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Conserved domains on  [gi|148664224|ref|NP_694938|]
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junctional adhesion molecule-like isoform 2 [Homo sapiens]

Protein Classification

immunoglobulin domain-containing protein( domain architecture ID 10542315)

immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets, similar to Homo sapiens T-cell antigen CD7 and voltage-gated sodium channel beta3 subunit Ig Domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 15-126 3.38e-22

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: 90.21  E-value: 3.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224   15 VSPPELTVHVGDSALMGCVFQSTEDKCIFKIDWTLSPGEHaKDEYVLYYYSNLSVPiGRFQNRVHLMGDILCNDGSLLLQ 94
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGK-GPTFLIAYYSNGSEE-GVKKGRFSGRGDPSNGDGSLTIQ 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 148664224   95 DVQEADQGTYICEIRLKGEsQVFKKAVVLHVL 126
Cdd:pfam07686  79 NLTLSDSGTYTCAVIPSGE-GVFGKGTRLTVL 109
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 128-241 3.40e-14

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: 68.25  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  128 EEPKELMVHVGGLIQMGCVFQSTEVKHVTKVEWIFSGRRAKEEIVFRYYHKLRMSveysqswGHFQNRVNLVGDIFRNDG 207
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEE-------GVKKGRFSGRGDPSNGDG 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 148664224  208 SIMLQGVRESDGGNYTCSIHLGN-LVFKKTIVLHV 241
Cdd:pfam07686  74 SLTIQNLTLSDSGTYTCAVIPSGeGVFGKGTRLTV 108
 
Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 15-126 3.38e-22

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: 90.21  E-value: 3.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224   15 VSPPELTVHVGDSALMGCVFQSTEDKCIFKIDWTLSPGEHaKDEYVLYYYSNLSVPiGRFQNRVHLMGDILCNDGSLLLQ 94
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGK-GPTFLIAYYSNGSEE-GVKKGRFSGRGDPSNGDGSLTIQ 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 148664224   95 DVQEADQGTYICEIRLKGEsQVFKKAVVLHVL 126
Cdd:pfam07686  79 NLTLSDSGTYTCAVIPSGE-GVFGKGTRLTVL 109
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 128-241 3.40e-14

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: 68.25  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  128 EEPKELMVHVGGLIQMGCVFQSTEVKHVTKVEWIFSGRRAKEEIVFRYYHKLRMSveysqswGHFQNRVNLVGDIFRNDG 207
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEE-------GVKKGRFSGRGDPSNGDG 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 148664224  208 SIMLQGVRESDGGNYTCSIHLGN-LVFKKTIVLHV 241
Cdd:pfam07686  74 SLTIQNLTLSDSGTYTCAVIPSGeGVFGKGTRLTV 108
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 130-226 4.74e-12

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 62.45  E-value: 4.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224 130 PKELMVHVGGLIQMGCVFQSTEVKH-VTKVEWIFSGRRAKEEIVFRYYHKLRMsveYSQSWGHFQNRVNLVGDIFRNDGS 208
Cdd:cd05715    6 PRELNVLNGSDVRLTCTFTSCYTVGdAFSVTWTYQPEGGNTTESMFHYSKGKP---YILKVGRFKDRVSWAGNPSKKDAS 82

                         90
                 ....*....|....*...
gi 148664224 209 IMLQGVRESDGGNYTCSI 226
Cdd:cd05715   83 IVISNLQFSDNGTYTCDV 100
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 16-109 6.54e-12

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 61.77  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  16 SPPELTVHVGDSALMGCVFQSTE---DKCIfkIDWTLSPGEHAKDEYVLYYYSNLSVPI-GRFQNRVHLMGDILCNDGSL 91
Cdd:cd05880    5 TSKEVEAVNGTDVRLKCTFSSSApigDTLV--ITWNFRPLDGGREESVFYYHKRPYPPPdGRFKGRVVWDGNIMRRDASI 82

