ID PVR_HUMAN Reviewed; 417 AA. AC P15151; B4DTS9; P15152; Q15267; Q15268; Q96BJ1; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 27-MAR-2024, entry version 234. DE RecName: Full=Poliovirus receptor; DE AltName: Full=Nectin-like protein 5; DE Short=NECL-5; DE AltName: CD_antigen=CD155; DE Flags: Precursor; GN Name=PVR; Synonyms=PVS; 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], FUNCTION (MICROBIAL INFECTION), AND INTERACTION RP WITH POLIOVIRUS CAPSID PROTEINS. RX PubMed=2538245; DOI=10.1016/0092-8674(89)90690-9; RA Mendelsohn C.L., Wimmer E., Racaniello V.R.; RT "Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, RT and expression of a new member of the immunoglobulin superfamily."; RL Cell 56:855-865(1989). RN [2] RP SEQUENCE REVISION. RA Racaniello V.R.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=2170108; DOI=10.1002/j.1460-2075.1990.tb07520.x; RA Koike S., Horie H., Ise I., Okitsu A., Yoshida M., Iizuka N., Takeuchi K., RA Takegami T., Nomoto A.; RT "The poliovirus receptor protein is produced both as membrane-bound and RT secreted forms."; RL EMBO J. 9:3217-3224(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT RP MET-340. 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 [7] RP DOMAINS. RX PubMed=1851992; DOI=10.1073/pnas.88.10.4104; RA Koike S., Ise I., Nomoto A.; RT "Functional domains of the poliovirus receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4104-4108(1991). RN [8] RP MUTAGENESIS OF GLYCOSYLATION SITES. RX PubMed=1331527; DOI=10.1128/jvi.66.12.7368-7373.1992; RA Zibert A., Wimmer E.; RT "N glycosylation of the virus binding domain is not essential for function RT of the human poliovirus receptor."; RL J. Virol. 66:7368-7373(1992). RN [9] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH PSEUDORAVIES VIRUS GD RP PROTEIN. 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 [10] RP INTERACTION WITH VTN. RX PubMed=11437656; DOI=10.1006/viro.2001.0943; RA Lange R., Peng X., Wimmer E., Lipp M., Bernhardt G.; RT "The poliovirus receptor CD155 mediates cell-to-matrix contacts by RT specifically binding to vitronectin."; RL Virology 285:218-227(2001). RN [11] RP INTERACTION WITH DYNLT1. RX PubMed=11751937; DOI=10.1074/jbc.m111937200; RA Mueller S., Cao X., Welker R., Wimmer E.; RT "Interaction of the poliovirus receptor CD155 with the dynein light chain RT Tctex-1 and its implication for poliovirus pathogenesis."; RL J. Biol. Chem. 277:7897-7904(2002). RN [12] RP TRANSCRIPTIONAL REGULATION BY SHH. RX PubMed=11983699; DOI=10.1074/jbc.m201378200; RA Solecki D.J., Gromeier M., Mueller S., Bernhardt G., Wimmer E.; RT "Expression of the human poliovirus receptor/CD155 gene is activated by RT sonic hedgehog."; RL J. Biol. Chem. 277:25697-25702(2002). RN [13] RP INTERACTION WITH NECTIN3. 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 [14] RP ITIM MOTIF, AND PHOSPHORYLATION AT TYR-398. RX PubMed=15194502; DOI=10.1016/j.bbrc.2004.05.111; RA Oda T., Ohka S., Nomoto A.; RT "Ligand stimulation of CD155alpha inhibits cell adhesion and enhances cell RT migration in fibroblasts."; RL Biochem. Biophys. Res. Commun. 319:1253-1264(2004). RN [15] RP INTERACTION WITH CD226. RX PubMed=15039383; DOI=10.1093/intimm/dxh059; RA Tahara-Hanaoka S., Shibuya K., Onoda Y., Zhang H., Yamazaki S., RA Miyamoto A., Honda S., Lanier L.L., Shibuya A.; RT "Functional characterization of DNAM-1 (CD226) interaction with its ligands RT PVR (CD155) and nectin-2 (PRR-2/CD112)."; RL Int. Immunol. 16:533-538(2004). RN [16] RP INTERACTION WITH DYNLT1, AND MUTAGENESIS OF 369-LYS--ARG-372. RX PubMed=15194795; DOI=10.1128/jvi.78.13.7186-7198.2004; RA Ohka S., Matsuda N., Tohyama K., Oda T., Morikawa M., Kuge S., Nomoto A.; RT "Receptor (CD155)-dependent endocytosis of poliovirus and retrograde axonal RT transport of the endosome."; RL J. Virol. 