NECTIN1
entrez
5818
canonical
uniprot
Q15223
canonical
ensembl
ENSG00000110400
resolver
ensp
ENSP00000264025
resolver
ensp
ENSP00000345289
resolver
ensp
ENSP00000513010
resolver
genesymbol
NECTIN1
resolver
genesymbol_syn
HVEC
resolver
genesymbol_syn
PRR1
resolver
genesymbol_syn
PVRL1
resolver
hgnc
HGNC:9706
resolver
uniprot
O75465
resolver
uniprot
Q2M3D3
resolver
uniprot
Q9HBE6
resolver
uniprot
Q9HBW2
resolver
uniprot_entry
NECT1_HUMAN
resolver
uniprot_sec
O75465
resolver
uniprot_sec
Q2M3D3
resolver
uniprot_sec
Q9HBE6
resolver
uniprot_sec
Q9HBW2
resolver
amino_acid_sequence
MARMGLAGAAGRWWGLALGLTAFFLPGVHSQVVQVNDSMYGFIGTDVVLHCSFANPLPSVKITQVTWQKSTNGSKQNVAIYNPSMGVSVLAPYRERVEFLRPSFTDGTIRLSRLELEDEGVYICEFATFPTGNRESQLNLTVMAKPTNWIEGTQAVLRAKKGQDDKVLVATCTSANGKPPSVVSWETRLKGEAEYQEIRNPNGTVTVISRYRLVPSREAHQQSLACIVNYHMDRFKESLTLNVQYEPEVTIEGFDGNWYLQRMDVKLTCKADANPPATEYHWTTLNGSLPKGVEAQNRTLFFKGPINYSLAGTYICEATNPIGTRSGQVEVNITEFPYTPSPPEHGRRAGPVPTAIIGGVAGSILLVLIVVGGIVVALRRRRHTFKGDYSTKKHVYGNGYSKAGIPQHHPPMAQNLQYPDDSDDEKKAGPLGGSSYEEEEEEEEGGGGGERKVGGPHPKYDEDAKRPYFTVDEAEARQDGYGDRTLGYQYDPEQLDLAENMVSQNDGSFISKKEWYV
uniprot
proteins
disease_involvement
DISEASE: Ectodermal dysplasia, Margarita Island type (EDMI) [MIM:225060]: An autosomal recessive form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is a syndrome characterized by the association of cleft lip/palate, ectodermal dysplasia (sparse short and dry scalp hair, sparse eyebrows and eyelashes), and partial syndactyly of the fingers and/or toes. Two thirds of the patients do not manifest oral cleft but present with abnormal teeth and nails. {ECO:0000269|PubMed:10932188, ECO:0000269|PubMed:11559849, ECO:0000269|PubMed:25913853}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Non-syndromic orofacial cleft 7 (OFC7) [MIM:225060]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. {ECO:0000269|PubMed:10932188}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cell adhesion molecule that promotes cell-cell contacts and plays important roles in the development of the nervous system (PubMed:21325282). Acts by forming homophilic or heterophilic trans-dimers (PubMed:21325282). Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4 (By similarity). Involved in axon guidance by promoting contacts between the commissural axons and the floor plate cells (By similarity). Involved in synaptogegesis (By similarity). Has some neurite outgrowth-promoting activity (By similarity). Promotes formation of checkerboard-like cellular pattern of hair cells and supporting cells in the auditory epithelium via heterophilic interaction with NECTIN3: NECTIN1 is present in the membrane of hair cells and associates with NECTIN3 on supporting cells, thereby mediating heterotypic adhesion between these two cell types (By similarity). Required for enamel mineralization (By similarity). {ECO:0000250|UniProtKB:Q9JKF6, ECO:0000269|PubMed:21325282}.; FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV (PubMed:21980294, PubMed:25231300, PubMed:28381567, PubMed:28542478, PubMed:34587223, PubMed:38857290, PubMed:39048823, PubMed:39048830, PubMed:7721102, PubMed:9616127, PubMed:9657005). Constitutes the major receptor for herpes simplex virus 1/HHV-1 entry into host cells (PubMed:34587223). {ECO:0000269|PubMed:21980294, ECO:0000269|PubMed:25231300, ECO:0000269|PubMed:28381567, ECO:0000269|PubMed:28542478, ECO:0000269|PubMed:34587223, ECO:0000269|PubMed:38857290, ECO:0000269|PubMed:39048823, ECO:0000269|PubMed:39048830, ECO:0000269|PubMed:7721102, ECO:0000269|PubMed:9616127, ECO:0000269|PubMed:9657005}.
