NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|528992104|ref|XP_005219253|]
View 

nectin-2 isoform X1 [Bos taurus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 264-349 3.69e-54

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: 177.37  E-value: 3.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 264 PQVSISGYDDNWYIGRSEATLNCNVRSKPEPTGYDWSTTSGVFPASAVAQGPKLIVHSVDRLFNTTFICTVTNAVGTGQA 343
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 528992104 344 EQVVLV 349
Cdd:cd20930   81 EQTIFV 86
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 35-161 2.03e-47

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 cd20989:

Pssm-ID: 472250  Cd Length: 112  Bit Score: 160.82  E-value: 2.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  35 VRVQVAAEVRGNLGDTVELPCHLLPSAPEIRVSQVTWLRLDApegKQNVAIFHPQYGRSFPSPkpgkERLSFVntapssG 114
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHDE---HGSVAVFHPKQGPSFPES----ERLSFV------A 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528992104 115 AGQGSELevRDATLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRV 161
Cdd:cd20989   68 ARLGAEL--RNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 165-261 8.14e-46

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: 155.64  E-value: 8.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 165 PQNHAEKQEVTFNLDPVPVARCVSAGGRPPARVSWLSPLDGEAKETQGSGPLPGTVTVTSRYTVTPLSEADGVKVICKVE 244
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 528992104 245 HESFQEPKLLPVILSVR 261
Cdd:cd07703   81 HETLEEPQLLPVTLSVR 97
 
Name Accession Description Interval E-value
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 264-349 3.69e-54

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: 177.37  E-value: 3.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 264 PQVSISGYDDNWYIGRSEATLNCNVRSKPEPTGYDWSTTSGVFPASAVAQGPKLIVHSVDRLFNTTFICTVTNAVGTGQA 343
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 528992104 344 EQVVLV 349
Cdd:cd20930   81 EQTIFV 86
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 35-161 2.03e-47

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: 160.82  E-value: 2.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  35 VRVQVAAEVRGNLGDTVELPCHLLPSAPEIRVSQVTWLRLDApegKQNVAIFHPQYGRSFPSPkpgkERLSFVntapssG 114
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHDE---HGSVAVFHPKQGPSFPES----ERLSFV------A 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528992104 115 AGQGSELevRDATLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRV 161
Cdd:cd20989   68 ARLGAEL--RNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 165-261 8.14e-46

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: 155.64  E-value: 8.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 165 PQNHAEKQEVTFNLDPVPVARCVSAGGRPPARVSWLSPLDGEAKETQGSGPLPGTVTVTSRYTVTPLSEADGVKVICKVE 244
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 528992104 245 HESFQEPKLLPVILSVR 261
Cdd:cd07703   81 HETLEEPQLLPVTLSVR 97
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 179-252 2.34e-16

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 74.38  E-value: 2.34e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528992104  179 DPVPVARCVSAGGRPPARVSWLspLDGE----AKETQGSGPLPGTVTVTSRYTVTPLSEADGVKVICKVEHESFQEPK 252
Cdd:pfam08205  14 GPEVVATCSSAGGKPAPRITWY--LDGKpleaAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSYGALRGSI 89
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 38-161 1.18e-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: 64.40  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104   38 QVAAEVRGNLGDTVELPCHLLPSAPEiRVSQVTWLRLDAPEGKQN-VAIFHPQYGRSFPspkpgKERLSFvNTAPSSGag 116
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSE-ASTSVYWYRQPPGKGPTFlIAYYSNGSEEGVK-----KGRFSG-RGDPSNG-- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528992104  117 qgselevrDATLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRV 161
Cdd:pfam07686  72 --------DGSLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
50-145 6.33e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 52.77  E-value: 6.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104    50 TVELPCHLLPSAPEIrvSQVTWLRLdaPEGKQN-VAIFHPQYGRSFPSPKPgKERLSFVntapssgaGQGSElevRDATL 128
Cdd:smart00406   1 SVTLSCKFSGSTFSS--YYVSWVRQ--PPGKGLeWLGYIGSNGSSYYQESY-KGRFTIS--------KDTSK---NDVSL 64

                           90
                   ....*....|....*..
gi 528992104   129 SLRGLTVEDEGNYTCEF 145
Cdd:smart00406  65 TISNLRVEDTGTYYCAV 81
 