78:7186-7198(2004). RN [17] RP FUNCTION. RX PubMed=15471548; DOI=10.1186/1471-2407-4-73; RA Sloan K.E., Eustace B.K., Stewart J.K., Zehetmeier C., Torella C., RA Simeone M., Roy J.E., Unger C., Louis D.N., Ilag L.L., Jay D.G.; RT "CD155/PVR plays a key role in cell motility during tumor cell invasion and RT migration."; RL BMC Cancer 4:73-73(2004). RN [18] RP INTERACTION WITH NECTIN3. 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 [19] RP INTERACTION WITH CD96. RX PubMed=15034010; DOI=10.4049/jimmunol.172.7.3994; RA Fuchs A., Cella M., Giurisato E., Shaw A.S., Colonna M.; RT "CD96 (tactile) promotes NK cell-target cell adhesion by interacting with RT the poliovirus receptor (CD155)."; RL J. Immunol. 172:3994-3998(2004). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, GLYCOSYLATION [LARGE SCALE RP ANALYSIS] AT ASN-352 (ISOFORM GAMMA), AND GLYCOSYLATION [LARGE SCALE RP ANALYSIS] AT ASN-360 (ISOFORM BETA). 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 [21] RP FUNCTION. RX PubMed=15607800; DOI=10.1016/j.molimm.2004.07.028; RA Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S., Rivera P., RA Spaggiari G.M., Dondero A., Carnemolla B., Reymond N., Mingari M.C., RA Lopez M., Moretta L., Moretta A.; RT "PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1 (CD226) RT activating receptor: involvement in tumor cell lysis."; RL Mol. Immunol. 42:463-469(2005). RN [22] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HHV-5 UL141. RX PubMed=15640804; DOI=10.1038/ni1156; RA Tomasec P., Wang E.C., Davison A.J., Vojtesek B., Armstrong M., Griffin C., RA McSharry B.P., Morris R.J., Llewellyn-Lacey S., Rickards C., Nomoto A., RA Sinzger C., Wilkinson G.W.; RT "Downregulation of natural killer cell-activating ligand CD155 by human RT cytomegalovirus UL141."; RL Nat. Immunol. 6:181-188(2005). RN [23] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-307. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [24] 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 [25] RP GLYCOSYLATION AT ASN-120, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.m111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of N- and RT O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 11:1-17(2012). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [27] RP X-RAY CRYSTALLOGRAPHY (22.0 ANGSTROMS) OF 28-329. RX PubMed=10618374; DOI=10.1073/pnas.97.1.79; RA He Y., Bowman V.D., Mueller S., Bator C.M., Bella J., Peng X., Baker T.S., RA Wimmer E., Kuhn R.J., Rossmann M.G.; RT "Interaction of the poliovirus receptor with poliovirus."; RL Proc. Natl. Acad. Sci. U.S.A. 97:79-84(2000). RN [28] RP X-RAY CRYSTALLOGRAPHY (15.0 ANGSTROMS) OF 28-329. RX PubMed=12663789; DOI=10.1128/jvi.77.8.4827-4835.2003; RA He Y., Mueller S., Chipman P.R., Bator C.M., Peng X., Bowman V.D., RA Mukhopadhyay S., Wimmer E., Kuhn R.J., Rossmann M.G.; RT "Complexes of poliovirus serotypes with their common cellular receptor, RT CD155."; RL J. Virol. 77:4827-4835(2003). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 28-145 IN COMPLEX WITH TIGIT, RP DISULFIDE BOND, AND PHOSPHORYLATION AT TYR-398. RX PubMed=22421438; DOI=10.1073/pnas.1120606109; RA Stengel K.F., Harden-Bowles K., Yu X., Rouge L., Yin J., Comps-Agrar L., RA Wiesmann C., Bazan J.F., Eaton D.L., Grogan J.L.; RT "Structure of TIGIT immunoreceptor bound to poliovirus receptor reveals a RT cell-cell adhesion and signaling mechanism that requires cis-trans receptor RT clustering."; RL Proc. Natl. Acad. Sci. U.S.A. 109:5399-5404(2012). CC -!