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Conserved domains on  [gi|228480273|ref|NP_033016|]
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nectin-2 isoform 1 precursor [Mus musculus]

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 ...
 34-149 4.37e-60

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: 193.95  E-value: 4.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  34 VRVRVLPEVRGRLGGTVELPCHLLPPTT-ERVSQVTWQRLD-GTVVAAFHPSFGVDFPNSqfskDRLSFVRARPetNADL 111
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMvTHVSQVTWQRHDeHGSVAVFHPKQGPSFPES----ERLSFVAARL--GAEL 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 228480273 112 RDATLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRV 149
Cdd:cd20989   75 RNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 252-337 1.86e-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: 178.14  E-value: 1.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 252 PEVSISGYDDNWYLGRSEAILTCDVRSNPEPTDYDWSTTSGVFPASAVAQGSQLLVHSVDRMVNTTFICTATNAVGTGRA 331
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 228480273 332 EQVILV 337
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; ...
 153-249 2.03e-45

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: 154.48  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 153 PENHAEAQEVTIGPQSVAVARCVSTGGRPPARITWISSLGGEAKDTQEPGIQAGTVTIISRYSLVPVGRADGVKVTCRVE 232
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 228480273 233 HESFEEPILLPVTLSVR 249
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 ...
 34-149 4.37e-60

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: 193.95  E-value: 4.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  34 VRVRVLPEVRGRLGGTVELPCHLLPPTT-ERVSQVTWQRLD-GTVVAAFHPSFGVDFPNSqfskDRLSFVRARPetNADL 111
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMvTHVSQVTWQRHDeHGSVAVFHPKQGPSFPES----ERLSFVAARL--GAEL 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 228480273 112 RDATLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRV 149
Cdd:cd20989   75 RNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 252-337 1.86e-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: 178.14  E-value: 1.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 252 PEVSISGYDDNWYLGRSEAILTCDVRSNPEPTDYDWSTTSGVFPASAVAQGSQLLVHSVDRMVNTTFICTATNAVGTGRA 331
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 228480273 332 EQVILV 337
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; ...
 153-249 2.03e-45

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: 154.48  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 153 PENHAEAQEVTIGPQSVAVARCVSTGGRPPARITWISSLGGEAKDTQEPGIQAGTVTIISRYSLVPVGRADGVKVTCRVE 232
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 228480273 233 HESFEEPILLPVTLSVR 249
Cdd:cd07703   81 HETLEEPQLLPVTLSVR 97
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 155-240 5.35e-20

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 84.39  E-value: 5.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  155 NHAEAQEVTI-GPQSVAVARCVSTGGRPPARITWISSLGGE--AKDTQEPGIQAGTVTIISRYSLVPVGRADGVKVTCRV 231
Cdd:pfam08205   1 PTIEPPASLLeGEGPEVVATCSSAGGKPAPRITWYLDGKPLeaAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQV 80


                  ....*....
gi 228480273  232 EHESFEEPI 240
Cdd:pfam08205  81 SYGALRGSI 89
IGv smart00406
Immunoglobulin V-Type;
49-133 1.63e-12

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 63.17  E-value: 1.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273    49 TVELPCHLLPPTTERvSQVTWQR---LDGTVVAAFHPSFGVDFPNSQFsKDRLSFVRarpetNADLRDATLAFRGLRVED 125
Cdd:smart00406   1 SVTLSCKFSGSTFSS-YYVSWVRqppGKGLEWLGYIGSNGSSYYQESY-KGRFTISK-----DTSKNDVSLTISNLRVED 73


