NECT3_HUMAN
ID NECT3_HUMAN Reviewed; 549 AA.
AC Q9NQS3; E9PFR0; Q6NVZ3; Q8NC05; Q8WVU4; Q9BVA9; Q9Y412;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Nectin-3;
DE AltName: Full=CDw113;
DE AltName: Full=Nectin cell adhesion molecule 3 {ECO:0000312|HGNC:HGNC:17664};
DE AltName: Full=Poliovirus receptor-related protein 3;
DE AltName: CD_antigen=CD113;
DE Flags: Precursor;
GN Name=NECTIN3 {ECO:0000312|HGNC:HGNC:17664}; Synonyms=PRR3, PVRL3;
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, AND INTERACTION
RP WITH AFDN.
RX PubMed=11024295; DOI=10.1016/s0378-1119(00)00316-4;
RA Reymond N., Borg J.-P., Lecocq E., Adelaide J., Campadelli-Fiume G.,
RA Dubreuil P., Lopez M.;
RT "Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that
RT interacts with afadin.";
RL Gene 255:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 246-549 (ISOFORM 1).
RC TISSUE=Brain, Cervix, and Kidney;
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 [LARGE SCALE MRNA] OF 143-549 (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INTERACTION WITH PVR.
RX PubMed=12759359; DOI=10.1074/jbc.m304166200;
RA Mueller S., Wimmer E.;
RT "Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic
RT interaction with CD155, a vitronectin and poliovirus receptor that
RT localizes to alpha(v)beta3 integrin-containing membrane microdomains.";
RL J. Biol. Chem. 278:31251-31260(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH PVR.
RX PubMed=16216929; DOI=10.1083/jcb.200501090;
RA Fujito T., Ikeda W., Kakunaga S., Minami Y., Kajita M., Sakamoto Y.,
RA Monden M., Takai Y.;
RT "Inhibition of cell movement and proliferation by cell-cell contact-induced
RT interaction of Necl-5 with nectin-3.";
RL J. Cell Biol. 171:165-173(2005).
RN [8]
RP INTERACTION WITH TIGIT.
RX PubMed=19011627; DOI=10.1038/ni.1674;
RA Yu X., Harden K., Gonzalez L.C., Francesco M., Chiang E., Irving B.,
RA Tom I., Ivelja S., Refino C.J., Clark H., Eaton D., Grogan J.L.;
RT "The surface protein TIGIT suppresses T cell activation by promoting the
RT generation of mature immunoregulatory dendritic cells.";
RL Nat. Immunol. 10:48-57(2009).
RN [9]
RP INTERACTION WITH C.DIFFICILE TCDB (MICROBIAL INFECTION), AND SUBCELLULAR
RP LOCATION.
RX PubMed=26038560; DOI=10.1073/pnas.1500791112;
RA LaFrance M.E., Farrow M.A., Chandrasekaran R., Sheng J., Rubin D.H.,
RA Lacy D.B.;
RT "Identification of an epithelial cell receptor responsible for Clostridium
RT difficile TcdB-induced cytotoxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7073-7078(2015).
RN [10]
RP INTERACTION WITH C.DIFFICILE TCDB (MICROBIAL INFECTION).
RX PubMed=27680706; DOI=10.1038/nature19799;
RA Tao L., Zhang J., Meraner P., Tovaglieri A., Wu X., Gerhard R., Zhang X.,
RA Stallcup W.B., Miao J., He X., Hurdle J.G., Breault D.T., Brass A.L.,
RA Dong M.;
RT "Frizzled proteins are colonic epithelial receptors for C. difficile toxin
RT B.";
RL Nature 538:350-355(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.93 ANGSTROMS) OF 58-359, SUBUNIT, GLYCOSYLATION AT
RP ASN-73; ASN-125; ASN-186; ASN-222 AND ASN-331, AND IDENTIFICATION BY MASS
RP 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: Plays a role in cell-cell adhesion through heterophilic
CC trans-interactions with nectin-like proteins or nectins, such as trans-
CC interaction with NECTIN2 at Sertoli-spermatid junctions. Trans-
CC interaction with PVR induces activation of CDC42 and RAC small G
CC proteins through common signaling molecules such as SRC and RAP1. Also
CC involved in the formation of cell-cell junctions, including adherens
CC junctions and synapses. Induces endocytosis-mediated down-regulation of
CC PVR from the cell surface, resulting in reduction of cell movement and
CC proliferation. Plays a role in the morphology of the ciliary body.
