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Conserved domains on  [gi|2462509344|ref|XP_054192651|]
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myelin protein P0 isoform X1 [Homo sapiens]

Protein Classification

immunoglobulin domain-containing family protein; immunoglobulin domain-containing protein( domain architecture ID 10147190)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets| immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and/or pattern recognition

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 40-156 2.48e-84

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: 246.33  E-value: 2.48e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  40 IVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPRWKD 119
Cdd:cd05879     1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462509344 120 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 156
Cdd:cd05879    81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
Myelin-PO_C super family cl11197
Myelin-PO cytoplasmic C-term p65 binding region; Myelin protein zero is the major myelin ...
 194-225 3.69e-15

Myelin-PO cytoplasmic C-term p65 binding region; Myelin protein zero is the major myelin protein in the peripheral central nervous system and is essential for normal myelination. The family is a single-pass transmembrane molecule containing one Ig-like loop in the extracellular domain and this highly basic 69 residue C-terminal cytoplasmic domain which is the region that interacts with protein p65.


The actual alignment was detected with superfamily member pfam10570:

Pssm-ID: 287532  Cd Length: 65  Bit Score: 67.77  E-value: 3.69e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462509344 194 LRRQAALQRRLSAMEKGKLHKPGKDASKRGRQ 225
Cdd:pfam10570   1 LRRQAFPQRDLSAVEKGKLHKPAKDSSKRGRQ 32
 
Name Accession Description Interval E-value
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 40-156 2.48e-84

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: 246.33  E-value: 2.48e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  40 IVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPRWKD 119
Cdd:cd05879     1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462509344 120 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 156
Cdd:cd05879    81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-156 1.02e-24

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: 94.06  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  43 YTDREVHGAVGSRVTLHCSFWSSeWVSDDISFTWRYQPEGGRDAISIFHYAKGQPyideVGTFKERIQWVGDPRWKDGSI 122
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYSNGSE----EGVKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462509344 123 VIHNLDYSDNGTFTCDVkNPPDIVGKTSQVTLYV 156
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
56-139 3.27e-16

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 70.87  E-value: 3.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344   56 VTLHCSFWSSEWVsdDISFTWRYQPEGGRDAISIFHYAKGQPYIDEvgTFKERIQWVGDPRWKDGSIVIHNLDYSDNGTF 135
Cdd:smart00406   2 VTLSCKFSGSTFS--SYYVSWVRQPPGKGLEWLGYIGSNGSSYYQE--SYKGRFTISKDTSKNDVSLTISNLRVEDTGTY 77


                   ....
gi 2462509344  136 TCDV 139
Cdd:smart00406  78 YCAV 81
Myelin-PO_C pfam10570
Myelin-PO cytoplasmic C-term p65 binding region; Myelin protein zero is the major myelin ...
 194-225 3.69e-15

Myelin-PO cytoplasmic C-term p65 binding region; Myelin protein zero is the major myelin protein in the peripheral central nervous system and is essential for normal myelination. The family is a single-pass transmembrane molecule containing one Ig-like loop in the extracellular domain and this highly basic 69 residue C-terminal cytoplasmic domain which is the region that interacts with protein p65.


Pssm-ID: 287532  Cd Length: 65  Bit Score: 67.77  E-value: 3.69e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462509344 194 LRRQAALQRRLSAMEKGKLHKPGKDASKRGRQ 225
Cdd:pfam10570   1 LRRQAFPQRDLSAVEKGKLHKPAKDSSKRGRQ 32
 
Name Accession Description Interval E-value
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
 40-156 2.48e-84

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: 246.33  E-value: 2.48e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  40 IVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPRWKD 119
Cdd:cd05879     1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462509344 120 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 156
Cdd:cd05879    81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 40-156 2.09e-68

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: 206.13  E-value: 2.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  40 IVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPRWKD 119
Cdd:cd05715     1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462509344 120 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 156
Cdd:cd05715    81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
 40-156 3.21e-32

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: 113.77  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  40 IVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKgQPYIDEVGTFKERIQWVGDPRWKD 119
Cdd:cd05880     1 IEVYTSKEVEAVNGTDVRLKCTFSSSAPIGDTLVITWNFRPLDGGREESVFYYHK-RPYPPPDGRFKGRVVWDGNIMRRD 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462509344 120 GSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYV 156
Cdd:cd05880    80 ASILIWQLQPTDNGTYTCQVKNPPDVHGPIGEIRLRV 116
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-156 1.02e-24

