{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q15223","secondaryAccessions":["O75465","Q2M3D3","Q9HBE6","Q9HBW2"],"uniProtkbId":"NECT1_HUMAN","entryAudit":{"firstPublicDate":"2001-09-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-09-26","entryVersion":221,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"}],"value":"Nectin-1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"}],"value":"Herpes virus entry mediator C"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"}],"value":"Herpesvirus entry mediator C"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"}],"value":"HveC"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"}],"value":"Herpesvirus Ig-like receptor"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"}],"value":"HIgR"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9706"}],"value":"Nectin cell adhesion molecule 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7721102"}],"value":"Poliovirus receptor-related protein 1"}}],"cdAntigenNames":[{"value":"CD111"}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9706"}],"value":"NECTIN1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11356977"}],"value":"HVEC"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7721102"}],"value":"PRR1"},{"value":"PVRL1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9JKF6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21325282"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21980294"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25231300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28381567"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28542478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34587223"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38857290"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39048823"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39048830"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7721102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9616127"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9657005"}],"value":"(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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9JKF6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10225955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11544254"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16679515"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22902367"}],"value":"Cis- and trans-homodimer (PubMed:22902367). Can form trans-heterodimers with NECTIN3 and with NECTIN4 (PubMed:11544254). Interaction between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites (PubMed:11544254). Interacts (via cytoplasmic domain) with AFDN (via PDZ domain); this interaction recruits NECTIN1 to cadherin-based adherens junctions and provides a connection with the actin cytoskeleton (PubMed:10225955). Interacts with integrin alphaV/beta3 (PubMed:16679515). Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and FGFR3 (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21980294"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22146396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28542478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9657005"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9696799"}],"value":"(Microbial infection) Interacts with herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV envelope glycoprotein 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Ig-like C2-type 2 mediates neurite outgrowth through binding, induction of phosphorylation, and activation of FGFR (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28381567"}],"value":"(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"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Ectodermal dysplasia, Margarita Island type","diseaseAccession":"DI-00426","acronym":"EDMI","description":"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.","diseaseCrossReference":{"database":"MIM","id":"225060"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10932188"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11559849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25913853"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Non-syndromic orofacial cleft 7","diseaseAccession":"DI-00828","acronym":"OFC7","description":"A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. 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