CC {ECO:0000269|PubMed:16216929}.
CC -!- SUBUNIT: Cis- and trans-homodimer. Can form trans-heterodimers with
CC NECTIN1, NECTIN2, PVR, IGSF4B/Necl-1 and with IGSF4. Interaction
CC between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites,
CC respectively, initiates the formation of puncta adherentia junctions
CC between axons and dendrites. Interacts (via Cytoplasmic domain) with
CC AFDN, providing a connection with the actin cytoskeleton. Binds with
CC low affinity to TIGIT. {ECO:0000269|PubMed:11024295,
CC ECO:0000269|PubMed:12759359, ECO:0000269|PubMed:16216929,
CC ECO:0000269|PubMed:19011627, ECO:0000269|PubMed:22902367}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.difficile toxin TcdB,
CC suggesting that it may contribute to TcdB toxin entry into cells
CC (PubMed:26038560). It was however shown that NECTIN3/PVRL3 does not act
CC as a major receptor for TcdB (PubMed:27680706).
CC {ECO:0000269|PubMed:26038560, ECO:0000269|PubMed:27680706}.
CC -!- INTERACTION:
CC Q9NQS3; P21333-2: FLNA; NbExp=3; IntAct=EBI-2826725, EBI-9641086;
CC Q9NQS3; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-2826725, EBI-10172290;
CC Q9NQS3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2826725, EBI-10171774;
CC Q9NQS3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-2826725, EBI-10172052;
CC Q9NQS3; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-2826725, EBI-10172511;
CC Q9NQS3; Q15223: NECTIN1; NbExp=2; IntAct=EBI-2826725, EBI-1771314;
CC Q9NQS3; Q92692: NECTIN2; NbExp=3; IntAct=EBI-2826725, EBI-718419;
CC Q9NQS3; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-2826725, EBI-945833;
CC Q9NQS3; O76081: RGS20; NbExp=3; IntAct=EBI-2826725, EBI-1052678;
CC Q9NQS3; Q495A1: TIGIT; NbExp=2; IntAct=EBI-2826725, EBI-4314807;
CC Q9NQS3-1; Q15223: NECTIN1; NbExp=3; IntAct=EBI-16007706, EBI-1771314;
CC Q9NQS3-1; Q92692: NECTIN2; NbExp=2; IntAct=EBI-16007706, EBI-718419;
CC Q9NQS3-1; Q9NQS3-1: NECTIN3; NbExp=3; IntAct=EBI-16007706, EBI-16007706;
CC Q9NQS3-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12106440, EBI-3867333;
CC Q9NQS3-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-12106440, EBI-11959885;
CC Q9NQS3-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-12106440, EBI-11749135;
CC Q9NQS3-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12106440, EBI-10171774;
CC Q9NQS3-2; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-12106440, EBI-11957260;
CC Q9NQS3-2; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-12106440, EBI-11993296;
CC Q9NQS3-2; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-12106440, EBI-3958099;
CC Q9NQS3-2; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-12106440, EBI-1043191;
CC Q9NQS3-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12106440, EBI-22310682;
CC Q9NQS3-2; P32242: OTX1; NbExp=3; IntAct=EBI-12106440, EBI-740446;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26038560};
CC Single-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NQS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQS3-2; Sequence=VSP_017435, VSP_017436;
CC Name=3;
CC IsoId=Q9NQS3-3; Sequence=VSP_046893, VSP_046894;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis and placenta as
CC well as in many cell lines, including epithelial cell lines.
CC {ECO:0000269|PubMed:11024295}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 1]:
CC Sequence=AAH17572.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 3]:
CC Sequence=BAC11404.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF282874; AAF97597.1; -; mRNA.
DR EMBL; AK075105; BAC11404.1; ALT_TERM; mRNA.
DR EMBL; AC133436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001336; AAH01336.1; -; mRNA.
DR EMBL; BC017572; AAH17572.1; ALT_INIT; mRNA.