- FUNCTION: Mediates NK cell adhesion and triggers NK cell effector CC functions. Binds two different NK cell receptors: CD96 and CD226. These CC interactions accumulates at the cell-cell contact site, leading to the CC formation of a mature immunological synapse between NK cell and target CC cell. This may trigger adhesion and secretion of lytic granules and CC IFN-gamma and activate cytotoxicity of activated NK cells. May also CC promote NK cell-target cell modular exchange, and PVR transfer to the CC NK cell. This transfer is more important in some tumor cells expressing CC a lot of PVR, and may trigger fratricide NK cell activation, providing CC tumors with a mechanism of immunoevasion. Plays a role in mediating CC tumor cell invasion and migration. {ECO:0000269|PubMed:15471548, CC ECO:0000269|PubMed:15607800}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for poliovirus. May CC play a role in axonal transport of poliovirus, by targeting virion-PVR- CC containing endocytic vesicles to the microtubular network through CC interaction with DYNLT1. This interaction would drive the virus- CC containing vesicle to the axonal retrograde transport. CC {ECO:0000269|PubMed:2538245}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Pseudorabies CC virus. {ECO:0000269|PubMed:9616127}. CC -!- FUNCTION: (Microbial infection) Is prevented to reach cell surface upon CC infection by Human cytomegalovirus /HHV-5, presumably to escape immune CC recognition of infected cell by NK cells. CC {ECO:0000269|PubMed:15640804}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=72 nM for VTN; CC -!- SUBUNIT: Can form trans-heterodimers with NECTIN3. The extracellular CC domain interacts with VTN, CD226 and CD96. The cytoplasmic domain CC interacts with DYNLT1. Binds with high affinity to TIGIT. CC {ECO:0000269|PubMed:11437656, ECO:0000269|PubMed:11751937, CC ECO:0000269|PubMed:12759359, ECO:0000269|PubMed:15034010, CC ECO:0000269|PubMed:15039383, ECO:0000269|PubMed:15194795, CC ECO:0000269|PubMed:16216929, ECO:0000269|PubMed:19011627, CC ECO:0000269|PubMed:22421438}. CC -!- SUBUNIT: (Microbial infection) Interacts with poliovirus capsid CC proteins. {ECO:0000269|PubMed:2538245}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC /HHV-5 UL141 protein. {ECO:0000269|PubMed:15640804}. CC -!- SUBUNIT: (Microbial infection) Interacts with pseudorabies virus gD CC protein. {ECO:0000269|PubMed:9616127}. CC -!- INTERACTION: CC P15151; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-3919694, EBI-10827839; CC P15151; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-3919694, EBI-12109402; CC P15151; Q96PS8: AQP10; NbExp=3; IntAct=EBI-3919694, EBI-12820279; CC P15151; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-3919694, EBI-12244618; CC P15151; Q15762: CD226; NbExp=3; IntAct=EBI-3919694, EBI-4314442; CC P15151; Q08722-3: CD47; NbExp=3; IntAct=EBI-3919694, EBI-17263290; CC P15151; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-3919694, EBI-12256978; CC P15151; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-3919694, EBI-12019274; CC P15151; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-3919694, EBI-10269179; CC P15151; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-3919694, EBI-3867333; CC P15151; Q15125: EBP; NbExp=3; IntAct=EBI-3919694, EBI-3915253; CC P15151; P56851: EDDM3B; NbExp=3; IntAct=EBI-3919694, EBI-10215665; CC P15151; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-3919694, EBI-13067820; CC P15151; Q9HCP6: HHATL; NbExp=3; IntAct=EBI-3919694, EBI-5916693; CC P15151; P49639: HOXA1; NbExp=3; IntAct=EBI-3919694, EBI-740785; CC P15151; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-3919694, EBI-8503746; CC