                         90
                 ....*....|....*...
gi 148664224  92 LLQDVQEADQGTYICEIR 109
Cdd:cd05880   83 LIWQLQPTDNGTYTCQVK 100
IGv smart00406
Immunoglobulin V-Type;
182-226 1.63e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 36.98  E-value: 1.63e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 148664224   182 SVEYSQSWghFQNRVNLVGDIFRNDGSIMLQGVRESDGGNYTCSI 226
Cdd:smart00406  39 GSSYYQES--YKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
IGv smart00406
Immunoglobulin V-Type;
58-108 8.71e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 35.05  E-value: 8.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 148664224    58 EYVLYYYSNLSVPI-GRFQNRVHLMGDILCNDGSLLLQDVQEADQGTYICEI 108
Cdd:smart00406  30 EWLGYIGSNGSSYYqESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
 
Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 15-126 3.38e-22

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: 90.21  E-value: 3.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224   15 VSPPELTVHVGDSALMGCVFQSTEDKCIFKIDWTLSPGEHaKDEYVLYYYSNLSVPiGRFQNRVHLMGDILCNDGSLLLQ 94
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGK-GPTFLIAYYSNGSEE-GVKKGRFSGRGDPSNGDGSLTIQ 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 148664224   95 DVQEADQGTYICEIRLKGEsQVFKKAVVLHVL 126
Cdd:pfam07686  79 NLTLSDSGTYTCAVIPSGE-GVFGKGTRLTVL 109
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 128-241 3.40e-14

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: 68.25  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  128 EEPKELMVHVGGLIQMGCVFQSTEVKHVTKVEWIFSGRRAKEEIVFRYYHKLRMSveysqswGHFQNRVNLVGDIFRNDG 207
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEE-------GVKKGRFSGRGDPSNGDG 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 148664224  208 SIMLQGVRESDGGNYTCSIHLGN-LVFKKTIVLHV 241
Cdd:pfam07686  74 SLTIQNLTLSDSGTYTCAVIPSGeGVFGKGTRLTV 108
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 130-226 4.74e-12

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 62.45  E-value: 4.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224 130 PKELMVHVGGLIQMGCVFQSTEVKH-VTKVEWIFSGRRAKEEIVFRYYHKLRMsveYSQSWGHFQNRVNLVGDIFRNDGS 208
Cdd:cd05715    6 PRELNVLNGSDVRLTCTFTSCYTVGdAFSVTWTYQPEGGNTTESMFHYSKGKP---YILKVGRFKDRVSWAGNPSKKDAS 82

                         90
                 ....*....|....*...
gi 148664224 209 IMLQGVRESDGGNYTCSI 226
Cdd:cd05715   83 IVISNLQFSDNGTYTCDV 100
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 16-109 6.54e-12

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 61.77  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  16 SPPELTVHVGDSALMGCVFQSTE---DKCIfkIDWTLSPGEHAKDEYVLYYYSNLSVPI-GRFQNRVHLMGDILCNDGSL 91
Cdd:cd05880    5 TSKEVEAVNGTDVRLKCTFSSSApigDTLV--ITWNFRPLDGGREESVFYYHKRPYPPPdGRFKGRVVWDGNIMRRDASI 82

                         90
                 ....*....|....*...
gi 148664224  92 LLQDVQEADQGTYICEIR 109
Cdd:cd05880   83 LIWQLQPTDNGTYTCQVK 100
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 17-109 1.25e-11

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 61.29  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  17 PPELTVHVGDSALMGCVFQSTE---DKciFKIDWTLSPgEHAKDEYVLYYYSNLSVPI---GRFQNRVHLMGDILCNDGS 90
Cdd:cd05715    6 PRELNVLNGSDVRLTCTFTSCYtvgDA--FSVTWTYQP-EGGNTTESMFHYSKGKPYIlkvGRFKDRVSWAGNPSKKDAS 82

                         90
                 ....*....|....*....
gi 148664224  91 LLLQDVQEADQGTYICEIR 109
Cdd:cd05715   83 IVISNLQFSDNGTYTCDVK 101
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 130-226 4.08e-10

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 56.76  E-value: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224 130 PKELMVHVGGLIQMGCVFQSTE-VKHVTKVEWIFSGRR-AKEEIVFrYYHKlrmsVEYSQSWGHFQNRVNLVGDIFRNDG 207
Cdd:cd05880    6 SKEVEAVNGTDVRLKCTFSSSApIGDTLVITWNFRPLDgGREESVF-YYHK----RPYPPPDGRFKGRVVWDGNIMRRDA 80