DR EMBL; BC067808; AAH67808.1; -; mRNA.
DR EMBL; AL050071; CAB43256.1; -; mRNA.
DR CCDS; CCDS2957.1; -. [Q9NQS3-1]
DR CCDS; CCDS58842.1; -. [Q9NQS3-2]
DR CCDS; CCDS58843.1; -. [Q9NQS3-3]
DR PIR; T08732; T08732.
DR RefSeq; NP_001230215.1; NM_001243286.1. [Q9NQS3-2]
DR RefSeq; NP_001230217.1; NM_001243288.1. [Q9NQS3-3]
DR RefSeq; NP_056295.1; NM_015480.2. [Q9NQS3-1]
DR PDB; 4FOM; X-ray; 3.93 A; A=58-359.
DR PDBsum; 4FOM; -.
DR AlphaFoldDB; Q9NQS3; -.
DR SMR; Q9NQS3; -.
DR BioGRID; 117441; 84.
DR CORUM; Q9NQS3; -.
DR DIP; DIP-41491N; -.
DR IntAct; Q9NQS3; 49.
DR MINT; Q9NQS3; -.
DR STRING; 9606.ENSP00000418070; -.
DR GlyGen; Q9NQS3; 10 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q9NQS3; -.
DR PhosphoSitePlus; Q9NQS3; -.
DR BioMuta; NECTIN3; -.
DR DMDM; 74762752; -.
DR EPD; Q9NQS3; -.
DR jPOST; Q9NQS3; -.
DR MassIVE; Q9NQS3; -.
DR MaxQB; Q9NQS3; -.
DR PaxDb; Q9NQS3; -.
DR PeptideAtlas; Q9NQS3; -.
DR PRIDE; Q9NQS3; -.
DR ProteomicsDB; 20157; -.
DR ProteomicsDB; 82178; -. [Q9NQS3-1]
DR ProteomicsDB; 82179; -. [Q9NQS3-2]
DR Antibodypedia; 2646; 354 antibodies from 35 providers.
DR DNASU; 25945; -.
DR Ensembl; ENST00000319792.7; ENSP00000321514.3; ENSG00000177707.11. [Q9NQS3-2]
DR Ensembl; ENST00000485303.6; ENSP00000418070.1; ENSG00000177707.11. [Q9NQS3-1]
DR Ensembl; ENST00000493615.5; ENSP00000420579.1; ENSG00000177707.11. [Q9NQS3-3]
DR GeneID; 25945; -.
DR KEGG; hsa:25945; -.
DR MANE-Select; ENST00000485303.6; ENSP00000418070.1; NM_015480.3; NP_056295.1.
DR UCSC; uc003dxt.3; human. [Q9NQS3-1]
DR CTD; 25945; -.
DR DisGeNET; 25945; -.
DR GeneCards; NECTIN3; -.
DR HGNC; HGNC:17664; NECTIN3.
DR HPA; ENSG00000177707; Tissue enhanced (testis).
DR MIM; 607147; gene.
DR neXtProt; NX_Q9NQS3; -.
DR OpenTargets; ENSG00000177707; -.
DR PharmGKB; PA134969621; -.
DR VEuPathDB; HostDB:ENSG00000177707; -.
DR eggNOG; ENOG502QTRU; Eukaryota.
DR GeneTree; ENSGT00940000156028; -.
DR HOGENOM; CLU_029618_3_0_1; -.
DR InParanoid; Q9NQS3; -.
DR OMA; QMYPLYS; -.
DR OrthoDB; 509401at2759; -.
DR PhylomeDB; Q9NQS3; -.
DR TreeFam; TF331051; -.
DR PathwayCommons; Q9NQS3; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
DR SignaLink; Q9NQS3; -.
DR BioGRID-ORCS; 25945; 13 hits in 1074 CRISPR screens.
DR ChiTaRS; NECTIN3; human.
DR GeneWiki; PVRL3; -.
DR GenomeRNAi; 25945; -.
DR Pharos; Q9NQS3; Tbio.
DR PRO; PR:Q9NQS3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NQS3; protein.
DR Bgee; ENSG00000177707; Expressed in stromal cell of endometrium and 165 other tissues.