P15151; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-3919694, EBI-11959885; CC P15151; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-3919694, EBI-11749135; CC P15151; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-3919694, EBI-10172290; CC P15151; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-3919694, EBI-10171774; CC P15151; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-3919694, EBI-10172052; CC P15151; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-3919694, EBI-9996449; CC P15151; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-3919694, EBI-3957694; CC P15151; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-3919694, EBI-1043191; CC P15151; O43934: MFSD11; NbExp=3; IntAct=EBI-3919694, EBI-17633886; CC P15151; Q92982: NINJ1; NbExp=3; IntAct=EBI-3919694, EBI-2802124; CC P15151; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-3919694, EBI-10317425; CC P15151; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-3919694, EBI-945833; CC P15151; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-3919694, EBI-22310682; CC P15151; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-3919694, EBI-2804156; CC P15151; P0DJD7: PGA4; NbExp=3; IntAct=EBI-3919694, EBI-12957629; CC P15151; Q04941: PLP2; NbExp=3; IntAct=EBI-3919694, EBI-608347; CC P15151; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-3919694, EBI-11721828; CC P15151; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-3919694, EBI-8636004; CC P15151; O00767: SCD; NbExp=3; IntAct=EBI-3919694, EBI-2684237; CC P15151; P11686: SFTPC; NbExp=3; IntAct=EBI-3919694, EBI-10197617; CC P15151; Q9BRI3: SLC30A2; NbExp=11; IntAct=EBI-3919694, EBI-8644112; CC P15151; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-3919694, EBI-10281213; CC P15151; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-3919694, EBI-10290130; CC P15151; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-3919694, EBI-12188413; CC P15151; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-3919694, EBI-10244848; CC P15151; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-3919694, EBI-13075176; CC P15151; P59542: TAS2R19; NbExp=3; IntAct=EBI-3919694, EBI-12847034; CC P15151; Q495A1: TIGIT; NbExp=2; IntAct=EBI-3919694, EBI-4314807; CC P15151; Q9BZW4: TM6SF2; NbExp=3; IntAct=EBI-3919694, EBI-13082040; CC P15151; P55061: TMBIM6; NbExp=3; IntAct=EBI-3919694, EBI-1045825; CC P15151; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-3919694, EBI-348587; CC P15151; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-3919694, EBI-12195227; CC P15151; P0DTL5: TMEM276; NbExp=3; IntAct=EBI-3919694, EBI-11997340; CC P15151; Q969K7: TMEM54; NbExp=3; IntAct=EBI-3919694, EBI-3922833; CC P15151; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-3919694, EBI-6656213; CC P15151; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-3919694, EBI-8649725; CC P15151; P30536: TSPO; NbExp=3; IntAct=EBI-3919694, EBI-6623146; CC P15151; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-3919694, EBI-10243654; CC P15151; O95183: VAMP5; NbExp=3; IntAct=EBI-3919694, EBI-10191195; CC P15151; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-3919694, EBI-12837904; CC P15151; Q8N966: ZDHHC22; NbExp=3; IntAct=EBI-3919694, EBI-10268111; CC P15151; O95159: ZFPL1; NbExp=3; IntAct=EBI-3919694, EBI-718439; CC P15151; Q8K4F0: Cd226; Xeno; NbExp=3; IntAct=EBI-3919694, EBI-27124659; CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type CC I membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform Delta]: Cell membrane; Single-pass type CC I membrane protein. CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Secreted. CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Alpha; CC IsoId=P15151-1; Sequence=Displayed; CC Name=Beta; CC IsoId=P15151-2; Sequence=VSP_002617; CC Name=Gamma; CC IsoId=P15151-3; Sequence=VSP_002618, VSP_002619; CC Name=Delta; CC IsoId=P15151-4; Sequence=VSP_002620, VSP_002621; CC -!