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Conserved domains on  [gi|1622891583|ref|XP_028694292|]
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nectin-2 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 34-158 4.48e-63

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: 201.65  E-value: 4.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDappDHQNVAAFHPKMGPSFPSPkpgsERLSFVSAKQstr 113
Cdd:cd20989     1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHD---EHGSVAVFHPKQGPSFPES----ERLSFVAARL--- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622891583 114 qdtEAELQDATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd20989    71 ---GAELRNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 261-346 1.97e-55

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: 180.84  E-value: 1.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 261 PEVSISGYDDNWYLGRTDATLSCDVHSNPEPTGYDWSTTSGIFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRA 340
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                  ....*.
gi 1622891583 341 EQVIFV 346
Cdd:cd20930    81 EQTIFV 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 162-258 7.42e-52

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: 171.82  E-value: 7.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 162 PQNHAEAQEVTFSQDPVPVARCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVE 241
Cdd:cd07703     1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                          90
                  ....*....|....*..
gi 1622891583 242 HESFEEPALIPVTLSVR 258
Cdd:cd07703    81 HETLEEPQLLPVTLSVR 97
 
Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 34-158 4.48e-63

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: 201.65  E-value: 4.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDappDHQNVAAFHPKMGPSFPSPkpgsERLSFVSAKQstr 113
Cdd:cd20989     1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHD---EHGSVAVFHPKQGPSFPES----ERLSFVAARL--- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622891583 114 qdtEAELQDATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd20989    71 ---GAELRNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 261-346 1.97e-55

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: 180.84  E-value: 1.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 261 PEVSISGYDDNWYLGRTDATLSCDVHSNPEPTGYDWSTTSGIFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRA 340
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                  ....*.
gi 1622891583 341 EQVIFV 346
Cdd:cd20930    81 EQTIFV 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 162-258 7.42e-52

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: 171.82  E-value: 7.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 162 PQNHAEAQEVTFSQDPVPVARCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVE 241
Cdd:cd07703     1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                          90
                  ....*....|....*..
gi 1622891583 242 HESFEEPALIPVTLSVR 258
Cdd:cd07703    81 HETLEEPQLLPVTLSVR 97
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 164-249 3.96e-17

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 76.30  E-value: 3.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 164 NHAEAQEVTFS-QDPVPVARCISKEGRPPARISWLSSLD--WEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKV 240
Cdd:pfam08205   1 PTIEPPASLLEgEGPEVVATCSSAGGKPAPRITWYLDGKplEAAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQV 80


                  ....*....
gi 1622891583 241 EHESFEEPA 249
Cdd:pfam08205  81 SYGALRGSI 89
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 37-158 5.87e-11

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: 59.39  E-value: 5.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  37 QVLPEVRGQLGGTVELPCHLLPPVPGlYISLVTW--QRPDAPPDHQnVAAFHPKMGPSFPSPKpgserlsfVSAKQSTRQ 114
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSE-ASTSVYWyrQPPGKGPTFL-IAYYSNGSEEGVKKGR--------FSGRGDPSN 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622891583 115 dteaelQDATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:pfam07686  71 ------GDGSLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
49-142 1.03e-07

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 49.30  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583   49 TVELPCHLLPPVPGLYIslVTWQRPdaPPDHQN-VAAFHPKMGPSFPSPKPgSERLSFVSAKQSTrqdteaelqDATLAL 127
Cdd:smart00406   1 SVTLSCKFSGSTFSSYY--VSWVRQ--PPGKGLeWLGYIGSNGSSYYQESY-KGRFTISKDTSKN---------DVSLTI 66

                           90
                   ....*....|....*
gi 1622891583  128 RGLTVEDEGNYTCEF 142
Cdd:smart00406  67 SNLRVEDTGTYYCAV 81
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 260-333 2.48e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 260 PPEVSISGYDDNWYLGRTdATLSCDVHSNPEPTgYDWS------TTSGIFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTN 333
Cdd:pfam13927   1 KPVITVSPSSVTVREGET-VTLTCEATGSPPPT-ITWYkngepiSSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
 
Name Accession Description Interval E-value
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 34-158 4.48e-63

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: 201.65  E-value: 4.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDappDHQNVAAFHPKMGPSFPSPkpgsERLSFVSAKQstr 113
Cdd:cd20989     1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHD---EHGSVAVFHPKQGPSFPES----ERLSFVAARL--- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622891583 114 qdtEAELQDATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd20989    71 ---GAELRNASLAMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
Ig3_Nectin-5_like cd20930
Third immunoglobulin domain of Nectin-like Protein-5, and similar domains; The members here ...
 261-346 1.97e-55

