GenomeNet

Database: UniProt
Entry: P06756
LinkDB: P06756
Original site: P06756 
ID   ITAV_HUMAN              Reviewed;        1048 AA.
AC   P06756; A0AV67; B0LPF4; B7Z883; B7ZLX0; D3DPG8; E7EWZ6; Q53SK4;
AC   Q59EB7; Q6LD15;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAY-2019, entry version 230.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-783.
RX   PubMed=2443500;
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;
RA   Sims M.A., Field S., Barnes M.R., Shaikh N., Ellington K.,
RA   Murphy K.E., Spurr N.K., Campbell D.A.;
RT   "Cloning and characterisation of ITGAV, the genomic sequence for human
RT   cell 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
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP   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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   with 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
RT   for 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.,
RA   Heino J., Hyypiae T.;
RT   "Entry of coxsackievirus A9 into host cells: specific interactions
RT   with alpha v beta 3 integrin, the vitronectin receptor.";
RL   Virology 203:357-365(1994).
RN   [13]
RP   INTERACTION WITH COXSACKIEVIRUS B1 CAPSID PROTEINS.
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.
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
RT   vascular cell growth and locomotion by engaging the alpha5beta1 and
RT   alphavbeta3 integrins and by mobilizing sequestered basic fibroblast
RT   growth factor.";
RL   Blood 94:663-672(1999).
RN   [15]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
RP   PARECHOVIRUS 1 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.,
RA   Lau L.F.;
RT   "CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
RT   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
RT   by 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.,
RA   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
RT   the latent TGF-beta binding protein-1.";
RL   J. Cell Biol. 165:723-734(2004).
RN   [21]
RP   INTERACTION WITH COXSACKIEVIRUS A9 CAPSID PROTEINS.
RX   PubMed=15194773; DOI=10.1128/JVI.78.13.6967-6973.2004;
RA   Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D.,
RA   Stanway G.;
RT   "Integrin alpha v beta 6 is an RGD-dependent receptor for
RT   coxsackievirus 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling 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
RT   integrin 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.,
RA   Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I.,
RA   McCaffrey M.W., Ozanne B.W., Norman J.C.;
RT   "Rab25 associates with alpha5beta1 integrin to promote invasive
RT   migration 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
RT   studies 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
RP   AND 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.,
RA   Liu F.T., Takada Y.K., Takada Y.;
RT   "Pro-inflammatory secretory phospholipase A2 type IIA binds to
RT   integrins alphavbeta3 and alpha4beta1 and induces proliferation of
RT   monocytic cells in an integrin-dependent manner.";
RL   J. Biol. Chem. 283:26107-26115(2008).
RN   [28]
RP   INTERACTION WITH HHV-8 GLYCOPROTEIN B.
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
RT   Kaposi's sarcoma-associated herpesvirus and functions as an RGD-
RT   dependent entry 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
RT   protein 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
RP   AND 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
RT   integrin 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
RT   multiple 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-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [34]
RP   FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1
RP   AND 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-
RT   negative 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.,
RA   Buerckstuemmer T., 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
RP   CX3CR1 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
RT   fractalkine, and the integrin-binding defective mutant of fractalkine
RT   is an antagonist 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.,
RA   Tripathy A., Dokholyan N.V., Leisner T.M., Parise L.V.;
RT   "Identification of novel integrin binding partners for calcium and
RT   integrin binding protein 1 (CIB1): structural and thermodynamic basis
RT   of CIB1 promiscuity.";
RL   Biochemistry 52:7082-7090(2013).
RN   [39]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLEX
RP   VIRUS 1 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
RT   receptors for HSV gH/gL to promote endocytosis and activation of
RT   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   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.,
RA   Takada Y.K., Takada Y.;
RT   "Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
RT   integrin activation through direct binding to a newly identified
RT   binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
RT   alpha5beta1.";
RL   J. Biol. Chem. 290:259-271(2015).
RN   [43]
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.,
RA   Takada Y.;
RT   "The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-
RT   binding site of integrin alphavbeta3.";
RL   Biochem. J. 474:589-596(2017).
RN   [44]
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.,
RA   Lam K.S., 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   [45]
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
RT   interleukin-1beta (IL-1beta) are involved in the agonistic action of
RT   IL-1beta.";
RL   J. Biol. Chem. 292:20067-20075(2017).
RN   [46]
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.,
RA   Takada Y.;
RT   "Direct integrin binding to insulin-like growth factor-2 through the
RT   C-domain is required for insulin-like growth factor receptor type 1
RT   (IGF1R) signaling.";
RL   PLoS ONE 12:E0184285-E0184285(2017).
RN   [47]
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
RT   Vbeta3.";
RL   Science 294:339-345(2001).
RN   [48] {ECO:0000244|PDB:5FFG, ECO:0000244|PDB:5FFO}
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 31-627 IN COMPLEX WITH TGFB1
RP   AND ITGB6, CALCIUM-BINDING, FUNCTION, SUBUNIT, DISULFIDE BONDS, AND
RP   GLYCOSYLATION AT ASN-74; ASN-290; ASN-296; ASN-488; ASN-554 AND
RP   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-
RT   beta.";
RL   Nature 542:55-59(2017).