                   ....*...
gi 228480273   126 EGNYTCEF 133
Cdd:smart00406  74 TGTYYCAV 81
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 40-149 1.12e-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: 58.62  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273   40 PEVRGRLGGTVELPCHLLPPTTERVSQVTWQRLDG-----TVVAAFHPSFGVDFPnsqfsKDRLSFvrarpETNADLRDA 114
Cdd:pfam07686   4 REVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPgkgptFLIAYYSNGSEEGVK-----KGRFSG-----RGDPSNGDG 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 228480273  115 TLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRV 149
Cdd:pfam07686  74 SLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 251-324 6.97e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  251 PPEVSISGYDDNWYLGrSEAILTCDVRSNPEPTdYDWS------TTSGVFPASAVAQGSQLLVHSVDRMVNTTFICTATN 324
Cdd:pfam13927   1 KPVITVSPSSVTVREG-ETVTLTCEATGSPPPT-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 ...
 34-149 4.37e-60

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: 193.95  E-value: 4.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  34 VRVRVLPEVRGRLGGTVELPCHLLPPTT-ERVSQVTWQRLD-GTVVAAFHPSFGVDFPNSqfskDRLSFVRARPetNADL 111
Cdd:cd20989    1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMvTHVSQVTWQRHDeHGSVAVFHPKQGPSFPES----ERLSFVAARL--GAEL 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 228480273 112 RDATLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRV 149
Cdd:cd20989   75 RNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 252-337 1.86e-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: 178.14  E-value: 1.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 252 PEVSISGYDDNWYLGRSEAILTCDVRSNPEPTDYDWSTTSGVFPASAVAQGSQLLVHSVDRMVNTTFICTATNAVGTGRA 331
Cdd:cd20930    1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                 ....*.
gi 228480273 332 EQVILV 337
Cdd:cd20930   81 EQTIFV 86
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 34-149 5.80e-53

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: 174.94  E-value: 5.80e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  34 VRVRVLPEVRGRLGGTVELPCHLLPPTTERVSQVTWQRLDG---TVVAAFHPSFGVDFPNSQfsKDRLSFVRARPetnaD 110
Cdd:cd05718    1 QRVQVPTEVTGFLGGSVTLPCSLTSPGTTKITQVTWMKIGAgssQNVAVFHPQYGPSVPNPY--AERVEFLAARL----G 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 228480273 111 LRDATLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRV 149
Cdd:cd05718   75 LRNATLRIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 153-249 2.03e-45

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: 154.48  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 153 PENHAEAQEVTIGPQSVAVARCVSTGGRPPARITWISSLGGEAKDTQEPGIQAGTVTIISRYSLVPVGRADGVKVTCRVE 232
Cdd:cd07703    1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                         90
                 ....*....|....*..
gi 228480273 233 HESFEEPILLPVTLSVR 249
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), ...
 153-248 7.31e-32

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: 117.98  E-value: 7.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 153 PENHAEAQEVT-IGPQSVAVARCVSTGGRPPARITWISSLGGEAKDTQEPGiQAGTVTIISRYSLVPVGRADGVKVTCRV 231
Cdd:cd05719    1 PTNSLEGGPALlIGGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRG-SNGTVTVTSRYRLVPSREADGQPLTCVV 79

                         90
                 ....*....|....*..
gi 228480273 232 EHESFEEPILLPVTLSV 248
Cdd:cd05719   80 EHPSLEKDQRISVTLNV 96
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 155-240 5.35e-20

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 84.39  E-value: 5.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  155 NHAEAQEVTI-GPQSVAVARCVSTGGRPPARITWISSLGGE--AKDTQEPGIQAGTVTIISRYSLVPVGRADGVKVTCRV 231
Cdd:pfam08205   1 PTIEPPASLLeGEGPEVVATCSSAGGKPAPRITWYLDGKPLeaAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQV 80


                  ....*....
gi 228480273  232 EHESFEEPI 240
Cdd:pfam08205  81 SYGALRGSI 89
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 36-150 5.34e-15

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: 71.15  E-value: 5.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  36 VRVLPEVRGRLGGTVELPCHL---LPPTteRVSQVTWQRL-DGTV--VAAFHPSFGVDFPNSQfsKDRLSFVrarpetNA 109
Cdd:cd05886    3 VQVNDSMSGFIGTDVVLHCSFanpLPSV--KITQVTWQKStNGSKqnVAIYNPSMGVSVLPPY--RERVTFL------NP 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 228480273 110 DLRDATLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRVI 150
Cdd:cd05886   73 SFTDGTIRLSRLELEDEGVYICEFATFPTGNRESQLNLTVM 113
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 46-149 7.80e-14