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: 180.84  E-value: 1.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 261 PEVSISGYDDNWYLGRTDATLSCDVHSNPEPTGYDWSTTSGIFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRA 340
Cdd:cd20930     1 PEVSISGYDDNWYLGRNEATLTCDVRSNPEPTGYDWSTTSGPFPTSAVAQGPQLLIHSVDRLVNTTFICTVTNAVGTGRA 80


                  ....*.
gi 1622891583 341 EQVIFV 346
Cdd:cd20930    81 EQTIFV 86
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 34-158 5.51e-52

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


Pssm-ID: 409383  Cd Length: 113  Bit Score: 172.63  E-value: 5.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  34 VRVQVLPEVRGQLGGTVELPCHLLPPVPgLYISLVTWQRPDAPpDHQNVAAFHPKMGPSFPSPKpgSERLSFVSAKQstr 113
Cdd:cd05718     1 QRVQVPTEVTGFLGGSVTLPCSLTSPGT-TKITQVTWMKIGAG-SSQNVAVFHPQYGPSVPNPY--AERVEFLAARL--- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622891583 114 qdteaELQDATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd05718    74 -----GLRNATLRIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 162-258 7.42e-52

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: 171.82  E-value: 7.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 162 PQNHAEAQEVTFSQDPVPVARCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVE 241
Cdd:cd07703     1 PKNSAEAQEVQAGGIPVPVARCVSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLVPTPEANGKEVTCKVE 80

                          90
                  ....*....|....*..
gi 1622891583 242 HESFEEPALIPVTLSVR 258
Cdd:cd07703    81 HETLEEPQLLPVTLSVR 97
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 162-257 6.82e-40

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: 139.94  E-value: 6.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 162 PQNHAEAQEVTF-SQDPVPVARCISKEGRPPARISWLSSLDWEAKETQVSGTlAGTVTVTSRFTLVPSGRADGVTVTCKV 240
Cdd:cd05719     1 PTNSLEGGPALLiGGEPTLVATCISANGKPPASVTWETDLKGEASTTQVRGS-NGTVTVTSRYRLVPSREADGQPLTCVV 79

                          90
                  ....*....|....*..
gi 1622891583 241 EHESFEEPALIPVTLSV 257
Cdd:cd05719    80 EHPSLEKDQRISVTLNV 96
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 164-249 3.96e-17

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 76.30  E-value: 3.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 164 NHAEAQEVTFS-QDPVPVARCISKEGRPPARISWLSSLD--WEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKV 240
Cdd:pfam08205   1 PTIEPPASLLEgEGPEVVATCSSAGGKPAPRITWYLDGKplEAAETSSEQDPESGLVTVTSELKLVPSRSDHGQSLTCQV 80


                  ....*....
gi 1622891583 241 EHESFEEPA 249
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 ...
 36-149 7.20e-16

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


Pssm-ID: 409469  Cd Length: 113  Bit Score: 73.85  E-value: 7.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  36 VQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPdAPPDHQNVAAFHPKMGPSFPSPKpgSERLSFVSAKqstrqd 115
Cdd:cd05886     3 VQVNDSMSGFIGTDVVLHCSFANPLPSVKITQVTWQKS-TNGSKQNVAIYNPSMGVSVLPPY--RERVTFLNPS------ 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622891583 116 teaeLQDATLALRGLTVEDEGNYTCEFATFPKGS 149
Cdd:cd05886    74 ----FTDGTIRLSRLELEDEGVYICEFATFPTGN 103
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 43-158 5.13e-13

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


Pssm-ID: 409433  Cd Length: 108  Bit Score: 65.44  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  43 RGQLGGTVELPCHLLPPVPglyISLVTWQRpDAPPDHQNVAAFHPKMG-PSFPSPKpgsERLSFvsakqstrqdTEAELQ 121
Cdd:cd05846     9 RAVLGGNATLSCNLTLPEE---VLQVTWQK-IKASSPENIVTYSKKYGvKIQPSYV---RRISF----------TSSGLN 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622891583 122 DATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:cd05846    72 STSITIWNVTLEDEGCYKCLFNTFPDGIKSGTACLTV 108
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 37-158 5.87e-11

