ID ITAV_HUMAN Reviewed; 1048 AA. AC P06756; A0AV67; B0LPF4; B7Z883; B7ZLX0; D3DPG8; E7EWZ6; Q53SK4; Q59EB7; AC Q6LD15; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 2. DT 27-NOV-2024, entry version 262. DE RecName: Full=Integrin alpha-V; DE AltName: Full=Vitronectin receptor {ECO:0000312|HGNC:HGNC:6150}; DE AltName: Full=Vitronectin receptor subunit alpha; DE AltName: CD_antigen=CD51; DE Contains: DE RecName: Full=Integrin alpha-V heavy chain; DE Contains: DE RecName: Full=Integrin alpha-V light chain; DE Flags: Precursor; GN Name=ITGAV {ECO:0000312|HGNC:HGNC:6150}; GN Synonyms=MSK8 {ECO:0000312|HGNC:HGNC:6150}, VNRA GN {ECO:0000312|HGNC:HGNC:6150}, VTNR {ECO:0000312|HGNC:HGNC:6150}; 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), AND VARIANT ILE-783. RX PubMed=2443500; DOI=10.1016/s0021-9258(18)47907-0; RA Suzuki S., Argraves W.S., Arai H., Languino L.R., Pierschbacher M.D., RA Ruoslahti E.; RT "Amino acid sequence of the vitronectin receptor alpha subunit and RT comparative expression of adhesion receptor mRNAs."; RL J. Biol. Chem. 262:14080-14085(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10965141; DOI=10.1159/000015631; RA Sims M.A., Field S., Barnes M.R., Shaikh N., Ellington K., Murphy K.E., RA Spurr N.K., Campbell D.A.; RT "Cloning and characterisation of ITGAV, the genomic sequence for human cell RT adhesion protein (vitronectin) receptor alpha subunit, CD51."; RL Cytogenet. Cell Genet. 89:268-271(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ILE-783. RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-783. RC TISSUE=Aortic endothelium; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-783. 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-783. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP ILE-783. 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 [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62. RX PubMed=7522056; DOI=10.1016/0167-4781(94)90278-x; RA Donahue J.P., Sugg N., Hawiger J.; RT "The integrin alpha v gene: identification and characterization of the RT promoter region."; RL Biochim. Biophys. Acta 1219:228-232(1994). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 413-1048, AND VARIANT ILE-783. RX PubMed=2430295; DOI=10.1073/pnas.83.22.8614; RA Suzuki S., Argraves W.S., Pytela R., Arai H., Krusius T., RA Pierschbacher M.D., Ruoslahti E.; RT "cDNA and amino acid sequences of the cell adhesion protein receptor RT recognizing vitronectin reveal a transmembrane domain and homologies with RT other adhesion protein receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 83:8614-8618(1986). RN [11] RP PROTEIN SEQUENCE OF 31-41. RX PubMed=2467745; DOI=10.1016/0092-8674(89)90172-4; RA Cheresh D.A., Smith J.W., Cooper H.M., Quaranta V.; RT "A novel vitronectin receptor integrin (alpha v beta x) is responsible for RT distinct adhesive properties of carcinoma cells."; RL Cell 57:59-69(1989). RN [12] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A9 RP CAPSID PROTEINS. RX PubMed=7519807; DOI=10.1006/viro.1994.1494; RA Roivainen M., Piirainen L., Hovi T., Virtanen I., Riikonen T., Heino J., RA Hyypiae T.; RT "Entry of coxsackievirus A9 into host cells: specific interactions with RT alpha v beta 3 integrin, the vitronectin receptor."; RL Virology 203:357-365(1994). RN [13] RP INTERACTION WITH COXSACKIEVIRUS B1 CAPSID PROTEINS (MICROBIAL INFECTION). RX PubMed=9426447; DOI=10.1006/viro.1997.8831; RA Agrez M.V., Shafren D.R., Gu X., Cox K., Sheppard D., Barry R.D.; RT "Integrin alpha v beta 6 enhances coxsackievirus B1 lytic infection of RT human colon cancer cells."; RL Virology 239:71-77(1997). RN [14] RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION). RX PubMed=10397733; RA Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., RA Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.; RT "The Tat protein of human immunodeficiency virus type-1 promotes vascular RT cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3 RT integrins and by mobilizing sequestered basic fibroblast growth factor."; RL Blood 94:663-672(1999). RN [15] RP FUNCTION. RX PubMed=10640428; DOI=10.1006/excr.1999.4765; RA Byzova T.V., Kim W., Midura R.J., Plow E.F.; RT "Activation of integrin alpha(V)beta(3) regulates cell adhesion and RT migration to bone sialoprotein."; RL Exp. Cell Res. 254:299-308(2000). RN [16] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN PARECHOVIRUS 1 RP CAPSID PROTEINS. RX PubMed=11160695; DOI=10.1128/jvi.75.4.1958-1967.2001; RA Joki-Korpela P., Marjomaki V., Krogerus C., Heino J., Hyypia T.; RT "Entry of human parechovirus 1."; RL J. Virol. 75:1958-1967(2001). RN [17] RP INTERACTION WITH CCN3. RX PubMed=12695522; DOI=10.1074/jbc.m302028200; RA Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y., Lau L.F.; RT "CCN3 (NOV) is a novel angiogenic regulator of the CCN protein family."; RL J. Biol. Chem. 278:24200-24208(2003). RN [18] RP FUNCTION, AND INTERACTION WITH FBN1. RX PubMed=12807887; DOI=10.1074/jbc.m303159200; RA Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J., RA Shuttleworth C.A., Humphries M.J., Kielty C.M.; RT "Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by RT alpha 5 beta 1 and alpha v beta 3 integrins."; RL J. Biol. Chem. 278:34605-34616(2003). RN [19] RP GLYCOSYLATION AT ASN-615. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [20] RP DISULFIDE BONDS. RX PubMed=14596610; DOI=10.1021/bi034726u; RA Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G., Wilkins J.A.; RT "Mass spectrometric based mapping of the disulfide bonding patterns of RT integrin alpha chains."; RL Biochemistry 42:12950-12959(2003). RN [21] RP FUNCTION. RX PubMed=15184403; DOI=10.1083/jcb.200312172; RA Annes J.P., Chen Y., Munger J.S., Rifkin D.B.; RT "Integrin alphaVbeta6-mediated activation of latent TGF-beta requires the RT latent TGF-beta binding protein-1."; RL J. Cell Biol. 165:723-734(2004). RN [22] RP INTERACTION WITH COXSACKIEVIRUS A9 CAPSID PROTEINS (MICROBIAL INFECTION). RX PubMed=15194773; DOI=10.1128/jvi.78.13.6967-6973.2004; RA Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.; RT "Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus RT A9."; RL J. Virol. 78:6967-6973(2004). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [24] RP INTERACTION WITH ADGRA2. RX PubMed=16982628; DOI=10.1074/jbc.m605291200; RA Vallon M., Essler M.; RT "Proteolytically processed soluble tumor endothelial marker (TEM) 5 RT mediates endothelial cell survival during angiogenesis by linking integrin RT alpha(v)beta3 to glycosaminoglycans."; RL J. Biol. Chem. 281:34179-34188(2006). RN [25] RP INTERACTION WITH RAB25. RX PubMed=17925226; DOI=10.1016/j.devcel.2007.08.012; RA Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W., RA Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W., RA Ozanne B.W., Norman J.C.; RT "Rab25 associates with alpha5beta1 integrin to promote invasive migration RT in 3D microenvironments."; RL Dev. Cell 13:496-510(2007). RN [26] RP FUNCTION, INTERACTION WITH FBN1, AND SUBCELLULAR LOCATION. RX PubMed=17158881; DOI=10.1074/jbc.m607008200; RA Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I., RA van der Merwe P.A., Mardon H.J., Handford P.A.; RT "alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative studies RT of molecular determinants underlying integrin-rgd affinity and RT specificity."; RL J. Biol. Chem. 282:6743-6751(2007). RN [27] RP FUNCTION, BINDING TO FGF1, AND IDENTIFICATION IN A COMPLEX WITH FGF1 AND RP FGFR1. RX PubMed=18441324; DOI=10.1074/jbc.m801213200; RA Mori S., Wu C.Y., Yamaji S., Saegusa J., Shi B., Ma Z., Kuwabara Y., RA Lam K.S., Isseroff R.R., Takada Y.K., Takada Y.; RT "Direct binding of integrin alphavbeta3 to FGF1 plays a role in FGF1 RT signaling."; RL J. Biol. Chem. 283:18066-18075(2008). RN [28] RP FUNCTION. RX PubMed=18635536; DOI=10.1074/jbc.m804835200; RA Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S., Liu F.T., RA Takada Y.K., Takada Y.; RT "Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins RT alphavbeta3 and alpha4beta1 and induces proliferation of monocytic cells in RT an integrin-dependent manner."; RL J. Biol. Chem. 283:26107-26115(2008). RN [29] RP INTERACTION WITH HHV-8 GLYCOPROTEIN B (MICROBIAL INFECTION). RX PubMed=18045938; DOI=10.1128/jvi.01673-07; RA Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.; RT "Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of Kaposi's RT sarcoma-associated herpesvirus and functions as an RGD-dependent entry RT receptor."; RL J. Virol. 82:1570-1580(2008). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [31] RP INTERACTION WITH PTN. RX PubMed=19141530; DOI=10.1096/fj.08-117564; RA Mikelis C., Sfaelou E., Koutsioumpa M., Kieffer N., Papadimitriou E.; RT "Integrin alpha(v)beta(3) is a pleiotrophin receptor required for RT pleiotrophin-induced endothelial cell migration through receptor protein RT tyrosine phosphatase beta/zeta."; RL FASEB J. 23:1459-1469(2009). RN [32] RP FUNCTION, BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH IGF1 AND RP IGF1R. RX PubMed=19578119; DOI=10.1074/jbc.m109.013201; RA Saegusa J., Yamaji S., Ieguchi K., Wu C.Y., Lam K.S., Liu F.T., RA Takada Y.K., Takada Y.; RT "The direct binding of insulin-like growth factor-1 (IGF-1) to integrin RT alphavbeta3 is involved in IGF-1 signaling."; RL J. Biol. Chem. 284:24106-24114(2009). RN [33] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615; ASN-704 AND RP ASN-874. 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 [34] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-874. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [35] RP FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1 AND RP ERBB3. RX PubMed=20682778; DOI=10.1074/jbc.m110.113878; RA Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K., RA Wang B., Takada Y.K., Takada Y.; RT "Direct binding of the EGF-like domain of neuregulin-1 to integrins RT ({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB RT signaling."; RL J. Biol. Chem. 285:31388-31398(2010). RN [36] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS TYPE C RP PENTON PROTEIN. RX PubMed=20615244; DOI=10.1186/1743-422x-7-148; RA Lyle C., McCormick F.; RT "Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative RT cells."; RL Virol. J. 7:148-148(2010). RN [37] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [38] RP FUNCTION, BINDING TO CX3CL1, AND IDENTIFICATION IN A COMPLEX WITH CX3CR1 RP AND CX3CL1. RX PubMed=23125415; DOI=10.4049/jimmunol.1200889; RA Fujita M., Takada Y.K., Takada Y.; RT "Integrins alphavbeta3 and alpha4beta1 act as coreceptors for fractalkine, RT and the integrin-binding defective mutant of fractalkine is an antagonist RT of CX3CR1."; RL J. Immunol. 189:5809-5819(2012). RN [39] RP INTERACTION WITH CIB1. RX PubMed=24011356; DOI=10.1021/bi400678y; RA Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I., Tripathy A., RA Dokholyan N.V., Leisner T.M., Parise L.V.; RT "Identification of novel integrin binding partners for calcium and integrin RT binding protein 1 (CIB1): structural and thermodynamic basis of CIB1 RT promiscuity."; RL Biochemistry 52:7082-7090(2013). RN [40] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLEX VIRUS 1 RP ENVELOPE GLYCOPROTEIN H. RX PubMed=24367260; DOI=10.1371/journal.ppat.1003806; RA Gianni T., Salvioli S., Chesnokova L.S., Hutt-Fletcher L.M., RA Campadelli-Fiume G.; RT "alphavbeta6- and alphavbeta8-integrins serve as interchangeable receptors RT for HSV gH/gL to promote endocytosis and activation of membrane fusion."; RL PLoS Pathog. 9:E1003806-E1003806(2013). RN [41] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH WEST NILE VIRUS RP ENVELOPE PROTEIN E. RX PubMed=23658209; DOI=10.1099/vir.0.052613-0; RA Schmidt K., Keller M., Bader B.L., Korytar T., Finke S., Ziegler U., RA Groschup M.H.; RT "Integrins modulate the infection efficiency of West Nile virus into RT cells."; RL J. Gen. Virol. 94:1723-1733(2013). RN [42] RP FUNCTION, AND INTERACTION WITH TGFB1. RX PubMed=22278742; DOI=10.1091/mbc.e11-12-1018; RA Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.; RT "GARP regulates the bioavailability and activation of TGFbeta."; RL Mol. Biol. Cell 23:1129-1139(2012). RN [43] RP INTERACTION WITH HERPES SIMPLEX VIRUS 2 GLYCOPROTEIN H (MICROBIAL RP INFECTION). RX PubMed=24942591; DOI=10.1128/jvi.00725-14; RA Cheshenko N., Trepanier J.B., Gonzalez P.A., Eugenin E.A., Jacobs W.R. Jr., RA Herold B.C.; RT "Herpes simplex virus type 2 glycoprotein H interacts with integrin RT alphavbeta3 to facilitate viral entry and calcium signaling in human RT genital tract epithelial cells."; RL J. Virol. 88:10026-10038(2014). RN [44] RP FUNCTION. RX PubMed=25398877; DOI=10.1074/jbc.m114.579946; RA Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J., Takada Y.K., RA Takada Y.; RT "Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces RT integrin activation through direct binding to a newly identified binding RT site (site 2) in integrins alphavbeta3, alpha4beta1, and alpha5beta1."; RL J. Biol. Chem. 290:259-271(2015). RN [45] RP INTERACTION WITH CD9; CD81 AND CD151. RX PubMed=27993971; DOI=10.1042/bcj20160998; RA Yu J., Lee C.Y., Changou C.A., Cedano-Prieto D.M., Takada Y.K., Takada Y.; RT "The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding RT site of integrin alphavbeta3."; RL Biochem. J. 474:589-596(2017). RN [46] RP FUNCTION, AND INTERACTION WITH FGF2. RX PubMed=28302677; DOI=10.1042/bsr20170173; RA Mori S., Hatori N., Kawaguchi N., Hamada Y., Shih T.C., Wu C.Y., Lam K.S., RA Matsuura N., Yamamoto H., Takada Y.K., Takada Y.; RT "The integrin-binding defective FGF2 mutants potently suppress FGF2 RT signalling and angiogenesis."; RL Biosci. Rep. 37:0-0(2017). RN [47] RP FUNCTION, AND INTERACTION WITH IL1B. RX PubMed=29030430; DOI=10.1074/jbc.m117.818302; RA Takada Y.K., Yu J., Fujita M., Saegusa J., Wu C.Y., Takada Y.; RT "Direct binding to integrins and loss of disulfide linkage in interleukin- RT 1beta (IL-1beta) are involved in the agonistic action of IL-1beta."; RL J. Biol. Chem. 292:20067-20075(2017). RN [48] RP FUNCTION, AND INTERACTION WITH IGF2. RX PubMed=28873464; DOI=10.1371/journal.pone.0184285; RA Cedano Prieto D.M., Cheng Y., Chang C.C., Yu J., Takada Y.K., Takada Y.; RT "Direct integrin binding to insulin-like growth factor-2 through the C- RT domain is required for insulin-like growth factor receptor type 1 (IGF1R) RT signaling."; RL PLoS ONE 12:E0184285-E0184285(2017). RN [49] RP FUNCTION. RX PubMed=31331973; DOI=10.4049/jimmunol.1801630; RA Takada Y.K., Yu J., Shimoda M., Takada Y.; RT "Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role RT in CD40/CD40L Signaling."; RL J. Immunol. 203:1383-1391(2019). RN [50] RP INTERACTION WITH SELP. RX PubMed=37184585; DOI=10.26508/lsa.202201747; RA Takada Y.K., Simon S.I., Takada Y.; RT "The C-type lectin domain of CD62P (P-selectin) functions as an integrin RT ligand."; RL Life. Sci Alliance 6:0-0(2023). RN [51] RP INTERACTION WITH TM4SF19. RX PubMed=38016540; DOI=10.1016/j.metabol.2023.155746; RA Park S., Heo J.S., Mizuno S., Kim M., An H., Hong E., Kang M.G., Kim J., RA Yun R., Park H., Noh E.H., Lee M.J., Yoon K., Kim P., Son M., Pang K., RA Lee J., Park J., Ooshima A., Kim T.J., Park J.Y., Yang K.M., Myung S.J., RA Bae H., Lee K.M., Letterio J., Park S.H., Takahashi S., Kim S.J.; RT "Tm4sf19 deficiency inhibits osteoclast multinucleation and prevents bone RT loss."; RL Metabolism 151:155746-155746(2024). RN [52] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 31-987. RX PubMed=11546839; DOI=10.1126/science.1064535; RA Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., RA Joachimiak A., Goodman S.L., Arnaout M.A.; RT "Crystal structure of the extracellular segment of integrin alpha Vbeta3."; RL Science 294:339-345(2001). RN [53] {ECO:0007744|PDB:3IJE} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-997 IN COMPLEX WITH ITGB3 AND RP CALCIUM, GLYCOSYLATION AT ASN-74; ASN-290; ASN-296; ASN-488; ASN-554; RP ASN-615; ASN-835; ASN-973 AND ASN-980, DISULFIDE BONDS, AND MUTAGENESIS OF RP 1020-PHE-PHE-1021. RX PubMed=19704023; DOI=10.1083/jcb.200905085; RA Xiong J.P., Mahalingham B., Alonso J.L., Borrelli L.A., Rui X., Anand S., RA Hyman B.T., Rysiok T., Mueller-Pompalla D., Goodman S.L., Arnaout M.A.; RT "Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an RT alpha/beta transmembrane fragment."; RL J. Cell Biol. 186:589-600(2009). RN [54] {ECO:0007744|PDB:5FFG, ECO:0007744|PDB:5FFO} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 31-627 IN COMPLEX WITH TGFB1; RP ITGB6 AND CALCIUM, FUNCTION, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT RP ASN-74; ASN-290; ASN-296; ASN-488; ASN-554 AND ASN-615. RX PubMed=28117447; DOI=10.1038/nature21035; RA Dong X., Zhao B., Iacob R.E., Zhu J., Koksal A.C., Lu C., Engen J.R., RA Springer T.A.; RT "Force interacts with macromolecular structure in activation of TGF-beta."; RL Nature 542:55-59(2017). CC -!- FUNCTION: The alpha-V (ITGAV) integrins are receptors for vitronectin, CC cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase- CC 2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They CC recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 CC binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1- CC dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to CC NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB CC signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding CC is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to CC FGF2 and this binding is essential for FGF2 signaling CC (PubMed:28302677). ITGAV:ITGB3 binds to IGF1 and this binding is CC essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to CC IGF2 and this binding is essential for IGF2 signaling CC (PubMed:28873464). ITGAV:ITGB3 binds to IL1B and this binding is CC essential for IL1B signaling (PubMed:29030430). ITGAV:ITGB3 binds to CC PLA2G2A via a site (site 2) which is distinct from the classical CC ligand-binding site (site 1) and this induces integrin conformational CC changes and enhanced ligand binding to site 1 (PubMed:18635536, CC PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for CC fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 CC (PubMed:12807887, PubMed:17158881). Integrin alpha-V/beta-6 or alpha- CC V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release CC of transforming growth factor beta-1 (TGF-beta-1) from regulatory CC Latency-associated peptide (LAP), thereby playing a key role in TGF- CC beta-1 activation (PubMed:15184403, PubMed:22278742, PubMed:28117447). CC ITGAV:ITGB3 acts as a receptor for CD40LG (PubMed:31331973). CC ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and CC migration to IBSP (PubMed:10640428). {ECO:0000269|PubMed:10640428, CC ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:15184403, CC ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18441324, CC ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:19578119, CC ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22278742, CC ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:25398877, CC ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:28302677, CC ECO:0000269|PubMed:28873464, ECO:0000269|PubMed:29030430, CC ECO:0000269|PubMed:31331973}. CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor CC for Adenovirus type C. {ECO:0000269|PubMed:20615244}. CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 and ITGAV:ITGB3 CC act as receptors for Coxsackievirus A9 and B1. CC {ECO:0000269|PubMed:15194773, ECO:0000269|PubMed:7519807, CC ECO:0000269|PubMed:9426447}. CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor CC for Herpes virus 8/HHV-8. {ECO:0000269|PubMed:18045938}. CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB6 acts as a receptor CC for herpes simplex 1/HHV-1. {ECO:0000269|PubMed:24367260}. CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor CC for Human parechovirus 1. {ECO:0000269|PubMed:11160695}. CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor CC for West nile virus. {ECO:0000269|PubMed:23658209}. CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, the CC interaction with extracellular viral Tat protein seems to enhance CC angiogenesis in Kaposi's sarcoma lesions. CC {ECO:0000269|PubMed:10397733}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit CC is composed of a heavy and a light chain linked by a disulfide bond. CC Alpha-V (ITGAV) associates with either beta-1 (ITGB1), beta-3 (ITGB3), CC beta-5 (ITGB5), beta-6 (ITGB6) or beta-8 (ITGB8). Interacts with CIB1 CC (PubMed:24011356). Interacts with RAB25 (PubMed:17925226). Integrins CC ITGAV:ITGB3 and ITGAV:ITGB5 interact with FBLN5 (via N-terminus) (By CC similarity). ITGAV:ITGB3 and ITGAV:ITGB5 interact with CCN3 CC (PubMed:12695522). ITGAV:ITGB3 interacts with ADGRA2 (PubMed:16982628). CC ITGAV:ITGB3 interacts with FGF2; it is likely that FGF2 can CC simultaneously bind ITGAV:ITGB3 and FGF receptors (PubMed:28302677). CC ITGAV:ITGB3 interacts with IL1B (PubMed:29030430). ITGAV:ITGB3 CC interacts with SELP (via C-type lectin domain); the interaction CC mediates cell-cell interaction and adhesion (PubMed:37184585). CC ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1 CC (PubMed:23125415). ITGAV:ITGB3 is found in a ternary complex with NRG1 CC and ERBB3 (PubMed:20682778). ITGAV:ITGB3 is found in a ternary complex CC with FGF1 and FGFR1 (PubMed:18441324). ITGAV:ITGB3 is found in a CC ternary complex with IGF1 and IGF1R (PubMed:19578119). ITGAV:ITGB3 CC interacts with IGF2 (PubMed:28873464). ITGAV:ITGB3 and ITGAV:ITGB6 CC interact with FBN1 (PubMed:12807887, PubMed:17158881). ITGAV:ITGB3 CC interacts with CD9, CD81 and CD151 (via second extracellular domain) CC (PubMed:27993971). ITGAV:ITGB6 interacts with TGFB1 (PubMed:22278742, CC PubMed:28117447). ITGAV:ITGB3 interacts with PTN (PubMed:19141530). CC Forms a complex with PTPRZ1 and PTN that stimulates endothelial cell CC migration through ITGB3 'Tyr-773' phosphorylation (PubMed:19141530). CC Interacts with TM4SF19 (PubMed:38016540). CC {ECO:0000250|UniProtKB:P43406, ECO:0000250|UniProtKB:P80746, CC ECO:0000269|PubMed:12695522, ECO:0000269|PubMed:12807887, CC ECO:0000269|PubMed:16982628, ECO:0000269|PubMed:17158881, CC ECO:0000269|PubMed:17925226, ECO:0000269|PubMed:18441324, CC ECO:0000269|PubMed:19141530, ECO:0000269|PubMed:19578119, CC ECO:0000269|PubMed:20615244, ECO:0000269|PubMed:20682778, CC ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:23125415, CC ECO:0000269|PubMed:23658209, ECO:0000269|PubMed:24011356, CC ECO:0000269|PubMed:27993971, ECO:0000269|PubMed:28117447, CC ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:28873464, CC ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:37184585, CC ECO:0000269|PubMed:38016540}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with CC herpes virus 8/HHV-8 envelope glycoprotein B. CC {ECO:0000269|PubMed:18045938}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 and ITGAV:ITGB6 CC bind to coxsackievirus A9 and coxsackievirus B1 capsid proteins CC (PubMed:15194773, PubMed:7519807, PubMed:9426447). CC {ECO:0000269|PubMed:15194773, ECO:0000269|PubMed:7519807, CC ECO:0000269|PubMed:9426447}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB6 interacts with CC herpes simplex 1/HHV-1 envelope glycoprotein H. CC {ECO:0000269|PubMed:24367260}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with CC Herpes simplex 2/HHV-2 envelope glycoprotein H. CC {ECO:0000269|PubMed:24942591}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB5 interacts with CC adenovirus type C penton protein. {ECO:0000269|PubMed:20615244}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with CC Human parechovirus 1 capsid proteins. {ECO:0000269|PubMed:11160695}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with West CC nile virus envelope protein E. {ECO:0000269|PubMed:23658209}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat. CC {ECO:0000269|PubMed:10397733}. CC -!- INTERACTION: CC P06756; P05106: ITGB3; NbExp=13; IntAct=EBI-298282, EBI-702847; CC P06756; P18084: ITGB5; NbExp=2; IntAct=EBI-298282, EBI-1223434; CC P06756; P18564: ITGB6; NbExp=8; IntAct=EBI-298282, EBI-2568070; CC P06756; Q38SD2-2: LRRK1; NbExp=3; IntAct=EBI-298282, EBI-25929016; CC P06756; P17612: PRKACA; NbExp=3; IntAct=EBI-298282, EBI-476586; CC P06756; P54725: RAD23A; NbExp=3; IntAct=EBI-298282, EBI-746453; CC P06756; P50454: SERPINH1; NbExp=3; IntAct=EBI-298282, EBI-350723; CC P06756; P37173: TGFBR2; NbExp=3; IntAct=EBI-298282, EBI-296151; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P06756-1; Sequence=Displayed; CC Name=2; CC IsoId=P06756-2; Sequence=VSP_024351; CC Name=3; CC IsoId=P06756-3; Sequence=VSP_044914; CC -!- MISCELLANEOUS: The constitutive activation of ITGAV:ITGB3 on neoplastic CC cells may contribute to tumor growth and metastatic potential. CC {ECO:0000269|PubMed:10640428}. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD93131.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; M14648; AAA36808.1; -; mRNA. DR EMBL; AF251841; AAG03000.1; -; Genomic_DNA. DR EMBL; AF251818; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251819; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251820; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251821; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251822; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251823; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251824; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251825; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251826; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251827; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251828; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251829; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251830; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251831; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251832; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251833; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251834; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251835; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251836; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251837; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251838; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251839; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AF251840; AAG03000.1; JOINED; Genomic_DNA. DR EMBL; AK302990; BAH13869.1; -; mRNA. DR EMBL; AB209894; BAD93131.1; ALT_INIT; mRNA. DR EMBL; AC017101; AAY24257.1; -; Genomic_DNA. DR EMBL; EU332844; ABY87533.1; -; Genomic_DNA. DR EMBL; CH471058; EAX10934.1; -; Genomic_DNA. DR EMBL; BC126231; AAI26232.1; -; mRNA. DR EMBL; BC136442; AAI36443.1; -; mRNA. DR EMBL; BC144100; AAI44101.1; -; mRNA. DR EMBL; U07375; AAA61631.1; -; Genomic_DNA. DR CCDS; CCDS2292.1; -. [P06756-1] DR CCDS; CCDS46470.1; -. [P06756-2] DR CCDS; CCDS46471.1; -. [P06756-3] DR PIR; A27421; A27421. DR RefSeq; NP_001138471.1; NM_001144999.2. [P06756-3] DR RefSeq; NP_001138472.1; NM_001145000.2. [P06756-2] DR RefSeq; NP_002201.1; NM_002210.4. [P06756-1] DR PDB; 1JV2; X-ray; 3.10 A; A=31-987. DR PDB; 1L5G; X-ray; 3.20 A; A=31-987. DR PDB; 1M1X; X-ray; 3.30 A; A=31-987. DR PDB; 1U8C; X-ray; 3.10 A; A=31-987. DR PDB; 3IJE; X-ray; 2.90 A; A=31-997. DR PDB; 4G1E; X-ray; 3.00 A; A=31-989. DR PDB; 4G1M; X-ray; 2.90 A; A=31-989. DR PDB; 4MMX; X-ray; 3.32 A; A=31-989. DR PDB; 4MMY; X-ray; 3.18 A; A=31-989. DR PDB; 4MMZ; X-ray; 3.10 A; A=31-989. DR PDB; 4O02; X-ray; 3.60 A; A=31-992. DR PDB; 4UM8; X-ray; 2.85 A; A/C=31-625. DR PDB; 4UM9; X-ray; 2.50 A; A/C=31-625. DR PDB; 5FFG; X-ray; 2.25 A; A=31-625. DR PDB; 5FFO; X-ray; 3.49 A; A/E=31-625. DR PDB; 5NEM; EM; 3.10 A; A=31-624. DR PDB; 5NER; EM; 3.10 A; A=31-624. DR PDB; 5NET; EM; 3.10 A; A=31-624. DR PDB; 5NEU; EM; 3.10 A; A=31-624. DR PDB; 6AVQ; EM; 35.00 A; A=31-987. DR PDB; 6AVR; EM; 35.00 A; A=31-987. DR PDB; 6AVU; EM; 35.00 A; A=31-987. DR PDB; 6DJP; EM; 4.80 A; A=31-995. DR PDB; 6MK0; X-ray; 3.00 A; A=31-984. DR PDB; 6MSL; X-ray; 3.10 A; A=31-997. DR PDB; 6MSU; X-ray; 3.11 A; A=31-997. DR PDB; 6NAJ; X-ray; 3.10 A; A=31-984. DR PDB; 6OM1; X-ray; 2.66 A; A/C/E/G=31-624. DR PDB; 6OM2; X-ray; 2.77 A; A/C=31-624. DR PDB; 6UJA; EM; 3.30 A; A=31-1048. DR PDB; 6UJB; EM; 3.51 A; A=31-1048. DR PDB; 6UJC; EM; 3.56 A; A=31-1048. DR PDB; 7Y1T; EM; 3.24 A; A=1-625. DR PDB; 8IJ5; EM; 3.00 A; E=31-623. DR PDB; 8TCF; EM; 2.90 A; A=31-473. DR PDB; 8TCG; EM; 3.40 A; A=31-469. DR PDBsum; 1JV2; -. DR PDBsum; 1L5G; -. DR PDBsum; 1M1X; -. DR PDBsum; 1U8C; -. DR PDBsum; 3IJE; -. DR PDBsum; 4G1E; -. DR PDBsum; 4G1M; -. DR PDBsum; 4MMX; -. DR PDBsum; 4MMY; -. DR PDBsum; 4MMZ; -. DR PDBsum; 4O02; -. DR PDBsum; 4UM8; -. DR PDBsum; 4UM9; -. DR PDBsum; 5FFG; -. DR PDBsum; 5FFO; -. DR PDBsum; 5NEM; -. DR PDBsum; 5NER; -. DR PDBsum; 5NET; -. DR PDBsum; 5NEU; -. DR PDBsum; 6AVQ; -. DR PDBsum; 6AVR; -. DR PDBsum; 6AVU; -. DR PDBsum; 6DJP; -. DR PDBsum; 6MK0; -. DR PDBsum; 6MSL; -. DR PDBsum; 6MSU; -. DR PDBsum; 6NAJ; -. DR PDBsum; 6OM1; -. DR PDBsum; 6OM2; -. DR PDBsum; 6UJA; -. DR PDBsum; 6UJB; -. DR PDBsum; 6UJC; -. DR PDBsum; 7Y1T; -. DR PDBsum; 8IJ5; -. DR PDBsum; 8TCF; -. DR PDBsum; 8TCG; -. DR AlphaFoldDB; P06756; -. DR EMDB; EMD-20794; -. DR EMDB; EMD-20795; -. DR EMDB; EMD-20796; -. DR EMDB; EMD-33572; -. DR EMDB; EMD-33573; -. DR EMDB; EMD-35465; -. DR EMDB; EMD-3632; -. DR EMDB; EMD-3633; -. DR EMDB; EMD-3634; -. DR EMDB; EMD-3635; -. DR EMDB; EMD-41153; -. DR EMDB; EMD-41154; -. DR EMDB; EMD-5955; -. DR EMDB; EMD-5956; -. DR EMDB; EMD-5957; -. DR EMDB; EMD-5958; -. DR EMDB; EMD-5959; -. DR EMDB; EMD-5960; -. DR EMDB; EMD-5961; -. DR EMDB; EMD-5962; -. DR EMDB; EMD-5963; -. DR EMDB; EMD-5964; -. DR EMDB; EMD-5965; -. DR EMDB; EMD-5966; -. DR EMDB; EMD-5967; -. DR EMDB; EMD-5968; -. DR EMDB; EMD-5969; -. DR EMDB; EMD-5970; -. DR EMDB; EMD-5971; -. DR EMDB; EMD-5972; -. DR EMDB; EMD-5973; -. DR EMDB; EMD-7011; -. DR EMDB; EMD-7012; -. DR EMDB; EMD-7013; -. DR EMDB; EMD-7939; -. DR SMR; P06756; -. DR BioGRID; 109891; 217. DR ComplexPortal; CPX-1795; Integrin alphav-beta3 complex. DR ComplexPortal; CPX-1796; Integrin alphav-beta5 complex. DR ComplexPortal; CPX-1819; Integrin alphav-beta1 complex. DR ComplexPortal; CPX-1820; Integrin alphav-beta6 complex. DR ComplexPortal; CPX-1821; Integrin alphav-beta8 complex. DR CORUM; P06756; -. DR DIP; DIP-31785N; -. DR ELM; P06756; -. DR IntAct; P06756; 81. DR MINT; P06756; -. DR STRING; 9606.ENSP00000261023; -. DR BindingDB; P06756; -. DR ChEMBL; CHEMBL3660; -. DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit). DR DrugBank; DB00451; Levothyroxine. DR DrugBank; DB16515; PLN-74809. DR GuidetoPHARMACOLOGY; 2453; -. DR TCDB; 8.A.54.1.4; the integrin (integrin) family. DR GlyConnect; 1412; 28 N-Linked glycans (4 sites). DR GlyCosmos; P06756; 13 sites, 28 glycans. DR GlyGen; P06756; 14 sites, 98 N-linked glycans (6 sites), 1 O-linked glycan (1 site). DR iPTMnet; P06756; -. DR PhosphoSitePlus; P06756; -. DR SwissPalm; P06756; -. DR BioMuta; ITGAV; -. DR DMDM; 143811408; -. DR jPOST; P06756; -. DR MassIVE; P06756; -. DR PaxDb; 9606-ENSP00000261023; -. DR PeptideAtlas; P06756; -. DR ProteomicsDB; 18948; -. DR ProteomicsDB; 51933; -. [P06756-1] DR ProteomicsDB; 51934; -. [P06756-2] DR Pumba; P06756; -. DR ABCD; P06756; 80 sequenced antibodies. DR Antibodypedia; 1498; 1473 antibodies from 48 providers. DR DNASU; 3685; -. DR Ensembl; ENST00000261023.8; ENSP00000261023.3; ENSG00000138448.13. [P06756-1] DR Ensembl; ENST00000374907.7; ENSP00000364042.3; ENSG00000138448.13. [P06756-2] DR Ensembl; ENST00000433736.6; ENSP00000404291.2; ENSG00000138448.13. [P06756-3] DR GeneID; 3685; -. DR KEGG; hsa:3685; -. DR MANE-Select; ENST00000261023.8; ENSP00000261023.3; NM_002210.5; NP_002201.2. DR UCSC; uc002upq.5; human. [P06756-1] DR AGR; HGNC:6150; -. DR CTD; 3685; -. DR DisGeNET; 3685; -. DR GeneCards; ITGAV; -. DR HGNC; HGNC:6150; ITGAV. DR HPA; ENSG00000138448; Low tissue specificity. DR MIM; 193210; gene. DR neXtProt; NX_P06756; -. DR OpenTargets; ENSG00000138448; -. DR PharmGKB; PA37336; -. DR VEuPathDB; HostDB:ENSG00000138448; -. DR eggNOG; KOG3637; Eukaryota. DR GeneTree; ENSGT00940000158361; -. DR HOGENOM; CLU_004111_4_0_1; -. DR InParanoid; P06756; -. DR OMA; YILHYEV; -. DR OrthoDB; 3816176at2759; -. DR PhylomeDB; P06756; -. DR TreeFam; TF105391; -. DR PathwayCommons; P06756; -. DR Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes). DR Reactome; R-HSA-1566948; Elastic fibre formation. DR Reactome; R-HSA-210990; PECAM1 interactions. DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. DR Reactome; R-HSA-3000157; Laminin interactions. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-HSA-445144; Signal transduction by L1. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P06756; -. DR SIGNOR; P06756; -. DR BioGRID-ORCS; 3685; 335 hits in 1189 CRISPR screens. DR ChiTaRS; ITGAV; human. DR EvolutionaryTrace; P06756; -. DR GeneWiki; ITGAV; -. DR GenomeRNAi; 3685; -. DR Pharos; P06756; Tchem. DR PRO; PR:P06756; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P06756; protein. DR Bgee; ENSG00000138448; Expressed in pigmented layer of retina and 213 other cell types or tissues. DR ExpressionAtlas; P06756; baseline and differential. DR GO; GO:0035868; C:alphav-beta3 integrin-HMGB1 complex; IDA:BHF-UCL. DR GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IDA:BHF-UCL. DR GO; GO:0035866; C:alphav-beta3 integrin-PKCalpha complex; NAS:BHF-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0034682; C:integrin alphav-beta1 complex; IPI:ComplexPortal. DR GO; GO:0034683; C:integrin alphav-beta3 complex; IDA:UniProtKB. DR GO; GO:0034684; C:integrin alphav-beta5 complex; IDA:UniProtKB. DR GO; GO:0034685; C:integrin alphav-beta6 complex; IDA:UniProtKB. DR GO; GO:0034686; C:integrin alphav-beta8 complex; IDA:UniProtKB. DR GO; GO:0008305; C:integrin complex; IDA:BHF-UCL. DR GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:BHF-UCL. DR GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB. DR GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB. DR GO; GO:0050840; F:extracellular matrix binding; IDA:UniProtKB. DR GO; GO:1990430; F:extracellular matrix protein binding; IDA:UniProtKB. DR GO; GO:0001968; F:fibronectin binding; IDA:UniProtKB. DR GO; GO:0005178; F:integrin binding; IPI:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001846; F:opsonin binding; IEA:Ensembl. DR GO; GO:0002020; F:protease binding; IDA:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl. DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IEP:UniProtKB. DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0043277; P:apoptotic cell clearance; IGI:BHF-UCL. DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IDA:BHF-UCL. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB. DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB. DR GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB. DR GO; GO:0085017; P:entry into host cell by a symbiont-containing vacuole; NAS:BHF-UCL. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:BHF-UCL. DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISS:BHF-UCL. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:ComplexPortal. DR GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB. DR GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; IDA:BHF-UCL. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL. DR GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL. DR GO; GO:0032369; P:negative regulation of lipid transport; IMP:BHF-UCL. DR GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; IMP:BHF-UCL. DR GO; GO:1905598; P:negative regulation of low-density lipoprotein receptor activity; IMP:BHF-UCL. DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL. DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL. DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IMP:BHF-UCL. DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl. DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IMP:BHF-UCL. DR GO; GO:0050764; P:regulation of phagocytosis; IDA:BHF-UCL. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB. DR GO; GO:0046718; P:symbiont entry into host cell; IMP:UniProtKB. DR GO; GO:0071604; P:transforming growth factor beta production; IEA:Ensembl. DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl. DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; NAS:ComplexPortal. DR DisProt; DP02742; -. DR FunFam; 2.130.10.130:FF:000003; Integrin alpha V; 1. DR FunFam; 2.60.40.1510:FF:000001; Integrin alpha V; 1. DR FunFam; 2.60.40.1530:FF:000002; integrin alpha-V isoform X2; 1. DR FunFam; 1.20.5.930:FF:000001; Integrin subunit alpha V; 1. DR FunFam; 2.60.40.1460:FF:000001; Integrin, alpha V; 1. DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1. DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR048286; Integrin_alpha_Ig-like_3. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF4; INTEGRIN ALPHA-V; 1. DR Pfam; PF01839; FG-GAP; 3. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF20806; Integrin_A_Ig_3; 1. DR Pfam; PF00357; Integrin_alpha; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction; KW Cell membrane; Cleavage on pair of basic residues; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; Integrin; KW Membrane; Metal-binding; Proteomics identification; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..30 FT /evidence="ECO:0000269|PubMed:2467745" FT CHAIN 31..1048 FT /note="Integrin alpha-V" FT /id="PRO_0000016301" FT CHAIN 31..889 FT /note="Integrin alpha-V heavy chain" FT /id="PRO_0000016302" FT CHAIN 891..1048 FT /note="Integrin alpha-V light chain" FT /id="PRO_0000016303" FT TOPO_DOM 31..992 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 993..1016 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1017..1048 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 32..98 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 109..170 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 173..225 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 237..291 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 292..357 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 358..415 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 419..482 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REGION 1027..1048 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1019..1023 FT /note="GFFKR motif" FT BINDING 260 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 262 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 264 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 266 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 314 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 316 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 318 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 320 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 322 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 379 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 381 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 383 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 385 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 387 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 443 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 445 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 447 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 449 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT BINDING 451 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE, FT ECO:0007744|PDB:5FFG" FT CARBOHYD 74 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE" FT CARBOHYD 290 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE" FT CARBOHYD 296 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE" FT CARBOHYD 488 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE" FT CARBOHYD 554 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE" FT CARBOHYD 615 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19704023, FT ECO:0000269|PubMed:28117447, ECO:0007744|PDB:3IJE" FT CARBOHYD 704 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 835 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0007744|PDB:3IJE" FT CARBOHYD 851 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 874 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973" FT CARBOHYD 945 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 973 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0007744|PDB:3IJE" FT CARBOHYD 980 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19704023, FT ECO:0007744|PDB:3IJE" FT DISULFID 89..97 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0000269|PubMed:28117447, FT ECO:0007744|PDB:3IJE" FT DISULFID 138..158 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0000269|PubMed:28117447, FT ECO:0007744|PDB:3IJE" FT DISULFID 172..185 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0000269|PubMed:28117447, FT ECO:0007744|PDB:3IJE" FT DISULFID 491..502 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE" FT DISULFID 508..565 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE" FT DISULFID 626..632 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE" FT DISULFID 698..711 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE" FT DISULFID 852..914 FT /note="Interchain (between heavy and light chains)" FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE" FT DISULFID 904..909 FT /evidence="ECO:0000269|PubMed:14596610, FT ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE" FT VAR_SEQ 1..62 FT /note="MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFA FT VDFFVPSASS -> MLLGTLLLILYILMLC (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044914" FT VAR_SEQ 175..211 FT /note="QDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQG -> R (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_024351" FT VARIANT 405 FT /note="I -> V (in dbSNP:rs3738918)" FT /id="VAR_024289" FT VARIANT 548 FT /note="S -> A (in dbSNP:rs2230615)" FT /id="VAR_055970" FT VARIANT 783 FT /note="V -> I (in dbSNP:rs2230616)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2430295, FT ECO:0000269|PubMed:2443500, ECO:0000269|Ref.4, FT ECO:0000269|Ref.6, ECO:0000269|Ref.7" FT /id="VAR_031547" FT MUTAGEN 1020..1021 FT /note="FF->AA: Increases ligand-binding activity." FT /evidence="ECO:0000269|PubMed:19704023" FT CONFLICT 425 FT /note="W -> R (in Ref. 2; AAG03000)" FT /evidence="ECO:0000305" FT CONFLICT 700 FT /note="F -> L (in Ref. 8; AAI44101)" FT /evidence="ECO:0000305" FT CONFLICT 1039 FT /note="H -> R (in Ref. 2; AAG03000)" FT /evidence="ECO:0000305" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:6MSL" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:5FFG" FT TURN 45..50 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:4UM9" FT STRAND 65..70 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 85..95 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 126..131 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 147..150 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:5FFG" FT TURN 178..184 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:5FFG" FT HELIX 206..209 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 211..217 FT /evidence="ECO:0007829|PDB:5FFG" FT HELIX 218..223 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:6OM2" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 254..259 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 261..266 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 268..273 FT /evidence="ECO:0007829|PDB:5FFG" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:5FFG" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 293..298 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 308..313 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 322..327 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:4G1M" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 344..350 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 364..368 FT /evidence="ECO:0007829|PDB:1JV2" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:6MK0" FT STRAND 374..378 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 387..392 FT /evidence="ECO:0007829|PDB:5FFG" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 402..409 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 410..413 FT /evidence="ECO:0007829|PDB:4UM8" FT STRAND 418..422 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:4UM9" FT STRAND 436..442 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 451..456 FT /evidence="ECO:0007829|PDB:5FFG" FT HELIX 457..459 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 470..485 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 489..492 FT /evidence="ECO:0007829|PDB:6UJA" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:6OM2" FT STRAND 502..512 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 514..516 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 519..528 FT /evidence="ECO:0007829|PDB:5FFG" FT TURN 529..532 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 535..537 FT /evidence="ECO:0007829|PDB:6OM2" FT STRAND 541..543 FT /evidence="ECO:0007829|PDB:5FFG" FT TURN 544..546 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 547..558 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:6MSU" FT STRAND 564..572 FT /evidence="ECO:0007829|PDB:5FFG" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 581..583 FT /evidence="ECO:0007829|PDB:6MSL" FT STRAND 585..593 FT /evidence="ECO:0007829|PDB:5FFG" FT TURN 595..597 FT /evidence="ECO:0007829|PDB:4UM9" FT STRAND 601..603 FT /evidence="ECO:0007829|PDB:4G1E" FT STRAND 610..612 FT /evidence="ECO:0007829|PDB:5FFG" FT STRAND 614..623 FT /evidence="ECO:0007829|PDB:5FFG" FT TURN 627..630 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 636..641 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 646..648 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 653..663 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 668..670 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 672..676 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 681..686 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:4G1E" FT STRAND 697..701 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 703..705 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 708..712 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 715..717 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 722..731 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 735..737 FT /evidence="ECO:0007829|PDB:4G1E" FT STRAND 739..748 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 752..754 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 760..767 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 772..786 FT /evidence="ECO:0007829|PDB:3IJE" FT TURN 798..802 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 805..814 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 816..818 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 820..833 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 839..856 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 900..902 FT /evidence="ECO:0007829|PDB:3IJE" FT TURN 904..906 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 907..916 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 923..933 FT /evidence="ECO:0007829|PDB:3IJE" FT HELIX 935..938 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 941..944 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 948..960 FT /evidence="ECO:0007829|PDB:3IJE" FT STRAND 964..966 FT /evidence="ECO:0007829|PDB:4G1E" FT STRAND 971..982 FT /evidence="ECO:0007829|PDB:3IJE" SQ SEQUENCE 1048 AA; 116038 MW; 364EE25C5303A2D7 CRC64; MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVDSPAE YSGPEGSYFG FAVDFFVPSA SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSTRRCQPI EFDATGNRDY AKDDPLEFKS HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSQDIDAD GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IVSKYDPNVY SIKYNNQLAT RTAQAIFDDS YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVYIYDGKN MSSLYNFTGE QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ RASGDFQTTK LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK GIVYIFNGRS TGLNAVPSQI LEGQWAARSM PPSFGYSMKG ATDIDKNGYP DLIVGAFGVD RAILYRARPV ITVNAGLEVY PSILNQDNKT CSLPGTALKV SCFNVRFCLK ADGKGVLPRK LNFQVELLLD KLKQKGAIRR ALFLYSRSPS HSKNMTISRG GLMQCEELIA YLRDESEFRD KLTPITIFME YRLDYRTAAD TTGLQPILNQ FTPANISRQA HILLDCGEDN VCKPKLEVSV DSDQKKIYIG DDNPLTLIVK AQNQGEGAYE AELIVSIPLQ ADFIGVVRNN EALARLSCAF KTENQTRQVV CDLGNPMKAG TQLLAGLRFS VHQQSEMDTS VKFDLQIQSS NLFDKVSPVV SHKVDLAVLA AVEIRGVSSP DHVFLPIPNW EHKENPETEE DVGPVVQHIY ELRNNGPSSF SKAMLHLQWP YKYNNNTLLY ILHYDIDGPM NCTSDMEINP LRIKISSLQT TEKNDTVAGQ GERDHLITKR DLALSEGDIH TLGCGVAQCL KIVCQVGRLD RGKSAILYVK SLLWTETFMN KENQNHSYSL KSSASFNVIE FPYKNLPIED ITNSTLVTTN VTWGIQPAPM PVPVWVIILA VLAGLLLLAV LVFVMYRMGF FKRVRPPQEE QEREQLQPHE NGEGNSET //