NECT4_HUMAN
ID NECT4_HUMAN Reviewed; 510 AA.
AC Q96NY8; B4DQW3; Q96K15;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Nectin-4;
DE AltName: Full=Ig superfamily receptor LNIR;
DE AltName: Full=Nectin cell adhesion molecule 4 {ECO:0000312|HGNC:HGNC:19688};
DE AltName: Full=Poliovirus receptor-related protein 4;
DE Contains:
DE RecName: Full=Processed poliovirus receptor-related protein 4;
DE Flags: Precursor;
GN Name=NECTIN4 {ECO:0000312|HGNC:HGNC:19688}; Synonyms=LNIR, PRR4, PVRL4;
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 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, SUBUNIT, AND INTERACTION WITH AFDN AND NECTIN1.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [6]
RP INTERACTION WITH NECTIN1.
RX PubMed=12011057; DOI=10.1074/jbc.m203228200;
RA Fabre S., Reymond N., Cocchi F., Menotti L., Dubreuil P.,
RA Campadelli-Fiume G., Lopez M.;
RT "Prominent role of the Ig-like V domain in trans-interactions of nectins.
RT Nectin3 and nectin 4 bind to the predicted C-C'-C'-D beta-strands of the
RT nectin1 V domain.";
RL J. Biol. Chem. 277:27006-27013(2002).
RN [7]
RP PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX PubMed=15784625; DOI=10.1074/jbc.m410943200;
RA Fabre-Lafay S., Garrido-Urbani S., Reymond N., Goncalves A., Dubreuil P.,
RA Lopez M.;
RT "Nectin-4, a new serological breast cancer marker, is a substrate for tumor
RT necrosis factor-alpha-converting enzyme (TACE)/ADAM-17.";
RL J. Biol. Chem. 280:19543-19550(2005).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=17474988; DOI=10.1186/1471-2407-7-73;
RA Fabre-Lafay S., Monville F., Garrido-Urbani S., Berruyer-Pouyet C.,
RA Ginestier C., Reymond N., Finetti P., Sauvan R., Adelaide J., Geneix J.,
RA Lecocq E., Popovici C., Dubreuil P., Viens P., Goncalves A.,
RA Charafe-Jauffret E., Jacquemier J., Birnbaum D., Lopez M.;
RT "Nectin-4 is a new histological and serological tumor associated marker for
RT breast cancer.";
RL BMC Cancer 7:73-73(2007).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MEASLES VIRUS PROTEIN
RP H.
RX PubMed=22048310; DOI=10.1038/nature10639;
RA Muhlebach M.D., Mateo M., Sinn P.L., Prufer S., Uhlig K.M., Leonard V.H.,
RA Navaratnarajah C.K., Frenzke M., Wong X.X., Sawatsky B., Ramachandran S.,
RA McCray P.B. Jr., Cichutek K., von Messling V., Lopez M., Cattaneo R.;
RT "Adherens junction protein nectin-4 is the epithelial receptor for measles
RT virus.";
RL Nature 480:530-533(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 32-243, SUBUNIT, DISULFIDE BONDS,
RP 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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 32-146 IN COMPLEX WITH FUNCTION
RP (MICROBIAL INFECTION), SUBUNIT, AND DISULFIDE BOND.
RX PubMed=23202587; DOI=10.1038/nsmb.2432;
RA Zhang X., Lu G., Qi J., Li Y., He Y., Xu X., Shi J., Zhang C.W., Yan J.,
RA Gao G.F.;
RT "Structure of measles virus hemagglutinin bound to its epithelial receptor
RT nectin-4.";
RL Nat. Struct. Mol. Biol. 20:67-72(2013).
RN [12]
RP VARIANT EDSS1 MET-185.
RX PubMed=20691405; DOI=10.1016/j.ajhg.2010.07.003;
RA Brancati F., Fortugno P., Bottillo I., Lopez M., Josselin E.,
RA Boudghene-Stambouli O., Agolini E., Bernardini L., Bellacchio E.,
RA Iannicelli M., Rossi A., Dib-Lachachi A., Stuppia L., Palka G., Mundlos S.,
RA Stricker S., Kornak U., Zambruno G., Dallapiccola B.;
RT "Mutations in PVRL4, encoding cell adhesion molecule nectin-4, cause
RT ectodermal dysplasia-syndactyly syndrome.";
RL Am. J. Hum. Genet. 87:265-273(2010).
CC -!- FUNCTION: Seems to be involved in cell adhesion through trans-
CC homophilic and -heterophilic interactions, the latter including
CC specifically interactions with NECTIN1. Does not act as receptor for
CC alpha-herpesvirus entry into cells.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for measles virus.
CC {ECO:0000269|PubMed:22048310, ECO:0000269|PubMed:23202587}.
CC -!- SUBUNIT: Self-associates. Interacts via its Ig-like V-type domain with
CC NECTIN1 Ig-like V-type domain. Interacts via its C-terminus with AFDN.
CC {ECO:0000269|PubMed:11544254, ECO:0000269|PubMed:12011057,
CC ECO:0000269|PubMed:22902367}.