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: 59.39  E-value: 5.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  37 QVLPEVRGQLGGTVELPCHLLPPVPGlYISLVTW--QRPDAPPDHQnVAAFHPKMGPSFPSPKpgserlsfVSAKQSTRQ 114
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSE-ASTSVYWyrQPPGKGPTFL-IAYYSNGSEEGVKKGR--------FSGRGDPSN 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622891583 115 dteaelQDATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRV 158
Cdd:pfam07686  71 ------GDGSLTIQNLTLSDSGTYTCAVIPSGEGVFGKGTRLTV 108
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
 180-257 2.69e-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: 57.14  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 180 VARCISKEGRPPARISWlsslDWEAKETQVSGTL--AGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPVTLSV 257
Cdd:cd07704    21 AASCTAETGKPAASVTW----ETDLGGMESSRTFehNRTATVTSEYHLVPTRFANGRPLTCVVSHPALQQDIRITHILDV 96
IgC1_2_Nectin-1_like cd05890
Second immunoglobulin (Ig) domain of nectin-1, and similar domains; member of the C1-set of Ig ...
 153-243 4.04e-09

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: 53.84  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 153 MTWLRVIAKPQNHAEAQEvtfsqDPVPVARCISKEGRPPARISWLSSLDWEAkETQVSGTLAGTVTVTSRFTLVPSGRAD 232
Cdd:cd05890     2 TNRMEGTTAVLRAKKGQD-----DKVLVATCTSANGKPPSVVSWDTRLKGEA-EFQEIRNPNGTVTVISRYRLVPSREAH 75

                          90
                  ....*....|.
gi 1622891583 233 GVTVTCKVEHE 243
Cdd:cd05890    76 QQSLACIVNYH 86
IGv smart00406
Immunoglobulin V-Type;
49-142 1.03e-07

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 49.30  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583   49 TVELPCHLLPPVPGLYIslVTWQRPdaPPDHQN-VAAFHPKMGPSFPSPKPgSERLSFVSAKQSTrqdteaelqDATLAL 127
Cdd:smart00406   1 SVTLSCKFSGSTFSSYY--VSWVRQ--PPGKGLeWLGYIGSNGSSYYQESY-KGRFTISKDTSKN---------DVSLTI 66

                           90
                   ....*....|....*
gi 1622891583  128 RGLTVEDEGNYTCEF 142
Cdd:smart00406  67 SNLRVEDTGTYYCAV 81
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 38-159 4.09e-07

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: 48.78  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  38 VLPEVRGQLGGTVELPCHLLPPVPglyISLVTWQRPdAPPDHQNVAAFHPKMGPSFPSPKPGseRLSFVSAkqstrqdte 117
Cdd:cd05887     5 VEPHVTAVWGKNVSLKCLIEVNET---ITQISWEKI-HGKSSQTVAVHHPQYGISIQGEYQG--RVSFKNY--------- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622891583 118 aELQDATLALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRVI 159
Cdd:cd05887    70 -SLNDATITLHNVGFSDSGKYICKAVTFPLGNAQSSTTVTVL 110
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 46-159 2.94e-06

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: 46.05  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  46 LGGTVELPCHLLPPvPGLYISLVTWQRPDAPPDHQNVAAFHPKMGPSfpspkpgserlSFVSAKQSTRQDTEAELQDATL 125
Cdd:cd05888     7 LGQDAKLPCFYRGD-SGEQVGQVAWARVDAGEGAQEIALLHSKYGLH-----------VFPAYEGRVEQPPPPRPADGSV 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622891583 126 ALRGLTVEDEGNYTCEFATFPKGSVRGMTWLRVI 159
Cdd:cd05888    75 LLRNAVQADEGEYECRVSTFPAGNFQAELRLRVL 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 40-158 7.69e-06

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 44.42  E-value: 7.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583   40 PEVRGQLGGTVELPCHllppVPGLYISLVTWQRPDappdhqnvaafhpkmgpsfPSPKPGSERLSFvsakqsTRQDTEAE 119
Cdd:smart00410   2 PSVTVKEGESVTLSCE----ASGSPPPEVTWYKQG-------------------GKLLAESGRFSV------SRSGSTST 52

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622891583  120 LQdatlaLRGLTVEDEGNYTCEfATFPKGSVRGMTWLRV 158
Cdd:smart00410  53 LT-----ISNVTPEDSGTYTCA-ATNSSGSASSGTTLTV 85
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 37-159 8.27e-06