                         90
                 ....*....|....*....
gi 148664224 208 SIMLQGVRESDGGNYTCSI 226
Cdd:cd05880   81 SILIWQLQPTDNGTYTCQV 99
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 121-226 4.18e-08

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: 50.91  E-value: 4.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224 121 VVLHVLPEEPKELmvhvGGLIQMGCVFQSTEVKHVTKVEWIFSGRRAKEEIVFrYYHKLRMSVEYSQswghfQNRVNLVG 200
Cdd:cd05718    1 QRVQVPTEVTGFL----GGSVTLPCSLTSPGTTKITQVTWMKIGAGSSQNVAV-FHPQYGPSVPNPY-----AERVEFLA 70

                         90       100
                 ....*....|....*....|....*..
gi 148664224 201 DIFR-NDGSIMLQGVRESDGGNYTCSI 226
Cdd:cd05718   71 ARLGlRNATLRIRNLRVEDEGNYICEF 97
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 24-109 4.93e-08

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


Pssm-ID: 409552  Cd Length: 114  Bit Score: 50.91  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  24 VGDSALMGCVFQ-STEDKCIFKIDWTLSPGEHAKDEYVLYY----YSNLSVPIgrfQNRVHLMGDILCNDGSLLLQDVQE 98
Cdd:cd20960   14 AGENVTLPCHHQlGLEDQGTLDIEWLLLPSDKVEKVVITYSgdrvYNHYYPAL---KGRVAFTSNDLSGDASLNISNLKL 90

                         90
                 ....*....|.
gi 148664224  99 ADQGTYICEIR 109
Cdd:cd20960   91 SDTGTYQCKVK 101
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 130-226 3.32e-07

Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 48.72  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224 130 PKELMVHVGGLIQMGCVFQSTE-VKHVTKVEWIFSGRRAKEEIVFRYYHKlrmSVEYSQSWGHFQNRVNLVGDIFRNDGS 208
Cdd:cd05879    6 DREVYGTVGSDVTLSCSFWSSEwISDDISFTWHYQPDGSRDAISIFHYGK---GQPYIDNVGPFKERIEWVGNPSRKDGS 82

                         90
                 ....*....|....*...
gi 148664224 209 IMLQGVRESDGGNYTCSI 226
Cdd:cd05879   83 IVIHNLDYTDNGTFTCDV 100
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 16-109 8.69e-06

Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 44.48  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  16 SPPELTVHVGDSALMGCVFQSTE---DKCIFKidWTLSPgEHAKDEYVLYYYSN-LSVP--IGRFQNRVHLMGDILCNDG 89
Cdd:cd05879    5 TDREVYGTVGSDVTLSCSFWSSEwisDDISFT--WHYQP-DGSRDAISIFHYGKgQPYIdnVGPFKERIEWVGNPSRKDG 81

                         90       100
                 ....*....|....*....|
gi 148664224  90 SLLLQDVQEADQGTYICEIR 109
Cdd:cd05879   82 SIVIHNLDYTDNGTFTCDVK 101
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 16-106 5.29e-05

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 41.94  E-value: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  16 SPPELTVHVGDSALMGCVFQSTedkciFKIDWTL----SPGEHAkdEYVLYYYSNLSVPIGRFQNRVHLMGDiLCNDGSL 91
Cdd:cd00099    4 SPRSLSVQEGESVTLSCEVSSS-----FSSTYIYwyrqKPGQGP--EFLIYLSSSKGKTKGGVPGRFSGSRD-GTSSFSL 75

                         90
                 ....*....|....*
gi 148664224  92 LLQDVQEADQGTYIC 106
Cdd:cd00099   76 TISNLQPEDSGTYYC 90
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 16-108 1.29e-04

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: 41.16  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  16 SPPELTVHVGDSALMGCVFQ---STEDKCIFKIDWTLSPGEHAKDEYVLYYYSNLSVPIGRFQNRVHLMGDILcNDGSLL 92
Cdd:cd05877    3 VQAKVFSHRGGNVTLPCRYHyepELSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADD-LDASLV 81