CC -!- SUBUNIT: (Microbial infection) Interacts with measles virus
CC Hemagglutinin protein (PubMed:22048310, PubMed:23202587).
CC {ECO:0000269|PubMed:22048310, ECO:0000269|PubMed:23202587}.
CC -!- INTERACTION:
CC Q96NY8; Q5J5C9: DEFB121; NbExp=3; IntAct=EBI-4314784, EBI-10244198;
CC Q96NY8; Q15223: NECTIN1; NbExp=5; IntAct=EBI-4314784, EBI-1771314;
CC Q96NY8; Q96NY8: NECTIN4; NbExp=3; IntAct=EBI-4314784, EBI-4314784;
CC Q96NY8; Q495A1: TIGIT; NbExp=2; IntAct=EBI-4314784, EBI-4314807;
CC Q96NY8; Q786F2: H; Xeno; NbExp=4; IntAct=EBI-4314784, EBI-5323300;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:11544254}. Note=Colocalizes with AFDN at cadherin-
CC based adherens junctions (PubMed:11544254).
CC -!- SUBCELLULAR LOCATION: [Processed poliovirus receptor-related protein
CC 4]: Secreted {ECO:0000269|PubMed:15784625}. Note=The secreted form is
CC found in breast tumor patients (PubMed:15784625).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96NY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96NY8-2; Sequence=VSP_056819, VSP_056820;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in placenta. Not detected
CC in normal breast epithelium but expressed in breast carcinoma.
CC {ECO:0000269|PubMed:11544254, ECO:0000269|PubMed:17474988}.
CC -!- PTM: The soluble form is produced by proteolytic cleavage at the cell
CC surface (shedding), probably by ADAM17/TACE.
CC {ECO:0000269|PubMed:15784625}.
CC -!- DISEASE: Ectodermal dysplasia-syndactyly syndrome 1 (EDSS1)
CC [MIM:613573]: A form of ectodermal dysplasia, a heterogeneous group of
CC disorders due to abnormal development of two or more ectodermal
CC structures. EDSS1 is characterized by the association of hair and teeth
CC abnormalities with cutaneous syndactyly of the hands and/or feet. Hair
CC morphologic abnormalities include twists at irregular intervals (pilli
CC torti) and swelling along the shafts, particularly associated with
CC areas of breakage. Dental findings consist of abnormally widely spaced
CC teeth, with peg-shaped and conical crowns. Patients have normal
CC sweating. {ECO:0000269|PubMed:20691405}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PVRL4ID44141ch1q23.html";
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DR EMBL; AF426163; AAL23958.1; -; mRNA.
DR EMBL; AK027753; BAB55344.1; -; mRNA.
DR EMBL; AK298981; BAG61075.1; -; mRNA.
DR EMBL; AL591806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52665.1; -; Genomic_DNA.
DR EMBL; BC010423; AAH10423.1; -; mRNA.
DR CCDS; CCDS1216.1; -. [Q96NY8-1]
DR RefSeq; NP_112178.2; NM_030916.2. [Q96NY8-1]
DR PDB; 4FRW; X-ray; 3.50 A; A/B/C/D/E/F=32-243.
DR PDB; 4GJT; X-ray; 3.10 A; B/C=32-146.
DR PDB; 4JJH; X-ray; 2.25 A; A/B=32-153.
DR PDBsum; 4FRW; -.
DR PDBsum; 4GJT; -.
DR PDBsum; 4JJH; -.
DR AlphaFoldDB; Q96NY8; -.
DR SMR; Q96NY8; -.
DR BioGRID; 123544; 25.
DR DIP; DIP-41492N; -.
DR IntAct; Q96NY8; 21.
DR MINT; Q96NY8; -.
DR STRING; 9606.ENSP00000356991; -.
DR ChEMBL; CHEMBL3712928; -.
DR DrugBank; DB13007; Enfortumab vedotin.
DR DrugCentral; Q96NY8; -.
DR GlyConnect; 1538; 7 N-Linked glycans (1 site).
DR GlyGen; Q96NY8; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; Q96NY8; -.
DR PhosphoSitePlus; Q96NY8; -.
DR BioMuta; NECTIN4; -.
DR DMDM; 74761016; -.
DR EPD; Q96NY8; -.
DR jPOST; Q96NY8; -.
DR MassIVE; Q96NY8; -.
DR MaxQB; Q96NY8; -.
DR PaxDb; Q96NY8; -.
DR PeptideAtlas; Q96NY8; -.
DR PRIDE; Q96NY8; -.
DR ProteomicsDB; 4909; -.
DR ProteomicsDB; 77578; -. [Q96NY8-1]
DR ABCD; Q96NY8; 1 sequenced antibody.
DR Antibodypedia; 2488; 252 antibodies from 32 providers.
DR DNASU; 81607; -.
DR Ensembl; ENST00000368012.4; ENSP00000356991.3; ENSG00000143217.9. [Q96NY8-1]
DR GeneID; 81607; -.
DR KEGG; hsa:81607; -.