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: 94.06  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  43 YTDREVHGAVGSRVTLHCSFWSSeWVSDDISFTWRYQPEGGRDAISIFHYAKGQPyideVGTFKERIQWVGDPRWKDGSI 122
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSS-MSEASTSVYWYRQPPGKGPTFLIAYYSNGSE----EGVKKGRFSGRGDPSNGDGSL 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462509344 123 VIHNLDYSDNGTFTCDVkNPPDIVGKTSQVTLYV 156
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAV-IPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
56-139 3.27e-16

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 70.87  E-value: 3.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344   56 VTLHCSFWSSEWVsdDISFTWRYQPEGGRDAISIFHYAKGQPYIDEvgTFKERIQWVGDPRWKDGSIVIHNLDYSDNGTF 135
Cdd:smart00406   2 VTLSCKFSGSTFS--SYYVSWVRQPPGKGLEWLGYIGSNGSSYYQE--SYKGRFTISKDTSKNDVSLTISNLRVEDTGTY 77


                   ....
gi 2462509344  136 TCDV 139
Cdd:smart00406  78 YCAV 81
Myelin-PO_C pfam10570
Myelin-PO cytoplasmic C-term p65 binding region; Myelin protein zero is the major myelin ...
 194-225 3.69e-15

Myelin-PO cytoplasmic C-term p65 binding region; Myelin protein zero is the major myelin protein in the peripheral central nervous system and is essential for normal myelination. The family is a single-pass transmembrane molecule containing one Ig-like loop in the extracellular domain and this highly basic 69 residue C-terminal cytoplasmic domain which is the region that interacts with protein p65.


Pssm-ID: 287532  Cd Length: 65  Bit Score: 67.77  E-value: 3.69e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462509344 194 LRRQAALQRRLSAMEKGKLHKPGKDASKRGRQ 225
Cdd:pfam10570   1 LRRQAFPQRDLSAVEKGKLHKPAKDSSKRGRQ 32
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 47-153 3.02e-10

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: 55.92  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  47 EVHGAVGSRVTLHC--SFWSSEWVSDDISftWRYQPEGGRDAISIFhYAKGQPYIDEVGTFKERIQWVGDPRWKDGSIVI 124
Cdd:cd20960     9 EIKKVAGENVTLPChhQLGLEDQGTLDIE--WLLLPSDKVEKVVIT-YSGDRVYNHYYPALKGRVAFTSNDLSGDASLNI 85

                          90       100
                  ....*....|....*....|....*....
gi 2462509344 125 HNLDYSDNGTFTCDVKNPPDIVGKTSQVT 153
Cdd:cd20960    86 SNLKLSDTGTYQCKVKKAPGYAWSKITLI 114
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 41-157 9.85e-10

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: 54.59  E-value: 9.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  41 VVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKG----QPYIDEVgTFKeriqwvgDPR 116
Cdd:cd05886     2 TVQVNDSMSGFIGTDVVLHCSFANPLPSVKITQVTWQKSTNGSKQNVAIYNPSMGvsvlPPYRERV-TFL-------NPS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462509344 117 WKDGSIVIHNLDYSDNGTFTCDVKNPPdIVGKTSQVTLYVF 157
Cdd:cd05886    74 FTDGTIRLSRLELEDEGVYICEFATFP-TGNRESQLNLTVM 113
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 46-156 4.61e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.43  E-value: 4.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344   46 REVHGAVGSRVTLHCSFWSSEwvsdDISFTWRYQPeggrdaisifhyakgqpyiDEVGTFKERIQWVGDPRwkDGSIVIH 125
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSP----PPEVTWYKQG-------------------GKLLAESGRFSVSRSGS--TSTLTIS 56

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462509344  126 NLDYSDNGTFTCDVKNppDIVGKTSQVTLYV 156
Cdd:smart00410  57 NVTPEDSGTYTCAATN--SSGSASSGTTLTV 85
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 40-156 2.08e-07