                         90
                 ....*....|....*.
gi 148664224  93 LQDVQEADQGTYICEI 108
Cdd:cd05877   82 ITDLRLEDYGRYRCEV 97
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 15-106 3.06e-04

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 39.68  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  15 VSPPELTVHVGDSALMGCVFQSTEDKCIFkidWtlspgEHAKDEYVL--YYYS--NLSVPIGRFQNRVHLMGDILCN-DG 89
Cdd:cd16091    2 VSEVIVVCLLSEDCILPCSFTPGSEVVIH---W-----YKQDSDIKVhsYYYGkdQLESQDQRYRNRTSLFKDQISNgNA 73

                         90
                 ....*....|....*..
gi 148664224  90 SLLLQDVQEADQGTYIC 106
Cdd:cd16091   74 SLLLRRVQLQDEGRYKC 90
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 127-226 8.25e-04

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: 38.85  E-value: 8.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224 127 PEEPKELMVHVGGLIQMGCVFQ---STEVKHVTKVEWI-FSGRRAKEEIVF---RYYHKlrmsveysqSWGHFQNRVNLV 199
Cdd:cd05877    1 ETVQAKVFSHRGGNVTLPCRYHyepELSAPRKIRVKWTkLEVDYAKEEDVLvaiGTRHK---------SYGSYQGRVFLR 71

                         90       100
                 ....*....|....*....|....*..
gi 148664224 200 GDiFRNDGSIMLQGVRESDGGNYTCSI 226
Cdd:cd05877   72 RA-DDLDASLVITDLRLEDYGRYRCEV 97
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 17-108 1.62e-03

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: 37.81  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224  17 PPELTVHVGDSALMGCVFQSTEDKCIFKIDWTLspgEHAKDEYVLYYYS---NLSVPiGRFQNRVHLMGDIL-CNDGSLL 92
Cdd:cd05718    6 PTEVTGFLGGSVTLPCSLTSPGTTKITQVTWMK---IGAGSSQNVAVFHpqyGPSVP-NPYAERVEFLAARLgLRNATLR 81

                         90
                 ....*....|....*.
gi 148664224  93 LQDVQEADQGTYICEI 108
Cdd:cd05718   82 IRNLRVEDEGNYICEF 97
IGv smart00406
Immunoglobulin V-Type;
182-226 1.63e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 36.98  E-value: 1.63e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 148664224   182 SVEYSQSWghFQNRVNLVGDIFRNDGSIMLQGVRESDGGNYTCSI 226
Cdd:smart00406  39 GSSYYQES--YKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 70-107 2.38e-03

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 36.60  E-value: 2.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 148664224  70 PIGRFQNRvhlmgdilcNDGSLLLQDVQEADQGTYICE 107
Cdd:cd05725   39 PKGRYEIL---------DDHSLKIRKVTAGDMGSYTCV 67
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 145-224 7.83e-03

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 35.83  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664224 145 CVFQST--EVKHvtkveWIfsgrRAKEEI-VFRYYHKlrmSVEYSQSWGHFQNRVNLVGDIFRN-DGSIMLQGVRESDGG 220
Cdd:cd16091   19 CSFTPGseVVIH-----WY----KQDSDIkVHSYYYG---KDQLESQDQRYRNRTSLFKDQISNgNASLLLRRVQLQDEG 86


                 ....
gi 148664224 221 NYTC 224
Cdd:cd16091   87 RYKC 90
IGv smart00406
Immunoglobulin V-Type;
58-108 8.71e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 35.05  E-value: 8.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 148664224    58 EYVLYYYSNLSVPI-GRFQNRVHLMGDILCNDGSLLLQDVQEADQGTYICEI 108
Cdd:smart00406  30 EWLGYIGSNGSSYYqESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCAV 81
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 187-241 9.72e-03

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: 35.17  E-value: 9.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 148664224   187 QSWGHFQNRVNLVGDifRNDGSIMLQGVRESDGGNYTCSIHLGNLVFKKTIVLHV 241
Cdd:smart00410  33 GKLLAESGRFSVSRS--GSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
 
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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