Name Accession Description Interval E-value
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 264-349 3.69e-54

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: 177.37  E-value: 3.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 264 PQVSISGYDDNWYIGRSEATLNCNVRSKPEPTGYDWSTTSGVFPASAVAQGPKLIVHSVDRLFNTTFICTVTNAVGTGQA 343
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 528992104 344 EQVVLV 349
Cdd:cd20930   81 EQTIFV 86
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 35-161 2.03e-47

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: 160.82  E-value: 2.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  35 VRVQVAAEVRGNLGDTVELPCHLLPSAPEIRVSQVTWLRLDApegKQNVAIFHPQYGRSFPSPkpgkERLSFVntapssG 114
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHDE---HGSVAVFHPKQGPSFPES----ERLSFV------A 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528992104 115 AGQGSELevRDATLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRV 161
Cdd:cd20989   68 ARLGAEL--RNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 165-261 8.14e-46

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: 155.64  E-value: 8.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 165 PQNHAEKQEVTFNLDPVPVARCVSAGGRPPARVSWLSPLDGEAKETQGSGPLPGTVTVTSRYTVTPLSEADGVKVICKVE 244
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 528992104 245 HESFQEPKLLPVILSVR 261
Cdd:cd07703   81 HETLEEPQLLPVTLSVR 97
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 35-161 1.50e-45

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: 155.68  E-value: 1.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  35 VRVQVAAEVRGNLGDTVELPCHLLPSAPEIrVSQVTWLRLDAPEgKQNVAIFHPQYGRSFPSPKpgKERLSFVNtapssg 114
Cdd:cd05718    1 QRVQVPTEVTGFLGGSVTLPCSLTSPGTTK-ITQVTWMKIGAGS-SQNVAVFHPQYGPSVPNPY--AERVEFLA------ 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528992104 115 agqgSELEVRDATLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRV 161
Cdd:cd05718   71 ----ARLGLRNATLRIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 165-260 2.91e-31

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: 116.44  E-value: 2.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 165 PQNHAEKQEVTF-NLDPVPVARCVSAGGRPPARVSWLSPLDGEAKETQGSGPlPGTVTVTSRYTVTPLSEADGVKVICKV 243
Cdd:cd05719    1 PTNSLEGGPALLiGGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRGS-NGTVTVTSRYRLVPSREADGQPLTCVV 79

                         90
                 ....*....|....*..
gi 528992104 244 EHESFQEPKLLPVILSV 260
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 ...
 37-151 7.58e-19

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: 82.32  E-value: 7.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  37 VQVAAEVRGNLGDTVELPCHLLPSAPEIRVSQVTWLRLdAPEGKQNVAIFHPQYGRSFPSPKpgKERLSFVNTApssgag 116
Cdd:cd05886    3 VQVNDSMSGFIGTDVVLHCSFANPLPSVKITQVTWQKS-TNGSKQNVAIYNPSMGVSVLPPY--RERVTFLNPS------ 73

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528992104 117 qgseleVRDATLSLRGLTVEDEGNYTCEFATFPKG 151
Cdd:cd05886   74 ------FTDGTIRLSRLELEDEGVYICEFATFPTG 102
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 179-252 2.34e-16

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 74.38  E-value: 2.34e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528992104  179 DPVPVARCVSAGGRPPARVSWLspLDGE----AKETQGSGPLPGTVTVTSRYTVTPLSEADGVKVICKVEHESFQEPK 252
Cdd:pfam08205  14 GPEVVATCSSAGGKPAPRITWY--LDGKpleaAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQVSYGALRGSI 89
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 38-161 1.18e-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: 64.40  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104   38 QVAAEVRGNLGDTVELPCHLLPSAPEiRVSQVTWLRLDAPEGKQN-VAIFHPQYGRSFPspkpgKERLSFvNTAPSSGag 116
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSE-ASTSVYWYRQPPGKGPTFlIAYYSNGSEEGVK-----KGRFSG-RGDPSNG-- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528992104  117 qgselevrDATLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRV 161
Cdd:pfam07686  72 --------DGSLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 47-161 1.99e-12