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: 48.21  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  40 IVVYTDREVHGAVGSRVTLHCSFWSSEWVSddIS-FTWRYQPEGGRDAISIFHYAKGqpyIDEVGTFKERIQWVGDP-RW 117
Cdd:cd05718     1 QRVQVPTEVTGFLGGSVTLPCSLTSPGTTK--ITqVTWMKIGAGSSQNVAVFHPQYG---PSVPNPYAERVEFLAARlGL 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462509344 118 KDGSIVIHNLDYSDNGTFTCDVKNPPdivGKTSQVTLYV 156
Cdd:cd05718    76 RNATLRIRNLRVEDEGNYICEFATFP---QGNRQGTTWL 111
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 40-143 1.44e-06

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: 45.65  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  40 IVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGrdAISIFHYAKGqPYIDEvgtfKERIQWVG---DPR 116
Cdd:cd20989     1 VRVQVPPEVRGFLGGSVTLPCHLLPPNMVTHVSQVTWQRHDEHG--SVAVFHPKQG-PSFPE----SERLSFVAarlGAE 73

                          90       100
                  ....*....|....*....|....*..
gi 2462509344 117 WKDGSIVIHNLDYSDNGTFTCDVKNPP 143
Cdd:cd20989    74 LRNASLAMFGLRVEDEGNYTCEFATFP 100
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 44-137 5.11e-03

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: 35.77  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  44 TDREVHGAVGSRVTLHCSFwSSEWVSDDISftWrYQPEGGRDAISIFHYAKGQPYIDevGTFKERIQWVGDPRwKDGSIV 123
Cdd:cd00099     4 SPRSLSVQEGESVTLSCEV-SSSFSSTYIY--W-YRQKPGQGPEFLIYLSSSKGKTK--GGVPGRFSGSRDGT-SSFSLT 76

                          90
                  ....*....|....
gi 2462509344 124 IHNLDYSDNGTFTC 137
Cdd:cd00099    77 ISNLQPEDSGTYYC 90
IgV_1_CD4 cd07690
First immunoglobulin (Ig) domain of Cluster of Differentiation (CD) 4; member of the V-set of ...
 48-156 5.61e-03

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


Pssm-ID: 409487  Cd Length: 97  Bit Score: 35.22  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  48 VHGAVGSRVTLHCSfwSSEWVSddISFTWRYQpeggrDAISIFHYakgQPYIDEVGTFKERIQWvgDPR---WKDGS--I 122
Cdd:cd07690     4 VLGKKGDTAELPCT--ASQKKS--IQFHWKNS-----NQIKILGN---QGSFLTKGPSKLNDRA--DSRrnlWDQGSfpL 69

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462509344 123 VIHNLDYSDNGTFTCDVKNppdivgKTSQVTLYV 156
Cdd:cd07690    70 IIKNLKIEDSDTYICEVED------KKEEVELLV 97
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 39-154 5.75e-03

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: 35.40  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  39 AIVVYTDREVhgAVGSRVTLHCSFWSSEWVsddISFTWRYQPEGGRDAISIFHYAKGQPYIdevGTFKERIQwVGDPRWK 118
Cdd:cd05846     1 VVVHTGDTRA--VLGGNATLSCNLTLPEEV---LQVTWQKIKASSPENIVTYSKKYGVKIQ---PSYVRRIS-FTSSGLN 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462509344 119 DGSIVIHNLDYSDNGTFTCDVKNPPD-IVGKTSQVTL 154
Cdd:cd05846    72 STSITIWNVTLEDEGCYKCLFNTFPDgIKSGTACLTV 108
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 52-152 9.36e-03

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 34.48  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509344  52 VGSRVTLHCSfwsSEWVSDDISFTWRYQpeggrdaisifhyakgqpyidevGTFKERIQWVGDPRWKDGSIVIH--NLDY 129
Cdd:pfam00047  10 EGDSATLTCS---ASTGSPGPDVTWSKE-----------------------GGTLIESLKVKHDNGRTTQSSLLisNVTK 63

                          90       100
                  ....*....|....*....|...
gi 2462509344 130 SDNGTFTCDVKNPPDIVGKTSQV 152
Cdd:pfam00047  64 EDAGTYTCVVNNPGGSATLSTSL 86
 
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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