NECT1_HUMAN
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 03-AUG-2022, entry version 203.
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};
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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; CCDS8425.1; -. [Q15223-2]
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; 17.
DR MINT; Q15223; -.
DR STRING; 9606.ENSP00000264025; -.
DR GlyConnect; 1536; 4 N-Linked glycans (3 sites).
DR GlyGen; Q15223; 10 sites, 3 N-linked glycans (3 sites), 2 O-linked glycans (1 site).
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; Q15223; -.
DR PeptideAtlas; Q15223; -.
DR PRIDE; Q15223; -.
DR ProteomicsDB; 60490; -. [Q15223-1]
DR ProteomicsDB; 60491; -. [Q15223-2]
DR ProteomicsDB; 60492; -. [Q15223-3]
DR Antibodypedia; 4247; 439 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 Ensembl; ENST00000341398.6; ENSP00000344974.2; ENSG00000110400.11. [Q15223-2]
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 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; 509401at2759; -.
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 1068 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 175 other tissues.
DR Genevisible; Q15223; HS.
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:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 GO; GO:0019062; P:virion attachment to host cell; IEA:InterPro.
DR CDD; cd05886; Ig1_Nectin-1_like; 1.
DR CDD; cd05890; Ig2_Nectin-1_like; 1.
DR Gene3D; 2.60.40.10; -; 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; IPR041849; Nectin-1_Ig1.
DR InterPro; IPR041850; Nectin-1_Ig2.
DR InterPro; IPR033314; Nectin1.
DR PANTHER; PTHR23277:SF69; PTHR23277:SF69; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 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; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
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