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: 63.52  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  47 LGDTVELPCHLLPSApeiRVSQVTWLRlDAPEGKQNVAIFHPQYGrsFPSPKPGKERLSFvntapssgagqgSELEVRDA 126
Cdd:cd05846   12 LGGNATLSCNLTLPE---EVLQVTWQK-IKASSPENIVTYSKKYG--VKIQPSYVRRISF------------TSSGLNST 73

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528992104 127 TLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRV 161
Cdd:cd05846   74 SITIWNVTLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 47-157 1.14e-11

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: 61.80  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  47 LGDTVELPChLLPSAPEIrvSQVTWLRLdaPEGKQNVAIFHPQYGRSFPSPKpgKERLSFVNTAPSSgagqgselevRDA 126
Cdd:cd05889   13 LSENMSLEC-VYPSTGIL--TQVEWTKI--GGQKDNIAVYHPTHGMHIRKPY--AGRVYFLNSTMAS----------NNM 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 528992104 127 TLSLRGLTVEDEGNYTCEFATFPKGTSRGVT 157
Cdd:cd05889   76 SLSFRNASEDDVGYYSCSLYTYPQGSWEKVI 106
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 39-162 1.79e-10

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: 58.02  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  39 VAAEVRGNLGDTVELPCHLlpsAPEIRVSQVTWLRLdAPEGKQNVAIFHPQYGRSFPSPKPGkeRLSFVNtaPSsgagqg 118
Cdd:cd05887    5 VEPHVTAVWGKNVSLKCLI---EVNETITQISWEKI-HGKSSQTVAVHHPQYGISIQGEYQG--RVSFKN--YS------ 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528992104 119 seleVRDATLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRVI 162
Cdd:cd05887   71 ----LNDATITLHNVGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IgC1_2_Nectin-1_like cd05890
Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig ...
 179-256 4.26e-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: 56.92  E-value: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 179 DPVPVARCVSAGGRPPARVSWLSPLDGEA--KETQGSGplpGTVTVTSRYTVTPLSEADGVKVICKVEH--ESFQEPKLL 254
Cdd:cd05890   20 DKVLVATCTSANGKPPSVVSWDTRLKGEAefQEIRNPN---GTVTVISRYRLVPSREAHQQSLACIVNYhmDRFTDSLTL 96


                 ..
gi 528992104 255 PV 256
Cdd:cd05890   97 NV 98
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 47-162 1.08e-09

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: 56.06  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  47 LGDTVELPCHLLPSAPEiRVSQVTWLRLDAPEGKQNVAIFHPQYGRSFPSPKPGKERlsfvntapssgagQGSELEVRDA 126
Cdd:cd05888    7 LGQDAKLPCFYRGDSGE-QVGQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVE-------------QPPPPRPADG 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528992104 127 TLSLRGLTVEDEGNYTCEFATFPKGTSRGVTWLRVI 162
Cdd:cd05888   73 SVLLRNAVQADEGEYECRVSTFPAGNFQAELRLRVL 108
IGv smart00406
Immunoglobulin V-Type;
50-145 6.33e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 52.77  E-value: 6.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104    50 TVELPCHLLPSAPEIrvSQVTWLRLdaPEGKQN-VAIFHPQYGRSFPSPKPgKERLSFVntapssgaGQGSElevRDATL 128
Cdd:smart00406   1 SVTLSCKFSGSTFSS--YYVSWVRQ--PPGKGLeWLGYIGSNGSSYYQESY-KGRFTIS--------KDTSK---NDVSL 64

                           90
                   ....*....|....*..
gi 528992104   129 SLRGLTVEDEGNYTCEF 145
Cdd:smart00406  65 TISNLRVEDTGTYYCAV 81
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 183-260 7.33e-09

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: 53.28  E-value: 7.33e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528992104 183 VARCVSAGGRPPARVSWLSPLdGEAKETQGSGPlPGTVTVTSRYTVTPLSEADGVKVICKVEHESFQEPKLLPVILSV 260
Cdd:cd07704   21 AASCTAETGKPAASVTWETDL-GGMESSRTFEH-NRTATVTSEYHLVPTRFANGRPLTCVVSHPALQQDIRITHILDV 96
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 168-256 2.55e-07

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: 48.61  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 168 HAEKQEVTFNLDPVPVARCVSAGGRPP-ARVSWL---SPLDGEAKETQGSGPLPGTVTVTSRYTVTPLSEADGVKVICKV 243
Cdd:cd00098    3 TLLPPSPEEKGGGKVTLVCLVSGFYPKdITVTWLkngVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVV 82