DR MANE-Select; ENST00000368012.4; ENSP00000356991.3; NM_030916.3; NP_112178.2.
DR UCSC; uc001fxo.3; human. [Q96NY8-1]
DR CTD; 81607; -.
DR DisGeNET; 81607; -.
DR GeneCards; NECTIN4; -.
DR HGNC; HGNC:19688; NECTIN4.
DR HPA; ENSG00000143217; Group enriched (esophagus, salivary gland, skin, vagina).
DR MalaCards; NECTIN4; -.
DR MIM; 609607; gene.
DR MIM; 613573; phenotype.
DR neXtProt; NX_Q96NY8; -.
DR OpenTargets; ENSG00000143217; -.
DR Orphanet; 247820; Ectodermal dysplasia-syndactyly syndrome.
DR PharmGKB; PA134991624; -.
DR VEuPathDB; HostDB:ENSG00000143217; -.
DR eggNOG; ENOG502R9I0; Eukaryota.
DR GeneTree; ENSGT00940000157535; -.
DR HOGENOM; CLU_029618_1_1_1; -.
DR InParanoid; Q96NY8; -.
DR OMA; ASFTGQC; -.
DR OrthoDB; 509401at2759; -.
DR PhylomeDB; Q96NY8; -.
DR TreeFam; TF338610; -.
DR PathwayCommons; Q96NY8; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
DR SignaLink; Q96NY8; -.
DR BioGRID-ORCS; 81607; 23 hits in 1058 CRISPR screens.
DR ChiTaRS; NECTIN4; human.
DR GenomeRNAi; 81607; -.
DR Pharos; Q96NY8; Tclin.
DR PRO; PR:Q96NY8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96NY8; protein.
DR Bgee; ENSG00000143217; Expressed in lower esophagus mucosa and 120 other tissues.
DR ExpressionAtlas; Q96NY8; baseline and differential.
DR Genevisible; Q96NY8; HS.
DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
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; IPR033320; Nectin-4.
DR PANTHER; PTHR23277:SF11; PTHR23277:SF11; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Disease variant; Disulfide bond; Ectodermal dysplasia;
KW Glycoprotein; Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..510
FT /note="Nectin-4"
FT /id="PRO_0000297673"
FT CHAIN 32..?
FT /note="Processed poliovirus receptor-related protein 4"
FT /id="PRO_0000311086"
FT TOPO_DOM 32..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..144
FT /note="Ig-like V-type"
FT DOMAIN 148..237
FT /note="Ig-like C2-type 1"
FT DOMAIN 248..331
FT /note="Ig-like C2-type 2"
FT REGION 399..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..127
FT /evidence="ECO:0000269|PubMed:22902367,
FT ECO:0000269|PubMed:23202587, ECO:0007744|PDB:4FRW"
FT DISULFID 171..223
FT /evidence="ECO:0000269|PubMed:22902367,
FT ECO:0007744|PDB:4FRW"
FT DISULFID 270..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..266
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056819"
FT VAR_SEQ 412..436
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056820"
FT VARIANT 53
FT /note="F -> L (in dbSNP:rs3737786)"
FT /id="VAR_034669"
FT VARIANT 185
FT /note="T -> M (in EDSS1; dbSNP:rs267606992)"
FT /evidence="ECO:0000269|PubMed:20691405"
FT /id="VAR_064189"
FT CONFLICT 35
FT /note="E -> G (in Ref. 2; BAB55344)"
FT /evidence="ECO:0000305"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4FRW"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:4JJH"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4JJH"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4JJH"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4JJH"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:4JJH"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4FRW"
FT STRAND 165..177
FT /evidence="ECO:0007829|PDB:4FRW"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:4FRW"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:4FRW"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:4FRW"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4FRW"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:4FRW"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4FRW"
SQ SEQUENCE 510 AA; 55454 MW; DCF5E1D794F227FA CRC64;
MPLSLGAEMW GPEAWLLLLL LLASFTGRCP AGELETSDVV TVVLGQDAKL PCFYRGDSGE
QVGQVAWARV DAGEGAQELA LLHSKYGLHV SPAYEGRVEQ PPPPRNPLDG SVLLRNAVQA
DEGEYECRVS TFPAGSFQAR LRLRVLVPPL PSLNPGPALE EGQGLTLAAS CTAEGSPAPS
VTWDTEVKGT TSSRSFKHSR SAAVTSEFHL VPSRSMNGQP LTCVVSHPGL LQDQRITHIL
HVSFLAEASV RGLEDQNLWH IGREGAMLKC LSEGQPPPSY NWTRLDGPLP SGVRVDGDTL
GFPPLTTEHS GIYVCHVSNE FSSRDSQVTV DVLDPQEDSG KQVDLVSASV VVVGVIAALL
FCLLVVVVVL MSRYHRRKAQ QMTQKYEEEL TLTRENSIRR LHSHHTDPRS QPEESVGLRA
EGHPDSLKDN SSCSVMSEEP EGRSYSTLTT VREIETQTEL LSPGSGRAEE EEDQDEGIKQ
AMNHFVQENG TLRAKPTGNG IYINGRGHLV