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: 67.75  E-value: 7.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  46 LGGTVELPCHLlpPTTERVSQVTWQRLDG---TVVAAFHPSFGV----DFpnsqfsKDRLSFvrarpeTNADLRDATLAF 118
Cdd:cd05846   12 LGGNATLSCNL--TLPEEVLQVTWQKIKAsspENIVTYSKKYGVkiqpSY------VRRISF------TSSGLNSTSITI 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 228480273 119 RGLRVEDEGNYTCEFATFPNGTRRGVTWLRV 149
Cdd:cd05846   78 WNVTLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IGv smart00406
Immunoglobulin V-Type;
49-133 1.63e-12

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 63.17  E-value: 1.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273    49 TVELPCHLLPPTTERvSQVTWQR---LDGTVVAAFHPSFGVDFPNSQFsKDRLSFVRarpetNADLRDATLAFRGLRVED 125
Cdd:smart00406   1 SVTLSCKFSGSTFSS-YYVSWVRqppGKGLEWLGYIGSNGSSYYQESY-KGRFTISK-----DTSKNDVSLTISNLRVED 73


                   ....*...
gi 228480273   126 EGNYTCEF 133
Cdd:smart00406  74 TGTYYCAV 81
IgC1_2_Nectin-1_like cd05890
Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig ...
 169-244 2.94e-12

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: 62.70  E-value: 2.94e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228480273 169 VAVARCVSTGGRPPARITWISSLGGEAkDTQEPGIQAGTVTIISRYSLVPVGRADGVKVTCRVEH--ESFEEPILLPV 244
Cdd:cd05890   22 VLVATCTSANGKPPSVVSWDTRLKGEA-EFQEIRNPNGTVTVISRYRLVPSREAHQQSLACIVNYhmDRFTDSLTLNV 98
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 40-149 1.12e-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: 58.62  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273   40 PEVRGRLGGTVELPCHLLPPTTERVSQVTWQRLDG-----TVVAAFHPSFGVDFPnsqfsKDRLSFvrarpETNADLRDA 114
Cdd:pfam07686   4 REVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPgkgptFLIAYYSNGSEEGVK-----KGRFSG-----RGDPSNGDG 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 228480273  115 TLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRV 149
Cdd:pfam07686  74 SLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 171-248 2.45e-10

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: 57.52  E-value: 2.45e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228480273 171 VARCVSTGGRPPARITWISSLGG-EAKDTQEPgiqAGTVTIISRYSLVPVGRADGVKVTCRVEHESFEEPILLPVTLSV 248
Cdd:cd07704   21 AASCTAETGKPAASVTWETDLGGmESSRTFEH---NRTATVTSEYHLVPTRFANGRPLTCVVSHPALQQDIRITHILDV 96
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 38-150 4.51e-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: 56.87  E-value: 4.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  38 VLPEVRGRLGGTVELPChlLPPTTERVSQVTWQRLDGT---VVAAFHPSFGVDFPNSQfsKDRLSFvrarpeTNADLRDA 114
Cdd:cd05887    5 VEPHVTAVWGKNVSLKC--LIEVNETITQISWEKIHGKssqTVAVHHPQYGISIQGEY--QGRVSF------KNYSLNDA 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 228480273 115 TLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRVI 150
Cdd:cd05887   75 TITLHNVGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 38-150 1.29e-08

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: 52.94  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  38 VLPEVRGRLGGTVELPChlLPPTTERVSQVTWQRLDGTV--VAAFHPSFGVDFPNSQfsKDRLSFVRarpeTNADLRDAT 115
Cdd:cd05889    5 VLWDTSVPLSENMSLEC--VYPSTGILTQVEWTKIGGQKdnIAVYHPTHGMHIRKPY--AGRVYFLN----STMASNNMS 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 228480273 116 LAFRGLRVEDEGNYTCEFATFPNGtrrgvTWLRVI 150
Cdd:cd05889   77 LSFRNASEDDVGYYSCSLYTYPQG-----SWEKVI 106
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 40-149 2.71e-08

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: 51.35  E-value: 2.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273    40 PEVRGRLGGTVELPCHLlppTTERVSQVTWQRLDGTVVAafhpsfgvdfpnsqfSKDRLSFVRarpetnaDLRDATLAFR 119
Cdd:smart00410   2 PSVTVKEGESVTLSCEA---SGSPPPEVTWYKQGGKLLA---------------ESGRFSVSR-------SGSTSTLTIS 56

                           90       100       110
                   ....*....|....*....|....*....|
gi 228480273   120 GLRVEDEGNYTCEfATFPNGTRRGVTWLRV 149
Cdd:smart00410  57 NVTPEDSGTYTCA-ATNSSGSASSGTTLTV 85
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 46-150 4.34e-07

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: 48.36  E-value: 4.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  46 LGGTVELPCHLLPPTTERVSQVTWQRLDGTVV----AAFHPSFGVD-FPNSQFskdrlsfvRARPETNADLRDATLAFRG 120
Cdd:cd05888    7 LGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGaqeiALLHSKYGLHvFPAYEG--------RVEQPPPPRPADGSVLLRN 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 228480273 121 LRVEDEGNYTCEFATFPNGTRRGVTWLRVI 150
Cdd:cd05888   79 AVQADEGEYECRVSTFPAGNFQAELRLRVL 108
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 154-244 3.70e-06

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: 45.53  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273 154 ENHAEAQEVTIGPQSVAVARCVSTGGRPP-ARITWI----SSLGGEAKDTQEPGiQAGTVTIISRYSLVPVGRADGVKVT 228
Cdd:cd00098    1 TVTLLPPSPEEKGGGKVTLVCLVSGFYPKdITVTWLkngvPLTSGVSTSSPVEP-NDGTYSVTSSLTVPPSDWDEGATYT 79

                         90
                 ....*....|....*.
gi 228480273 229 CRVEHESFEEPILLPV 244
Cdd:cd00098   80 CVVTHESLKSPLSKTW 95
IgV_1_CD4 cd07690
First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of ...
 42-132 6.43e-06

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


Pssm-ID: 409487  Cd Length: 97  Bit Score: 44.85  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  42 VRGRLGGTVELPCHllpPTTERVSQVTWQRLDGTVVAAFHPSFGVDFPNSQFSkdrlsfvRARPETNA-DLRDATLAFRG 120
Cdd:cd07690    4 VLGKKGDTAELPCT---ASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLND-------RADSRRNLwDQGSFPLIIKN 73

                         90
                 ....*....|..
gi 228480273 121 LRVEDEGNYTCE 132
Cdd:cd07690   74 LKIEDSDTYICE 85
IgI_2_Necl-1 cd07705
Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set ...
 170-238 7.45e-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: 44.96  E-value: 7.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228480273 170 AVARCVSTGGRPPARITWI---SSLGGEAKDTQEPGiQAGTVTIISRYSLVPVGRADGVKVTCRVEHESFEE 238
Cdd:cd07705   22 AKLRCTSSGSKPAANIKWRkgdQELEGAPTSVQEDG-NGKTFTVSSSVEFQVTREDDGAEITCSVGHESLHD 92
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 41-133 2.31e-05

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


Pssm-ID: 409461  Cd Length: 117  Bit Score: 43.85  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  41 EVRGRLGGTVELPCHLL-PPTTERVSQV----TWQRLDGT----VVAAF---HPSFGvDFpnsqfsKDRLSFVRARPetn 108
Cdd:cd05877    6 KVFSHRGGNVTLPCRYHyEPELSAPRKIrvkwTKLEVDYAkeedVLVAIgtrHKSYG-SY------QGRVFLRRADD--- 75

