36.82  E-value: 4.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112789532 167 EAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEH 242
Cdd:cd05883   10 DIQKDTAVEGEEIELNCTAMASKPAATIRWFKGNKELTGKSEVEEWYSRMFTVTSQLMLKVTKEDDGVPVICLVDH 85
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 40-141 9.68e-03

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the 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, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. 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: 409482  Cd Length: 128  Bit Score: 36.48  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789532  40 PEVRGQLGGTVELPCHL--LPPVPGLY--------ISLVTWQRPDAPANHQNVAAFHPKMGpsfpSPKPGSE---RLSFV 106
Cdd:cd05901    5 SRVHGSLSGSVVLPCRFstLPTLPPSYnitseflrIKWTKIQVDKNGKDHKETTVLVAQNG----IIKIGQEymgRVSVP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 112789532 107 SAKQSTGqdteaelqDATLALHGLTVEDEGNYTCE 141
Cdd:cd05901   81 SHPEDQG--------DASLTIVKLRASDAGVYRCE 107
 
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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