- INDUCTION: Transcriptionally regulated by SHH. CC {ECO:0000269|PubMed:11983699}. CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). The CC phosphorylated ITIM motif can bind the SH2 domain of several SH2- CC containing phosphatases. {ECO:0000269|PubMed:1851992}. CC -!- PTM: N-glycosylated. N-glycan at Asn-120: Hex5HexNAc4. CC {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:22171320}. CC -!- PTM: Phosphorylated by Src kinases on tyrosine residues in the ITIM CC motif upon ligation. Interaction with TIGIT is required for CC Phosphorylation. {ECO:0000269|PubMed:15194502, CC ECO:0000269|PubMed:22421438}. CC -!- MISCELLANEOUS: The V-type domain is necessary and sufficient for virus CC binding and uptake. CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The accidental crippler CC - Issue 75 of October 2006; CC URL="https://web.expasy.org/spotlight/back_issues/075"; 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; M24407; AAA36461.1; -; mRNA. DR EMBL; M24406; AAA36462.1; -; mRNA. DR EMBL; X64116; CAA45478.1; -; Genomic_DNA. DR EMBL; X64117; CAA45478.1; JOINED; Genomic_DNA. DR EMBL; X64118; CAA45478.1; JOINED; Genomic_DNA. DR EMBL; X64119; CAA45478.1; JOINED; Genomic_DNA. DR EMBL; X64120; CAA45478.1; JOINED; Genomic_DNA. DR EMBL; X64121; CAA45478.1; JOINED; Genomic_DNA. DR EMBL; X64122; CAA45478.1; JOINED; Genomic_DNA. DR EMBL; X64123; CAA45478.1; JOINED; Genomic_DNA. DR EMBL; X64116; CAA45479.1; -; Genomic_DNA. DR EMBL; X64117; CAA45479.1; JOINED; Genomic_DNA. DR EMBL; X64118; CAA45479.1; JOINED; Genomic_DNA. DR EMBL; X64119; CAA45479.1; JOINED; Genomic_DNA. DR EMBL; X64120; CAA45479.1; JOINED; Genomic_DNA. DR EMBL; X64121; CAA45479.1; JOINED; Genomic_DNA. DR EMBL; X64122; CAA45479.1; JOINED; Genomic_DNA. DR EMBL; X64123; CAA45479.1; JOINED; Genomic_DNA. DR EMBL; X64116; CAA45480.1; -; Genomic_DNA. DR EMBL; X64117; CAA45480.1; JOINED; Genomic_DNA. DR EMBL; X64118; CAA45480.1; JOINED; Genomic_DNA. DR EMBL; X64119; CAA45480.1; JOINED; Genomic_DNA. DR EMBL; X64120; CAA45480.1; JOINED; Genomic_DNA. DR EMBL; X64122; CAA45480.1; JOINED; Genomic_DNA. DR EMBL; X64123; CAA45480.1; JOINED; Genomic_DNA. DR EMBL; AK300349; BAG62091.1; -; mRNA. DR EMBL; AC068948; AAF69803.1; -; Genomic_DNA. DR EMBL; BC015542; AAH15542.1; -; mRNA. DR CCDS; CCDS12640.1; -. [P15151-1] DR CCDS; CCDS46105.1; -. [P15151-2] DR CCDS; CCDS46106.1; -. [P15151-3] DR CCDS; CCDS46107.1; -. [P15151-4] DR PIR; A43024; RWHUPD. DR PIR; S12048; RWHUPA. DR RefSeq; NP_001129240.1; NM_001135768.2. [P15151-2] DR RefSeq; NP_001129241.1; NM_001135769.2. [P15151-3] DR RefSeq; NP_001129242.2; NM_001135770.3. DR RefSeq; NP_006496.4; NM_006505.4. DR PDB; 1DGI; EM; 22.00 A; R=28-329. DR PDB; 1NN8; EM; 15.00 A; R/S/T=28-329. DR PDB; 3EPC; EM; 8.00 A; R=30-242. DR PDB; 3EPD; EM; 9.00 A; R=30-242. DR PDB; 3EPF; EM; 9.00 A; R=30-242. DR PDB; 3J8F; EM; 3.70 A; 7=1-417. DR PDB; 3J9F; EM; 9.00 A; 7=28-143, 8=142-243, 9=242-333. DR PDB; 3UDW; X-ray; 2.90 A; C/D=28-145. DR PDB; 3URO; X-ray; 3.50 A; R=29-243. DR PDB; 4FQP; X-ray; 3.60 A; A=28-334. DR PDB; 6ARQ; X-ray; 2.88 A; D=28-334. DR PDB; 6ISC; X-ray; 2.20 A; B=28-145. DR PDB; 6O3O; X-ray; 2.80 A; C/D=28-334. DR PDBsum; 1DGI; -. DR PDBsum; 1NN8; -. DR PDBsum; 3EPC; -. DR PDBsum; 3EPD; -. DR PDBsum; 3EPF; -. DR PDBsum; 3J8F; -. DR PDBsum; 3J9F; -. DR PDBsum; 3UDW; -. DR PDBsum; 3URO; -. DR PDBsum; 4FQP; -. DR PDBsum; 