ID NECT1_HUMAN Reviewed; 517 AA. AC Q15223; O75465; Q2M3D3; Q9HBE6; Q9HBW2; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 3. DT 24-JAN-2024, entry version 211. DE RecName: Full=Nectin-1; DE AltName: Full=Herpes virus entry mediator C; DE Short=Herpesvirus entry mediator C; DE Short=HveC; DE AltName: Full=Herpesvirus Ig-like receptor; DE Short=HIgR; DE AltName: Full=Nectin cell adhesion molecule 1 {ECO:0000312|HGNC:HGNC:9706}; DE AltName: Full=Poliovirus receptor-related protein 1; DE AltName: CD_antigen=CD111; DE Flags: Precursor; GN Name=NECTIN1 {ECO:0000312|HGNC:HGNC:9706}; Synonyms=HVEC, PRR1, PVRL1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA), AND FUNCTION AS A RECEPTOR FOR RP HHV-1; HHV-2 AND PRV. RX PubMed=7721102; DOI=10.1016/0378-1119(94)00842-g; RA Lopez M., Eberle F., Mattei M.-G., Gabert J., Bardin F., Maroc C., RA Dubreuil P.; RT "cDNA characterization and chromosomal localization of a gene related to RT the poliovirus receptor gene."; RL Gene 155:261-265(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA). RX PubMed=9616127; DOI=10.1126/science.280.5369.1618; RA Geraghty R.J., Krummenacher C., Cohen G.H., Eisenberg R.J., Spear P.G.; RT "Entry of alphaherpesviruses mediated by poliovirus receptor-related RT protein 1 and poliovirus receptor."; RL Science 280:1618-1620(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA). RX PubMed=11356977; DOI=10.1128/jvi.75.12.5684-5691.2001; RA Lopez M., Cocchi F., Avitabile E., Leclerc A., Adelaide J., RA Campadelli-Fjume G., Dubreuil P.; RT "Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 RT (or prr1-HIgR-Hvec) modulates positively and negatively susceptibility to RT hsv infection."; RL J. Virol. 75:5684-5691(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-517 (ISOFORMS ALPHA AND DELTA), RP INVOLVEMENT IN EDMI, AND INVOLVEMENT IN OFC7. RX PubMed=10932188; DOI=10.1038/78119; RA Suzuki K., Hu D., Bustos T., Zlotogora J., Richieri-Costa A., Helms J.A., RA Spritz R.A.; RT "Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus RT receptor, in cleft lip/palate-ectodermal dysplasia."; RL Nat. Genet. 25:427-430(2000). RN [6] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLEX VIRUS RP 1/HHV-1 AND HERPES SIMPLEX VIRUS 2/HHV-2 GLYCOPROTEIN D. RX PubMed=9696799; DOI=10.1128/jvi.72.9.7064-7074.1998; RA Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D., RA Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.; RT "Herpes simplex virus glycoprotein D can bind to poliovirus receptor- RT related protein 1 or herpesvirus entry mediator, two structurally unrelated RT mediators of virus entry."; RL J. Virol. 72:7064-7074(1998). RN [7] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLEX VIRUS RP 1/HHV-1; HERPES SIMPLEX VIRUS 2/HHV-2 GLYCOPROTEIN D AND PSEUDORABIES VIRUS RP GLYCOPROTEIN D. RX PubMed=9657005; DOI=10.1006/viro.1998.9218; RA Warner M.S., Geraghty R.J., Martinez W.M., Montgomery R.I., Whitbeck J.C., RA Xu R., Eisenberg R.J., Cohen G.H., Spear P.G.; RT "A cell surface protein with herpesvirus entry activity (HveB) confers RT susceptibility to infection by mutants of herpes simplex virus type 1, RT herpes simplex virus type 2, and pseudorabies virus."; RL Virology 246:179-189(1998). RN [8] RP INTERACTION WITH AFADIN. RX PubMed=10225955; DOI=10.1083/jcb.145.3.539; RA Takahashi K., Nakanishi H., Miyahara M., Mandai K., Satoh K., Satoh A., RA Nishioka H., Aoki J., Nomoto A., Mizoguchi A., Takai Y.; RT "Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to RT cadherin-based adherens junctions through interaction with Afadin, a PDZ RT domain-containing protein."; RL J. Cell Biol. 145:539-549(1999). RN [9] RP INTERACTION WITH NECTIN3 AND NECTIN4. RX PubMed=11544254; DOI=10.1074/jbc.m103810200; RA Reymond N., Fabre S., Lecocq E., Adelaide J., Dubreuil P., Lopez M.; RT "Nectin4/PRR4, a new afadin-associated member of the nectin family that RT trans-interacts with nectin1/PRR1 through V domain interaction."; RL J. Biol. Chem. 276:43205-43215(2001). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [11] RP INTERACTION WITH INTEGRIN ITGAV/ITGB3. RX PubMed=16679515; DOI=10.1074/jbc.m600301200; RA Sakamoto Y., Ogita H., Hirota T., Kawakatsu T., Fukuyama T., Yasumi M., RA Kanzaki N., Ozaki M., Takai Y.; RT "Interaction of integrin alpha(v)beta3 with nectin. Implication in cross- RT talk between cell-matrix and cell-cell junctions."; RL J. Biol. Chem. 281:19631-19644(2006). RN [12] RP GLYCOSYLATION AT ASN-202. RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., RA Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core fucosylated RT glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-332. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422 AND SER-434, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-335 IN COMPLEX WITH HERPES RP SIMPLEX VIRUS GLYCOPROTEIN D, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=22146396; DOI=10.1038/ncomms1571; RA Zhang N., Yan J., Lu G., Guo Z., Fan Z., Wang J., Shi Y., Qi J., Gao G.F.; RT "Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host RT cell adhesion."; RL Nat. Commun. 2:577-577(2011). RN [18] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 31-345 IN COMPLEX WITH HERPES RP SIMPLEX VIRUS GLYCOPROTEIN D, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-82; RP SER-84 AND PHE-129, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-72; ASN-139 RP AND ASN-202. RX PubMed=21980294; DOI=10.1371/journal.ppat.1002277; RA Di Giovine P., Settembre E.C., Bhargava A.K., Luftig M.A., Lou H., RA Cohen G.H., Eisenberg R.J., Krummenacher C., Carfi A.; RT "Structure of herpes simplex virus glycoprotein D bound to the human RT receptor nectin-1."; RL PLoS Pathog. 7:E1002277-E1002277(2011). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 31-337, SUBUNIT, GLYCOSYLATION AT RP ASN-202, DISULFIDE BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22902367; DOI=10.1038/nsmb.2366; RA Harrison O.J., Vendome J., Brasch J., Jin X., Hong S., Katsamba P.S., RA Ahlsen G., Troyanovsky R.B., Troyanovsky S.M., Honig B., Shapiro L.; RT "Nectin ectodomain structures reveal a canonical adhesive interface."; RL Nat. Struct. Mol. Biol. 19:906-915(2012). CC -!- FUNCTION: Promotes cell-cell contacts by forming homophilic or CC heterophilic trans-dimers. Heterophilic interactions have been detected CC between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4. Has some CC neurite outgrowth-promoting activity. {ECO:0000269|PubMed:21980294}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for herpes simplex CC virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies CC virus/PRV. {ECO:0000269|PubMed:7721102, ECO:0000269|PubMed:9657005}. CC -!