ITAV_HUMAN
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 03-AUG-2022, entry version 249.
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},
GN VNRA {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 (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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50] {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 {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 is found
CC in a ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415).
CC ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3
CC (PubMed:20682778). ITGAV:ITGB3 is found in a ternary complex with FGF1
CC and FGFR1 (PubMed:18441324). ITGAV:ITGB3 is found in a ternary complex
CC with IGF1 and IGF1R (PubMed:19578119). ITGAV:ITGB3 interacts with IGF2
CC (PubMed:28873464). ITGAV:ITGB3 and ITGAV:ITGB6 interact with FBN1
CC (PubMed:12807887, PubMed:17158881). ITGAV:ITGB3 interacts with CD9,
CC CD81 and CD151 (via second extracellular domain) (PubMed:27993971).
CC ITGAV:ITGB6 interacts with TGFB1 (PubMed:22278742, PubMed:28117447).
CC ITGAV:ITGB3 interacts with PTN (PubMed:19141530). Forms a complex with
CC PTPRZ1 and PTN that stimulates endothelial cell migration through ITGB3
CC 'Tyr-773' phosphorylation (PubMed:19141530).
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}.
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:9426447, PubMed:15194773, PubMed:7519807).
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 -!- 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};
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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 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 AlphaFoldDB; P06756; -.
DR SMR; P06756; -.
DR BioGRID; 109891; 199.
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; 52.
DR MINT; P06756; -.
DR STRING; 9606.ENSP00000261023; -.
DR BindingDB; P06756; -.
DR ChEMBL; CHEMBL3660; -.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR DrugBank; DB00451; Levothyroxine.
DR GuidetoPHARMACOLOGY; 2453; -.
DR TCDB; 8.A.54.1.4; the integrin (integrin) family.
DR GlyConnect; 1412; 28 N-Linked glycans (4 sites).
DR GlyGen; P06756; 13 sites, 29 N-linked glycans (4 sites).
DR iPTMnet; P06756; -.
DR PhosphoSitePlus; P06756; -.
DR BioMuta; ITGAV; -.
DR DMDM; 143811408; -.
DR EPD; P06756; -.
DR jPOST; P06756; -.
DR MassIVE; P06756; -.
DR MaxQB; P06756; -.
DR PaxDb; P06756; -.
DR PeptideAtlas; P06756; -.
DR PRIDE; P06756; -.
DR ProteomicsDB; 18948; -.
DR ProteomicsDB; 51933; -. [P06756-1]
DR ProteomicsDB; 51934; -. [P06756-2]
DR ABCD; P06756; 70 sequenced antibodies.
DR Antibodypedia; 1498; 1471 antibodies from 47 providers.
DR DNASU; 3685; -.
DR Ensembl; ENST00000261023.8; ENSP00000261023.3; ENSG00000138448.12. [P06756-1]
DR Ensembl; ENST00000374907.7; ENSP00000364042.3; ENSG00000138448.12. [P06756-2]
DR Ensembl; ENST00000433736.6; ENSP00000404291.2; ENSG00000138448.12. [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 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; VGQVTIC; -.
DR OrthoDB; 743479at2759; -.
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; 317 hits in 1103 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 211 other tissues.
DR ExpressionAtlas; P06756; baseline and differential.
DR Genevisible; P06756; HS.
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:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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:1901388; P:regulation of transforming growth factor beta activation; IDA:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0071604; P:transforming growth factor beta production; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IMP:UniProtKB.
DR DisProt; DP02742; -.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 3.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
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; Receptor; Reference proteome; Repeat; Signal;
KW 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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447,
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:28117447"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28117447"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28117447"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28117447"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28117447"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:28117447"
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:0000255"
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:0000255"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..97
FT /evidence="ECO:0000269|PubMed:14596610,
FT ECO:0000269|PubMed:28117447"
FT DISULFID 138..158
FT /evidence="ECO:0000269|PubMed:14596610,
FT ECO:0000269|PubMed:28117447"
FT DISULFID 172..185
FT /evidence="ECO:0000269|PubMed:14596610,
FT ECO:0000269|PubMed:28117447"
FT DISULFID 491..502
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 508..565
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 626..632
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 698..711
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 852..914
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000269|PubMed:14596610"
FT DISULFID 904..909
FT /evidence="ECO:0000269|PubMed:14596610"
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 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