uniprot
proteins
mass_dalton
57158
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="K->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 63..64; /note="TQ->AA: Impaired homophilic interaction in cis and cell adhsion activity; when associated with A-125 and A-133."; /evidence="ECO:0000269|PubMed:21325282"; MUTAGEN 63; /note="T->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 64; /note="Q->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 76; /note="Q->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 77; /note="N->A: Decreased interaction with herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2 and pseudorabies virus glycoprotein D, leading to decreased cell fusion with the virus."; /evidence="ECO:0000269|PubMed:28542478"; MUTAGEN 80; /note="I->A: Decreased interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 82; /note="N->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 82; /note="N->Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus."; /evidence="ECO:0000269|PubMed:21980294"; MUTAGEN 84; /note="S->Y: Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus."; /evidence="ECO:0000269|PubMed:21980294"; MUTAGEN 85; /note="M->A: Decreased interaction with herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2 and pseudorabies virus glycoprotein D, leading to decreased cell fusion with the virus."; /evidence="ECO:0000269|PubMed:25231300, ECO:0000269|PubMed:28542478"; MUTAGEN 90; /note="L->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 125; /note="E->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D. Impaired homophilic interaction in cis and cell adhsion activity; when associated with A-63-64-A and A-133."; /evidence="ECO:0000269|PubMed:21325282, ECO:0000269|PubMed:25231300"; MUTAGEN 129; /note="F->A,S: Abolished interaction with herpes simplex and pseudorabies glycoprotein D. Decreases susceptibility to infection by herpes simplex virus."; /evidence="ECO:0000269|PubMed:21980294, ECO:0000269|PubMed:25231300, ECO:0000269|PubMed:28542478"; MUTAGEN 130; /note="P->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D."; /evidence="ECO:0000269|PubMed:25231300"; MUTAGEN 133; /note="N->A: Does not affect interaction with herpes simplex virus 1/HHV-1 and herpes simplex virus 2/HHV-2 glycoprotein D. Impaired homophilic interaction in cis and cell adhsion activity; when associated with A-63-64-A and A-125."; /evidence="ECO:0000269|PubMed:21325282, ECO:0000269|PubMed:25231300
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Ubiquitinated by CBL following infection by herpes simplex virus 1/HHV-1 and association with HHV-1 envelope glycoprotein D, leading to its removal from cell surface. {ECO:0000269|PubMed:28381567}.
uniprot
proteins
protein_family
Nectin family
uniprot
proteins
pubmed
10225955
uniprot
proteins
pubmed
10932188
uniprot
proteins
pubmed
11356977
uniprot
proteins
pubmed
11544254
uniprot
proteins
pubmed
11559849
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16679515
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21325282
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21980294
uniprot
proteins
pubmed
22146396
uniprot
proteins
pubmed
22902367
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25231300
uniprot
proteins
pubmed
25913853
uniprot
proteins
pubmed
28381567
uniprot
proteins
pubmed
28542478
uniprot
proteins
pubmed
34587223
uniprot
proteins
pubmed
38857290
uniprot
proteins
pubmed
39048823
uniprot
proteins
pubmed
39048830
uniprot
proteins
pubmed
7721102
uniprot
proteins
pubmed
9616127
uniprot
proteins
pubmed
9657005
uniprot
proteins
pubmed
9696799
uniprot
proteins
sequence_length
517
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11356977, ECO:0000269|PubMed:21325282, ECO:0000269|PubMed:34587223, ECO:0000269|PubMed:38857290}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, adherens junction {ECO:0000269|PubMed:10225955}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9JKF6}; Single-pass type I membrane protein. Note=In the auditory epithelium, specificaly localizes to the apical side of the lateral membranes of hair cells. {ECO:0000250|UniProtKB:Q9JKF6}.; SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane {ECO:0000269|PubMed:11356977}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform Delta]: Cell membrane {ECO:0000269|PubMed:11356977}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted {ECO:0000269|PubMed:11356977}.
uniprot
proteins
transmembrane_region
TRANSMEM 356..376; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins