PVR_HUMAN
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 03-AUG-2022, entry version 225.
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; Q6ZMK1-3: CYHR1; NbExp=3; IntAct=EBI-3919694, EBI-11997340;
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; 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";
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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 SMR; P15151; -.
DR BioGRID; 111775; 189.
DR DIP; DIP-43987N; -.
DR IntAct; P15151; 107.
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 GlyGen; P15151; 10 sites, 2 N-linked glycans (1 site).
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; P15151; -.
DR PeptideAtlas; P15151; -.
DR PRIDE; P15151; -.
DR ProteomicsDB; 53110; -. [P15151-1]
DR ProteomicsDB; 53111; -. [P15151-2]
DR ProteomicsDB; 53112; -. [P15151-3]
DR ProteomicsDB; 53113; -. [P15151-4]
DR Antibodypedia; 2235; 702 antibodies from 38 providers.
DR CPTC; P15151; 1 antibody.
DR DNASU; 5817; -.
DR Ensembl; ENST00000344956.8; ENSP00000340870.3; ENSG00000073008.15. [P15151-3]
DR Ensembl; ENST00000403059.8; ENSP00000385344.3; ENSG00000073008.15. [P15151-2]
DR GeneID; 5817; -.
DR KEGG; hsa:5817; -.
DR UCSC; uc032hzv.2; human. [P15151-1]
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; 1087343at2759; -.
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; 9 hits in 1088 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 140 other tissues.
DR ExpressionAtlas; P15151; baseline and differential.
DR Genevisible; P15151; HS.
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:0016021; C:integral component of 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 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 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; 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; 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