                         90       100
                 ....*....|....*....|....*
gi 228480273 109 adlRDATLAFRGLRVEDEGNYTCEF 133
Cdd:cd05877   76 ---LDASLVITDLRLEDYGRYRCEV 97
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 36-132 5.73e-05

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: 43.02  E-value: 5.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  36 VRVLPEVRGRLGGTVELPCHL-----LPPTTERVSQ---VTWQRL----------DGTVVAAFHPSFGVdfpnSQFSKDR 97
Cdd:cd05901    1 VRKSSRVHGSLSGSVVLPCRFstlptLPPSYNITSEflrIKWTKIqvdkngkdhkETTVLVAQNGIIKI----GQEYMGR 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 228480273  98 LSfVRARPEtnaDLRDATLAFRGLRVEDEGNYTCE 132
Cdd:cd05901   77 VS-VPSHPE---DQGDASLTIVKLRASDAGVYRCE 107
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 42-133 6.71e-05

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: 42.18  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  42 VRGRLGGTVELPCHLLPPTTERVSQVTWQRldgtvvAAFHPSF-----GVDFPNSQFS--KDRLSFVRarpETNADLRdA 114
Cdd:cd05713   10 ILALVGEDAELPCHLSPKMSAEHMEVRWFR------SQFSPVVhlyrdGQDQEEEQMPeyRGRTELLK---DAIAEGS-V 79

                         90
                 ....*....|....*....
gi 228480273 115 TLAFRGLRVEDEGNYTCEF 133
Cdd:cd05713   80 ALRIHNVRPSDEGQYTCFF 98
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 174-235 1.17e-04

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: 41.26  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228480273 174 CVSTGGRPPARITWI---SSLGGEAKDTQEPGIQAGTVTIISRYSlvpVGRAD-GVKVTCRVEHES 235
Cdd:cd05761   26 CTTSGSKPAADIRWFkndKELKGVKEVQESGAGKTFTVTSTLRFR---VDRDDdGVAVICRVDHES 88
IgI_2_Necl-3 cd05884
Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set ...
 174-235 3.10e-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: 40.30  E-value: 3.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228480273 174 CVSTGGRPPARITWISSlGGEAKDTQ---EPGIQAGTVTIISRYSLVPVGRADGVKVTCRVEHES 235
Cdd:cd05884   27 CKTSGSKPAADIRWFKN-DKEVKDVKylkAEDANRKTFTVSSSLDFHVDRDDDGVAITCRVDHES 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 38-145 2.25e-03

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 37.17  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273   38 VLPEVRGRLGGTVELPCHLLPPTTErvSQVTWQRLDGTvvaafhpsfgvdFPNSQFSKDrlsfvrarpeTNADLRDATLA 117
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSASTGSPG--PDVTWSKEGGT------------LIESLKVKH----------DNGRTTQSSLL 57

                          90       100
                  ....*....|....*....|....*...
gi 228480273  118 FRGLRVEDEGNYTCEFATFPNGTRRGVT 145
Cdd:pfam00047  58 ISNVTKEDAGTYTCVVNNPGGSATLSTS 85
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 204-240 3.09e-03

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: 37.09  E-value: 3.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 228480273 204 QAGTVTIISRYSLVPVGRADGVKVTCRVEHESFEEPI 240
Cdd:cd05771   61 VDGTYSISSYLTLEPGTENRGATYTCRVTHVSLEEPL 97
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 251-324 6.97e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 35.62  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228480273  251 PPEVSISGYDDNWYLGrSEAILTCDVRSNPEPTdYDWS------TTSGVFPASAVAQGSQLLVHSVDRMVNTTFICTATN 324
Cdd:pfam13927   1 KPVITVSPSSVTVREG-ETVTLTCEATGSPPPT-ITWYkngepiSSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 270-334 7.00e-03

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 35.38  E-value: 7.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228480273 270 AILTCDVRSNPEPTdYDWS------TTSGVFPASAVAQGSQLLVHSVDRMVNTTFICTATNAVGTGRAEQV 334
Cdd:cd00096    1 VTLTCSASGNPPPT-ITWYkngkplPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
 
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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