- SUBUNIT: Interacts (via Ig-like C2-type domain 2) with FGFR1, FGFR2 and CC FGFR3 (By similarity). Cis- and trans-homodimer. Can form trans- CC heterodimers with NECTIN3 and with NECTIN4. Interaction between NECTIN1 CC and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates CC the formation of puncta adherentia junctions between axons and CC dendrites. Interacts (via cytoplasmic domain) with AFDN (via PDZ CC domain); this interaction recruits NECTIN1 to cadherin-based adherens CC junctions and provides a connection with the actin cytoskeleton. CC Interacts with integrin alphaV/beta3. {ECO:0000250, CC ECO:0000269|PubMed:10225955, ECO:0000269|PubMed:11544254, CC ECO:0000269|PubMed:16679515, ECO:0000269|PubMed:22902367}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus CC 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV CC envelope glycoprotein D (PubMed:21980294, PubMed:22146396, CC PubMed:9696799, PubMed:9657005). {ECO:0000269|PubMed:21980294, CC ECO:0000269|PubMed:22146396, ECO:0000269|PubMed:9657005, CC ECO:0000269|PubMed:9696799}. CC -!- INTERACTION: CC Q15223; Q92520: FAM3C; NbExp=3; IntAct=EBI-1771314, EBI-2876774; CC Q15223; Q15223: NECTIN1; NbExp=4; IntAct=EBI-1771314, EBI-1771314; CC Q15223; Q9NQS3: NECTIN3; NbExp=2; IntAct=EBI-1771314, EBI-2826725; CC Q15223; Q9NQS3-1: NECTIN3; NbExp=3; IntAct=EBI-1771314, EBI-16007706; CC Q15223; Q96NY8: NECTIN4; NbExp=5; IntAct=EBI-1771314, EBI-4314784; CC Q15223; O00560: SDCBP; NbExp=8; IntAct=EBI-1771314, EBI-727004; CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type CC I membrane protein. Presynaptic cell membrane {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform Delta]: Cell membrane; Single-pass type CC I membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Delta; CC IsoId=Q15223-1; Sequence=Displayed; CC Name=Alpha; CC IsoId=Q15223-2; Sequence=VSP_002626, VSP_002627; CC Name=Gamma; CC IsoId=Q15223-3; Sequence=VSP_002624, VSP_002625; CC -!- DOMAIN: Ig-like C2-type 2 mediates neurite outgrowth through binding, CC induction of phosphorylation, and activation of FGFR. {ECO:0000250}. CC -!- DISEASE: Ectodermal dysplasia, Margarita Island type (EDMI) CC [MIM:225060]: An autosomal recessive form of ectodermal dysplasia, a CC heterogeneous group of disorders due to abnormal development of two or CC more ectodermal structures. It is a syndrome characterized by the CC association of cleft lip/palate, ectodermal dysplasia (sparse short and CC dry scalp hair, sparse eyebrows and eyelashes), and partial syndactyly CC of the fingers and/or toes. Two thirds of the patients do not manifest CC oral cleft but present with abnormal teeth and nails. CC {ECO:0000269|PubMed:10932188}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Non-syndromic orofacial cleft 7 (OFC7) [MIM:225060]: A birth CC defect consisting of cleft lips with or without cleft palate. Cleft CC lips are associated with cleft palate in two-third of cases. A cleft CC lip can occur on one or both sides and range in severity from a simple CC notch in the upper lip to a complete opening in the lip extending into CC the floor of the nostril and involving the upper gum. CC {ECO:0000269|PubMed:10932188}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA53980.