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


Pssm-ID: 409472  Cd Length: 111  Bit Score: 44.85  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  37 QVLPEVRGQLGGTVELPChlLPPVPGLyISLVTWQRpdAPPDHQNVAAFHPKMGPSFPSPKPGseRLSFvsakqstrQDT 116
Cdd:cd05889     4 EVLWDTSVPLSENMSLEC--VYPSTGI-LTQVEWTK--IGGQKDNIAVYHPTHGMHIRKPYAG--RVYF--------LNS 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622891583 117 EAELQDATLALRGLTVEDEGNYTCEFATFPKGSvrgmtWLRVI 159
Cdd:cd05889    69 TMASNNMSLSFRNASEDDVGYYSCSLYTYPQGS-----WEKVI 106
IgC1 cd00098
Immunoglobulin Constant-1 (C1)-set domain; The members here are composed of C1-set domains, ...
 190-253 5.14e-05

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


Pssm-ID: 409354  Cd Length: 95  Bit Score: 42.06  E-value: 5.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891583 190 PPARISWL---SSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPV 253
Cdd:cd00098    29 KDITVTWLkngVPLTSGVSTSSPVEPNDGTYSVTSSLTVPPSDWDEGATYTCVVTHESLKSPLSKTW 95
IgI_2_Necl-1 cd07705
Second immunoglobulin (Ig)-like domain of nectin-like molcule-1 (Necl-1); member of the I-set ...
 182-249 5.90e-05

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


Pssm-ID: 409502  Cd Length: 103  Bit Score: 42.26  E-value: 5.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 182 RCISKEGRPPARISWLSS-LDWEAKETQVSGTLAG-TVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPA 249
Cdd:cd07705    25 RCTSSGSKPAANIKWRKGdQELEGAPTSVQEDGNGkTFTVSSSVEFQVTREDDGAEITCSVGHESLHDSD 94
IgI_2_Necl-1-4 cd05761
Second immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 - Necl-4; member of ...
 183-244 8.91e-05

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


Pssm-ID: 409418  Cd Length: 102  Bit Score: 41.65  E-value: 8.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622891583 183 CISKEGRPPARISWLSSlDWE---AKETQVSGTlAGTVTVTSRFTLVPSGRADGVTVTCKVEHES 244
Cdd:cd05761    26 CTTSGSKPAADIRWFKN-DKElkgVKEVQESGA-GKTFTVTSTLRFRVDRDDDGVAVICRVDHES 88
IgI_2_Necl-3 cd05884
Second immunoglobulin (Ig)-like domain of nectin-like molecule-3 (Necl-3); member of the I-set ...
 183-244 1.56e-04

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


Pssm-ID: 409467  Cd Length: 104  Bit Score: 41.07  E-value: 1.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622891583 183 CISKEGRPPARISWLSSlDWE---AKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHES 244
Cdd:cd05884    27 CKTSGSKPAADIRWFKN-DKEvkdVKYLKAEDANRKTFTVSSSLDFHVDRDDDGVAITCRVDHES 90
IgC1_Tapasin_R cd05771
Tapasin-R immunoglobulin-like domain; member of the C1-set of Ig superfamily (IgSF) domains; ...
 214-248 7.95e-04

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


Pssm-ID: 409428  Cd Length: 100  Bit Score: 39.02  E-value: 7.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622891583 214 AGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEP 248
Cdd:cd05771    62 DGTYSISSYLTLEPGTENRGATYTCRVTHVSLEEP 96
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 279-343 1.11e-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: 37.69  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622891583 279 ATLSCDVHSNPEPTgYDWS------TTSGIFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQV 343
Cdd:cd00096     1 VTLTCSASGNPPPT-ITWYkngkplPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 260-333 2.48e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583 260 PPEVSISGYDDNWYLGRTdATLSCDVHSNPEPTgYDWS------TTSGIFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTN 333
Cdd:pfam13927   1 KPVITVSPSSVTVREGET-VTLTCEATGSPPPT-ITWYkngepiSSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 40-141 4.33e-03

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409482  Cd Length: 128  Bit Score: 37.63  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891583  40 PEVRGQLGGTVELPCHL--LPPVPGLY--------ISLVTWQRPDAPPDHQNVAAFHPKMGpsfpSPKPGSERLSFVSAK 109
Cdd:cd05901     5 SRVHGSLSGSVVLPCRFstLPTLPPSYnitseflrIKWTKIQVDKNGKDHKETTVLVAQNG----IIKIGQEYMGRVSVP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622891583 110 qstrqdTEAELQ-DATLALRGLTVEDEGNYTCE 141
Cdd:cd05901    81 ------SHPEDQgDASLTIVKLRASDAGVYRCE 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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