                         90
                 ....*....|...
gi 528992104 244 EHESFQEPKLLPV 256
Cdd:cd00098   83 THESLKSPLSKTW 95
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 170-247 3.87e-07

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: 48.58  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104 170 EKQEVTFNldpvpvarCVSAGGRPPARVSWLSPlDGE---AKETQGSGPLPgTVTVTSRYTVTPLSEADGVKVICKVEHE 246
Cdd:cd05761   18 EGDEITLT--------CTTSGSKPAADIRWFKN-DKElkgVKEVQESGAGK-TFTVTSTLRFRVDRDDDGVAVICRVDHE 87


                 .
gi 528992104 247 S 247
Cdd:cd05761   88 S 88
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 41-145 2.32e-06

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: 46.55  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  41 AEVRGNLGDTVELPCHLL--PSAPEIRVSQVTWLRLDAPEGKQN---VAI--FHPQYGrsfpspkpgkerlSFVNTAPSS 113
Cdd:cd05877    5 AKVFSHRGGNVTLPCRYHyePELSAPRKIRVKWTKLEVDYAKEEdvlVAIgtRHKSYG-------------SYQGRVFLR 71

                         90       100       110
                 ....*....|....*....|....*....|..
gi 528992104 114 GAGQgselevRDATLSLRGLTVEDEGNYTCEF 145
Cdd:cd05877   72 RADD------LDASLVITDLRLEDYGRYRCEV 97
IgI_2_Necl-1 cd07705
Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set ...
 185-250 2.73e-06

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: 46.11  E-value: 2.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528992104 185 RCVSAGGRPPARVSWL---SPLDGEAKETQgSGPLPGTVTVTSRYTVTPLSEADGVKVICKVEHESFQE 250
Cdd:cd07705   25 RCTSSGSKPAANIKWRkgdQELEGAPTSVQ-EDGNGKTFTVSSSVEFQVTREDDGAEITCSVGHESLHD 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 43-161 3.01e-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: 45.57  E-value: 3.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104    43 VRGNLGDTVELPCHLLPSAPeirvSQVTWLRLDapegkqnvaifhpqygrsfPSPKPGKERLSFVNTAPSSgagqgsele 122
Cdd:smart00410   4 VTVKEGESVTLSCEASGSPP----PEVTWYKQG-------------------GKLLAESGRFSVSRSGSTS--------- 51

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 528992104   123 vrdaTLSLRGLTVEDEGNYTCEfATFPKGTSRGVTWLRV 161
Cdd:smart00410  52 ----TLTISNVTPEDSGTYTCA-ATNSSGSASSGTTLTV 85
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 48-162 1.28e-05

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 44.36  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  48 GDTVELPCHLLPSAPEIRVSQVTWLrLDAPEGKQNVAIFHPQyGRSF-PSPKPGKERLSFVntapssgagqgSELEVRDA 126
Cdd:cd20960   15 GENVTLPCHHQLGLEDQGTLDIEWL-LLPSDKVEKVVITYSG-DRVYnHYYPALKGRVAFT-----------SNDLSGDA 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528992104 127 TLSLRGLTVEDEGNYTCEFATFPkgtsrGVTWLRVI 162
Cdd:cd20960   82 SLNISNLKLSDTGTYQCKVKKAP-----GYAWSKIT 112
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 35-149 1.08e-04