6ARQ; -. DR PDBsum; 6ISC; -. DR PDBsum; 6O3O; -. DR AlphaFoldDB; P15151; -. DR EMDB; EMD-6147; -. DR EMDB; EMD-6148; -. DR EMDB; EMD-6243; -. DR SMR; P15151; -. DR BioGRID; 111775; 197. DR DIP; DIP-43987N; -. DR IntAct; P15151; 110. DR MINT; P15151; -. DR STRING; 9606.ENSP00000402060; -. DR DrugBank; DB08231; Myristic acid. DR DrugBank; DB03203; Sphingosine. DR GlyConnect; 782; 1 N-Linked glycan (1 site). DR GlyCosmos; P15151; 10 sites, 2 glycans. DR GlyGen; P15151; 13 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (3 sites). DR iPTMnet; P15151; -. DR PhosphoSitePlus; P15151; -. DR SwissPalm; P15151; -. DR BioMuta; PVR; -. DR DMDM; 1346922; -. DR EPD; P15151; -. DR jPOST; P15151; -. DR MassIVE; P15151; -. DR MaxQB; P15151; -. DR PaxDb; 9606-ENSP00000402060; -. DR PeptideAtlas; P15151; -. DR ProteomicsDB; 53110; -. [P15151-1] DR ProteomicsDB; 53111; -. [P15151-2] DR ProteomicsDB; 53112; -. [P15151-3] DR ProteomicsDB; 53113; -. [P15151-4] DR Pumba; P15151; -. DR Antibodypedia; 2235; 764 antibodies from 39 providers. DR CPTC; P15151; 1 antibody. DR DNASU; 5817; -. DR Ensembl; ENST00000344956.8; ENSP00000340870.3; ENSG00000073008.16. [P15151-3] DR Ensembl; ENST00000403059.8; ENSP00000385344.3; ENSG00000073008.16. [P15151-2] DR GeneID; 5817; -. DR KEGG; hsa:5817; -. DR UCSC; uc032hzv.2; human. [P15151-1] DR AGR; HGNC:9705; -. DR CTD; 5817; -. DR DisGeNET; 5817; -. DR GeneCards; PVR; -. DR HGNC; HGNC:9705; PVR. DR HPA; ENSG00000073008; Low tissue specificity. DR MIM; 173850; gene+phenotype. DR neXtProt; NX_P15151; -. DR OpenTargets; ENSG00000073008; -. DR PharmGKB; PA34050; -. DR VEuPathDB; HostDB:ENSG00000073008; -. DR eggNOG; ENOG502QWSY; Eukaryota. DR GeneTree; ENSGT00940000162848; -. DR HOGENOM; CLU_029618_0_0_1; -. DR InParanoid; P15151; -. DR OrthoDB; 5358399at2759; -. DR PhylomeDB; P15151; -. DR TreeFam; TF331051; -. DR PathwayCommons; P15151; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization. DR SignaLink; P15151; -. DR SIGNOR; P15151; -. DR BioGRID-ORCS; 5817; 10 hits in 1169 CRISPR screens. DR ChiTaRS; PVR; human. DR EvolutionaryTrace; P15151; -. DR GeneWiki; CD155; -. DR GenomeRNAi; 5817; -. DR Pharos; P15151; Tbio. DR PRO; PR:P15151; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P15151; Protein. DR Bgee; ENSG00000073008; Expressed in stromal cell of endometrium and 141 other cell types or tissues. DR ExpressionAtlas; P15151; baseline and differential. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. 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 GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:BHF-UCL. DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:BHF-UCL. DR GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IMP:BHF-UCL. DR GO; GO:0060370; P:susceptibility to T cell mediated cytotoxicity; IDA:BHF-UCL. DR CDD; cd20930; Ig3_Nectin-5_like; 1. DR CDD; cd07703; IgC1_2_Nectin-2_Necl-5_like; 1. DR CDD; cd20989; IgV_1_Nectin-2_NecL-5_like_CD112_CD155; 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; IPR013106; Ig_V-set. DR PANTHER; PTHR47387; NECTIN-2; 1. DR PANTHER; PTHR47387:SF1; NECTIN-2; 1. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. DR Genevisible; P15151; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry; KW Host-virus interaction; Immunoglobulin domain; Membrane; Phosphoprotein; KW Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..417 FT /note="Poliovirus receptor" FT /id="PRO_0000015131" FT TOPO_DOM 21..343 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 344..367 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 368..417 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 24..139 FT /note="Ig-like V-type" FT DOMAIN 