DR ExpressionAtlas; Q9NQS3; baseline and differential.
DR Genevisible; Q9NQS3; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; ISS:ARUK-UCL.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
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; ISS:HGNC-UCL.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:1902414; P:protein localization to cell junction; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:InterPro.
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; IPR013106; Ig_V-set.
DR InterPro; IPR033319; Nectin-3.
DR PANTHER; PTHR23277:SF12; PTHR23277:SF12; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
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 membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..57
FT /evidence="ECO:0000255"
FT CHAIN 58..549
FT /note="Nectin-3"
FT /id="PRO_0000226372"
FT TOPO_DOM 58..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 59..165
FT /note="Ig-like V-type"
FT DOMAIN 170..258
FT /note="Ig-like C2-type 1"
FT DOMAIN 269..354
FT /note="Ig-like C2-type 2"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22902367"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22902367"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22902367"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22902367"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22902367"
FT DISULFID 78..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 193..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 291..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..54
FT /note="MARTLRPSPLCPGGGKAQLSSASLLGAGLLLQPPTPPPLLLLLFPLLLFSRL
FT CG -> MAEGWRWCFVRRTPGLLRGPLLPRSFSGNPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046893"
FT VAR_SEQ 357..549
FT /note="DPPTTTTLQPTIQWHPSTADIEDLATEPKKLPFPLSTLATIKDDTIATIIAS
FT VVGGALFIVLVSVLAGIFCYRRRRTFRGDYFAKNYIPPSDMQKESQIDVLQQDELDSYP
FT DSVKKENKNPVNNLIRKDYLEEPEKTQWNNVENLNRFERPMDYYEDLKMGMKFVSDEHY
FT DENEDDLVSHVDGSVISRREWYV -> DVPFKQTSSIAVAGAVIGAVLALFIIAIFVTV
FT LLTPRKKRPSYLDKVIDLPPTHKPPPLYEERSPPLPQKDLFQPEHLPLQTQFKEREVGN
FT LQHSNGLNSRSFDYEDENPVGEDGIQQMYPLYNQMCYQDRSPGKHHQNNDPKRVYIDPR
FT EHYV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046894"
FT VAR_SEQ 357..366
FT /note="DPPTTTTLQP -> AYNSVASLNC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017435"
FT VAR_SEQ 367..549
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017436"
FT VARIANT 432
FT /note="R -> L (in dbSNP:rs15611)"
FT /id="VAR_049995"
FT CONFLICT 251
FT /note="P -> Q (in Ref. 4; AAH67808)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="R -> G (in Ref. 2; BAC11404)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="K -> E (in Ref. 4; AAH17572)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="S -> P (in Ref. 5; CAB43256)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="K -> R (in Ref. 5; CAB43256)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="Y -> C (in Ref. 5; CAB43256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 61002 MW; 6D1104CCB4A9D731 CRC64;
MARTLRPSPL CPGGGKAQLS SASLLGAGLL LQPPTPPPLL LLLFPLLLFS RLCGALAGPI
IVEPHVTAVW GKNVSLKCLI EVNETITQIS WEKIHGKSSQ TVAVHHPQYG FSVQGEYQGR
VLFKNYSLND ATITLHNIGF SDSGKYICKA VTFPLGNAQS STTVTVLVEP TVSLIKGPDS
LIDGGNETVA AICIAATGKP VAHIDWEGDL GEMESTTTSF PNETATIISQ YKLFPTRFAR
GRRITCVVKH PALEKDIRYS FILDIQYAPE VSVTGYDGNW FVGRKGVNLK CNADANPPPF
KSVWSRLDGQ WPDGLLASDN TLHFVHPLTF NYSGVYICKV TNSLGQRSDQ KVIYISDPPT
TTTLQPTIQW HPSTADIEDL ATEPKKLPFP LSTLATIKDD TIATIIASVV GGALFIVLVS
VLAGIFCYRR RRTFRGDYFA KNYIPPSDMQ KESQIDVLQQ DELDSYPDSV KKENKNPVNN
LIRKDYLEEP EKTQWNNVEN LNRFERPMDY YEDLKMGMKF VSDEHYDENE DDLVSHVDGS
VISRREWYV