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X76400; CAA53980.2; ALT_INIT; mRNA. DR EMBL; AF060231; AAC23798.1; -; mRNA. DR EMBL; AY029539; AAK33124.1; -; mRNA. DR EMBL; BC104948; AAI04949.1; -; mRNA. DR EMBL; BC113471; AAI13472.1; -; mRNA. DR EMBL; AF252867; AAG16648.1; -; Genomic_DNA. DR EMBL; AF196768; AAG16648.1; JOINED; Genomic_DNA. DR EMBL; AF196769; AAG16648.1; JOINED; Genomic_DNA. DR EMBL; AF196770; AAG16648.1; JOINED; Genomic_DNA. DR EMBL; AF196771; AAG16648.1; JOINED; Genomic_DNA. DR EMBL; AF196774; AAG16649.1; -; Genomic_DNA. DR EMBL; AF196768; AAG16649.1; JOINED; Genomic_DNA. DR EMBL; AF196769; AAG16649.1; JOINED; Genomic_DNA. DR EMBL; AF196770; AAG16649.1; JOINED; Genomic_DNA. DR EMBL; AF196771; AAG16649.1; JOINED; Genomic_DNA. DR EMBL; AF196772; AAG16649.1; JOINED; Genomic_DNA. DR EMBL; AF196773; AAG16649.1; JOINED; Genomic_DNA. DR CCDS; CCDS8426.1; -. [Q15223-1] DR CCDS; CCDS8427.1; -. [Q15223-3] DR PIR; JC4024; JC4024. DR RefSeq; NP_002846.3; NM_002855.4. [Q15223-1] DR RefSeq; NP_976030.1; NM_203285.1. [Q15223-2] DR RefSeq; NP_976031.1; NM_203286.1. [Q15223-3] DR PDB; 3ALP; X-ray; 2.80 A; A/B=30-335. DR PDB; 3SKU; X-ray; 4.00 A; D/E/F=31-345. DR PDB; 3U82; X-ray; 3.16 A; B=30-335. DR PDB; 3U83; X-ray; 2.50 A; A=30-335. DR PDB; 4FMF; X-ray; 3.20 A; A/B/C/D=31-337. DR PDB; 4MYW; X-ray; 3.19 A; B/D=30-335. DR PDBsum; 3ALP; -. DR PDBsum; 3SKU; -. DR PDBsum; 3U82; -. DR PDBsum; 3U83; -. DR PDBsum; 4FMF; -. DR PDBsum; 4MYW; -. DR AlphaFoldDB; Q15223; -. DR SMR; Q15223; -. DR BioGRID; 111776; 16. DR CORUM; Q15223; -. DR DIP; DIP-40302N; -. DR IntAct; Q15223; 18. DR MINT; Q15223; -. DR STRING; 9606.ENSP00000264025; -. DR GlyConnect; 1536; 4 N-Linked glycans (3 sites). DR GlyCosmos; Q15223; 9 sites, 5 glycans. DR GlyGen; Q15223; 11 sites, 3 N-linked glycans (3 sites), 4 O-linked glycans (2 sites). DR iPTMnet; Q15223; -. DR PhosphoSitePlus; Q15223; -. DR BioMuta; NECTIN1; -. DR DMDM; 18202503; -. DR EPD; Q15223; -. DR jPOST; Q15223; -. DR MassIVE; Q15223; -. DR MaxQB; Q15223; -. DR PaxDb; 9606-ENSP00000264025; -. DR PeptideAtlas; Q15223; -. DR ProteomicsDB; 60490; -. [Q15223-1] DR ProteomicsDB; 60491; -. [Q15223-2] DR ProteomicsDB; 60492; -. [Q15223-3] DR Antibodypedia; 4247; 480 antibodies from 38 providers. DR DNASU; 5818; -. DR Ensembl; ENST00000264025.8; ENSP00000264025.3; ENSG00000110400.11. [Q15223-1] DR Ensembl; ENST00000340882.2; ENSP00000345289.2; ENSG00000110400.11. [Q15223-3] DR GeneID; 5818; -. DR KEGG; hsa:5818; -. DR MANE-Select; ENST00000264025.8; ENSP00000264025.3; NM_002855.5; NP_002846.3. DR UCSC; uc001pwu.2; human. [Q15223-1] DR AGR; HGNC:9706; -. DR CTD; 5818; -. DR DisGeNET; 5818; -. DR GeneCards; NECTIN1; -. DR HGNC; HGNC:9706; NECTIN1. DR HPA; ENSG00000110400; Tissue enhanced (esophagus, skin). DR MalaCards; NECTIN1; -. DR MIM; 225060; phenotype. DR MIM; 600644; gene. DR neXtProt; NX_Q15223; -. DR OpenTargets; ENSG00000110400; -. DR Orphanet; 141291; Cleft lip and alveolus. DR Orphanet; 199306; Cleft lip/palate. DR Orphanet; 3253; Cleft lip/palate-ectodermal dysplasia syndrome. DR Orphanet; 199302; Isolated cleft lip. DR PharmGKB; PA34051; -. DR VEuPathDB; HostDB:ENSG00000110400; -. DR eggNOG; ENOG502QVRJ; Eukaryota. DR GeneTree; ENSGT00940000156933; -. DR HOGENOM; CLU_029618_1_2_1; -. DR InParanoid; Q15223; -. DR OMA; TTEPGEC; -. DR OrthoDB; 5358399at2759; -. DR PhylomeDB; Q15223; -. DR TreeFam; TF331051; -. DR PathwayCommons; Q15223; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization. DR SignaLink; Q15223; -. DR BioGRID-ORCS; 5818; 10 hits in 1137 CRISPR screens. DR ChiTaRS; NECTIN1; human. DR EvolutionaryTrace; Q15223; -. DR GeneWiki; PVRL1; -. DR GenomeRNAi; 5818; -. DR Pharos; Q15223; Tbio. DR PRO; PR:Q15223; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q15223; Protein. DR Bgee; ENSG00000110400; Expressed in lower esophagus mucosa and 177 other cell types or tissues. DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL. DR GO; GO:0043296; C:apical junction complex; IEA:Ensembl. DR GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0032584; C:growth cone membrane; IEA:Ensembl. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl. DR GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl. DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL. DR GO; GO:0015026; F:coreceptor activity; TAS:ProtInc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0046790; F:virion binding; IEA:Ensembl. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0007411; P:axon guidance; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB. DR GO; GO:0002934; P:desmosome organization; IEA:Ensembl. DR GO; GO:0070166; P:enamel mineralization; IEA:Ensembl. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:HGNC-UCL. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC-UCL. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0006826; P:iron ion transport; IEA:Ensembl. DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl. DR GO; GO:1902414; P:protein localization to cell junction; IBA:GO_Central. DR GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR GO; GO:0046718; P:viral entry into host cell; NAS:UniProtKB. DR CDD; cd05890; IgC1_2_Nectin-1_like; 1. DR CDD; cd05886; IgV_1_Nectin-1_like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR041850; Nectin-1_Ig2. DR InterPro; IPR041849; Nectin-1_IgV1. DR PANTHER; PTHR23277:SF69; NECTIN-1; 1. DR PANTHER; PTHR23277; NECTIN-RELATED; 1. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 2. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; Q15223; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Cell projection; Disulfide bond; Ectodermal dysplasia; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor; KW Reference proteome; Repeat; Secreted; Signal; Synapse; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..517 FT /note="Nectin-1" FT /id="PRO_0000015133" FT TOPO_DOM 31..355 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 356..376 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 377..517 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 31..141 FT /note="Ig-like V-type" FT DOMAIN 149..238 FT /note="Ig-like C2-type 1" FT DOMAIN 247..334 FT /note="Ig-like C2-type 2" FT REGION 282..299 FT /note="Interaction with FGFR" FT /evidence="ECO:0000250" FT REGION 399..488 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 419..434 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 446..480 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 422 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 435 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JKF6" FT MOD_RES 436 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9JKF6" FT MOD_RES 511 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JKF6" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 72 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21980294" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21980294" FT CARBOHYD 202 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:21980294, FT ECO:0000269|PubMed:22902367" FT CARBOHYD 286 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 297 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 307 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 332 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT DISULFID 51..124 FT /evidence="ECO:0000269|PubMed:22146396, FT ECO:0000269|PubMed:22902367, ECO:0000305|PubMed:21980294" FT DISULFID 172..226 FT /evidence="ECO:0000269|PubMed:22146396, FT ECO:0000269|PubMed:22902367, ECO:0000305|PubMed:21980294" FT DISULFID 269..316 FT /evidence="ECO:0000269|PubMed:22146396, FT ECO:0000269|PubMed:22902367, ECO:0000305|PubMed:21980294" FT VAR_SEQ 335..352 FT /note="EFPYTPSPPEHGRRAGPV -> AFCQLIYPGKGRTRARMF (in isoform FT Gamma)" FT /evidence="ECO:0000303|PubMed:11356977" FT /id="VSP_002624" FT VAR_SEQ 336..458 FT /note="FPYTPSPPEHGRRAGPVPTAIIGGVAGSILLVLIVVGGIVVALRRRRHTFKG FT DYSTKKHVYGNGYSKAGIPQHHPPMAQNLQYPDDSDDEKKAGPLGGSSYEEEEEEEEGG FT GGGERKVGGPHP -> KPRPQRGLGSAARLLAGTVAVFLILVAVLTVFFLYNRQQKSPP FT ETDGAGTDQPLSQKPEPSPSRQSSLVPEDIQVVHLDPGRQQQQEEEDLQKLSLQPPYYD FT LGVSPSYHPSVRTTEPRGECP (in isoform Alpha)" FT /evidence="ECO:0000305" FT /id="VSP_002626" FT VAR_SEQ 353..517 FT /note="Missing (in isoform Gamma)" FT /evidence="ECO:0000303|PubMed:11356977" FT /id="VSP_002625" FT VAR_SEQ 459..517 FT /note="Missing (in isoform Alpha)" FT /evidence="ECO:0000305" FT /id="VSP_002627" FT MUTAGEN 82 FT /note="N->Y: Impairs interaction with herpes simplex FT glycoprotein D. Decreases susceptibility to infection by FT herpes simplex virus." FT /evidence="ECO:0000269|PubMed:21980294" FT MUTAGEN 84 FT /note="S->Y: Impairs interaction with herpes simplex FT glycoprotein D. Decreases susceptibility to infection by FT herpes simplex virus." FT /evidence="ECO:0000269|PubMed:21980294" FT MUTAGEN 129 FT /note="F->A,S: Impairs interaction with herpes simplex FT glycoprotein D. Decreases susceptibility to infection by FT herpes simplex virus." FT /evidence="ECO:0000269|PubMed:21980294" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 61..71 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 74..82 FT /evidence="ECO:0007829|PDB:3U83" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:3U83" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:3U83" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 120..129 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 132..144 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 167..179 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 205..213 FT /evidence="ECO:0007829|PDB:3U83" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 223..230 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 233..240 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 243..252 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 265..275 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 279..284 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:3U83" FT HELIX 308..310 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 312..320 FT /evidence="ECO:0007829|PDB:3U83" FT STRAND 323..331 FT /evidence="ECO:0007829|PDB:3U83" SQ SEQUENCE 517 AA; 57158 MW; DF34C8AEC893EE6D CRC64; MARMGLAGAA GRWWGLALGL TAFFLPGVHS QVVQVNDSMY GFIGTDVVLH CSFANPLPSV KITQVTWQKS TNGSKQNVAI YNPSMGVSVL APYRERVEFL RPSFTDGTIR LSRLELEDEG VYICEFATFP TGNRESQLNL TVMAKPTNWI EGTQAVLRAK KGQDDKVLVA TCTSANGKPP SVVSWETRLK GEAEYQEIRN PNGTVTVISR YRLVPSREAH QQSLACIVNY HMDRFKESLT LNVQYEPEVT IEGFDGNWYL QRMDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL FFKGPINYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP SPPEHGRRAG PVPTAIIGGV AGSILLVLIV VGGIVVALRR RRHTFKGDYS TKKHVYGNGY SKAGIPQHHP PMAQNLQYPD DSDDEKKAGP LGGSSYEEEE EEEEGGGGGE RKVGGPHPKY DEDAKRPYFT VDEAEARQDG YGDRTLGYQY DPEQLDLAEN MVSQNDGSFI SKKEWYV //