145..237 FT /note="Ig-like C2-type 1" FT DOMAIN 244..328 FT /note="Ig-like C2-type 2" FT REGION 368..372 FT /note="DYNLT1 binding" FT MOTIF 396..401 FT /note="ITIM motif" FT MOD_RES 398 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:15194502, FT ECO:0000269|PubMed:22421438" FT CARBOHYD 105 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 120 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:22171320" FT CARBOHYD 188 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 218 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 237 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 278 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 307 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 313 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 49..123 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:22421438" FT DISULFID 166..221 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 266..312 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 331 FT /note="E -> G (in isoform Gamma)" FT /evidence="ECO:0000305" FT /id="VSP_002618" FT VAR_SEQ 332..384 FT /note="Missing (in isoform Gamma)" FT /evidence="ECO:0000305" FT /id="VSP_002619" FT VAR_SEQ 340..384 FT /note="Missing (in isoform Beta)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_002617" FT VAR_SEQ 385..392 FT /note="TEHASASA -> EHHQSCRN (in isoform Delta)" FT /evidence="ECO:0000305" FT /id="VSP_002620" FT VAR_SEQ 393..417 FT /note="Missing (in isoform Delta)" FT /evidence="ECO:0000305" FT /id="VSP_002621" FT VARIANT 67 FT /note="A -> T (in dbSNP:rs1058402)" FT /id="VAR_003952" FT VARIANT 295 FT /note="A -> T (in dbSNP:rs35365841)" FT /id="VAR_049994" FT VARIANT 340 FT /note="I -> M (in dbSNP:rs203710)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_011736" FT MUTAGEN 369..372 FT /note="KCSR->ACSA: Partial loss of DYNLT1 binding." FT /evidence="ECO:0000269|PubMed:15194795" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 60..68 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 75..79 FT /evidence="ECO:0007829|PDB:6ISC" FT TURN 80..82 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 83..88 FT /evidence="ECO:0007829|PDB:6ISC" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:6ISC" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 119..128 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 131..142 FT /evidence="ECO:0007829|PDB:6ISC" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 161..173 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 176..180 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 186..193 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 200..208 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 218..224 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 262..269 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 275..285 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 310..315 FT /evidence="ECO:0007829|PDB:6O3O" FT STRAND 320..329 FT /evidence="ECO:0007829|PDB:6ARQ" FT CARBOHYD P15151-2:360 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD P15151-3:352 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" SQ SEQUENCE 417 AA; 45303 MW; D15C012CE853169B CRC64; MARAMAAAWP LLLVALLVLS WPPPGTGDVV VQAPTQVPGF LGDSVTLPCY LQVPNMEVTH VSQLTWARHG ESGSMAVFHQ TQGPSYSESK RLEFVAARLG AELRNASLRM FGLRVEDEGN YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE VQKVQLTGEP VPMARCVSTG GRPPAQITWH SDLGGMPNTS QVPGFLSGTV TVTSLWILVP SSQVDGKNVT CKVEHESFEK PQLLTVNLTV YYPPEVSISG YDNNWYLGQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR PVDKPINTTL ICNVTNALGA RQAELTVQVK EGPPSEHSGI SRNAIIFLVL GILVFLILLG IGIYFYWSKC SREVLWHCHL CPSSTEHASA SANGHVSYSA VSRENSSSQD PQTEGTR //