Immunoglobulin (Ig)-like domain of protein zero (P0); 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 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.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 41.79  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  35 VRVQVAAEVRGNLGDTVELPCHLLPS---APEIrvsQVTWlRLDAPEGKQNVAIFHPQYGRSFPSPK-PGKERLSFVNTa 110
Cdd:cd05879    1 IVVYTDREVYGTVGSDVTLSCSFWSSewiSDDI---SFTW-HYQPDGSRDAISIFHYGKGQPYIDNVgPFKERIEWVGN- 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528992104 111 PSSgagqgselevRDATLSLRGLTVEDEGNYTCEFATFP 149
Cdd:cd05879   76 PSR----------KDGSIVIHNLDYTDNGTFTCDVKNPP 104
IgI_2_Necl-3 cd05884
Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set ...
 186-247 1.35e-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: 41.45  E-value: 1.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528992104 186 CVSAGGRPPARVSWLSPlDGE---AKETQGSGPLPGTVTVTSRYTVTPLSEADGVKVICKVEHES 247
Cdd:cd05884   27 CKTSGSKPAADIRWFKN-DKEvkdVKYLKAEDANRKTFTVSSSLDFHVDRDDDGVAITCRVDHES 90
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 35-143 1.70e-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: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  35 VRVQVAAEVRGNLGDTVELPCHLLPSAPEIRVSQVTWlRLDAPEGKQNVAIFHPQYGRSFPsPKPG--KERLSFVntaps 112
Cdd:cd05715    1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTW-TYQPEGGNTTESMFHYSKGKPYI-LKVGrfKDRVSWA----- 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 528992104 113 sgagqgSELEVRDATLSLRGLTVEDEGNYTC 143
Cdd:cd05715   74 ------GNPSKKDASIVISNLQFSDNGTYTC 98
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 43-145 2.32e-04

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: 40.64  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  43 VRGNLGDTVELPCHLLP--SAP--EIRvsqvtWLR--LDAP-----EGKQNVAIFHPQYgrsfpspkpgKERLSFVntap 111
Cdd:cd05713   10 ILALVGEDAELPCHLSPkmSAEhmEVR-----WFRsqFSPVvhlyrDGQDQEEEQMPEY----------RGRTELL---- 70

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528992104 112 SSGAGQGSelevrdATLSLRGLTVEDEGNYTCEF 145
Cdd:cd05713   71 KDAIAEGS------VALRIHNVRPSDEGQYTCFF 98
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
 47-161 1.25e-03

Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H6 (also known as NCR3LG1). B7-H6 contains one IgV domain and one IgC domain (IgV-IgC) and belongs to the B7-family, which consists of structurally related cell-surface protein ligands which bind to receptors on lymphocytes that regulate immune responses. B7-H6 is a ligand of NKp30, which is a member of CD28 family and an activating receptor of natural killer (NK) cells. The expression of NKp30 has been found in most of NK cells, which is involved in the process of tumor cell killing and interaction with antigen presenting cells (APCs) such as dendritic cells. Studies showed that NK cells eliminate B7-H6-expressing tumor cells either directly via cytotoxicity or indirectly by cytokine secretion. For instance, chimeric NKp30-expressing T cells responded to B7-H6(+) tumor cells and those T cells produced IFN-gamma and killed B7-H6-expressing tumor cells in vivo. B7-H6 mRNA is not found in normal cells, while high expression of B7-H6 is found in certain type tumor cells, such as lymphoma, leukemia, ovarian cancer, brain tumors, breast cancers, and various sarcomas. Since B7-H6 can bind NKp30 to exert anti-tumor effects by NK cells, which are able to recognize the difference between cancer cells and normal cells, B7-H6 may serve as a promising target for cancer immunotherapy.


Pssm-ID: 409573  Cd Length: 114  Bit Score: 38.75  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528992104  47 LGDTVELPCHLLPSAP-EIRVSQVTWLRLDaPEGKQNVAIFHpQYGRSFPSPKPGkerlsfVNTAPSsgagqgsELEVRD 125
Cdd:cd20981   15 LNDNVTIFCNIFYSQPlNITSMGITWFRKS-LTFDKEVKVFE-FFGDHQKAFRPG------AIVSPW-------RLKSGD 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528992104 126 ATLSLRGLTVEDEGNYTCEFATFPKgTSRGVTWLRV 161
Cdd:cd20981   80 ASLQLPGVQLEEAGEYRCEVVVTPL-KAQGTVQLEV 114
C1-set pfam07654
Immunoglobulin C1-set domain;
193-247 9.68e-03

Immunoglobulin C1-set domain;


Pssm-ID: 462221  Cd Length: 85  Bit Score: 35.30  E-value: 9.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528992104  193 PPARVSWLSplDGEaKETQG---SGPLP---GTVTVTSRYTVTPLSEADGVKVICKVEHES 247
Cdd:pfam07654  27 PDITVTWLK--NGQ-EVTEGvktTPPSPnsdWTYQLSSYLTVTPSDWESGDEYTCRVEHEG 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH