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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
 
 
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