CC   -!- FUNCTION: The alpha-V (ITGAV) integrins are receptors for
CC       vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix
CC       metalloproteinase-2, osteopontin, osteomodulin, prothrombin,
CC       thrombospondin and vWF. They recognize the sequence R-G-D in a
CC       wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1)
CC       and may act as its coreceptor in CX3CR1-dependent fractalkine
CC       signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF
CC       domain) and this binding is essential for NRG1-ERBB signaling
CC       (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is
CC       essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds
CC       to 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
CC       to 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
CC       to PLA2G2A via a site (site 2) which is distinct from the
CC       classical ligand-binding site (site 1) and this induces integrin
CC       conformational changes and enhanced ligand binding to site 1
CC       (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6
CC       act as a receptor for fibrillin-1 (FBN1) and mediate R-G-D-
CC       dependent cell adhesion to FBN1 (PubMed:12807887,
CC       PubMed:17158881). Integrin alpha-V/beta-6 or alpha-V/beta-8
CC       (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of
CC       transforming growth factor beta-1 (TGF-beta-1) from regulatory
CC       Latency-associated peptide (LAP), thereby playing a key role in
CC       TGF-beta-1 activation (PubMed:15184403, PubMed:22278742,
CC       PubMed:28117447). {ECO:0000269|PubMed:12807887,
CC       ECO:0000269|PubMed:15184403, ECO:0000269|PubMed:17158881,
CC       ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:18635536,
CC       ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778,
CC       ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:23125415,
CC       ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:28117447,
CC       ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:28873464,
CC       ECO:0000269|PubMed:29030430}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a
CC       receptor for Adenovirus type C. {ECO:0000269|PubMed:20615244}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 and
CC       ITGAV:ITGB3 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
CC       receptor for Herpes virus 8/HHV-8. {ECO:0000269|PubMed:18045938}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB6 acts as a
CC       receptor for herpes simplex 1/HHV-1.
CC       {ECO:0000269|PubMed:24367260}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a
CC       receptor for Human parechovirus 1. {ECO:0000269|PubMed:11160695}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a
CC       receptor 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
CC       subunit is composed of a heavy and a light chain linked by a
CC       disulfide bond. Alpha-V (ITGAV) associates with either beta-1
CC       (ITGB1), beta-3 (ITGB3), beta-5 (ITGB5), beta-6 (ITGB6) or beta-8
CC       (ITGB8). Interacts with CIB1 (PubMed:24011356). Interacts with
CC       RAB25 (PubMed:17925226). Integrins ITGAV:ITGB3 and ITGAV:ITGB5
CC       interact with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB3
CC       and ITGAV:ITGB5 interact with CCN3 (PubMed:12695522). ITGAV:ITGB3
CC       interacts with ADGRA2 (PubMed:16982628). ITGAV:ITGB3 interacts
CC       with FGF2; it is likely that FGF2 can simultaneously bind
CC       ITGAV:ITGB3 and FGF receptors (PubMed:28302677). ITGAV:ITGB3
CC       interacts with IL1B (PubMed:29030430). ITGAV:ITGB3 is found in a
CC       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
CC       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
CC       domain) (PubMed:27993971). ITGAV:ITGB6 interacts with TGFB1
CC       (PubMed:22278742, PubMed:28117447). ITGAV:ITGB3 interacts with PTN
CC       (PubMed:19141530). Forms a complex with PTPRZ1 and PTN that
CC       stimulates endothelial cell migration through ITGB3 'Tyr-773'
CC       phosphorylation (PubMed:19141530). {ECO:0000250|UniProtKB:P43406,
CC       ECO:0000250|UniProtKB:P80746, ECO:0000269|PubMed:12695522,
CC       ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16982628,
CC       ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17925226,
CC       ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:19141530,
CC       ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20615244,
CC       ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22278742,
CC       ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:23658209,
CC       ECO:0000269|PubMed:24011356, ECO:0000269|PubMed:27993971,
CC       ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:28302677,
CC       ECO:0000269|PubMed:28873464, 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
CC       ITGAV:ITGB6 bind to coxsackievirus A9 and coxsackievirus B1 capsid
CC       proteins (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: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.
CC       {ECO:0000269|PubMed:11160695}.
CC   -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
CC       West 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       P05106:ITGB3; NbExp=13; IntAct=EBI-298282, EBI-702847;
CC       P18084:ITGB5; NbExp=2; IntAct=EBI-298282, EBI-1223434;
CC       P18564:ITGB6; NbExp=7; IntAct=EBI-298282, EBI-2568070;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell junction, focal adhesion
CC       {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         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P06756-3; Sequence=VSP_044914;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD93131.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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.
DR   RefSeq; NP_001138472.1; NM_001145000.2.
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   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   SMR; P06756; -.
DR   BioGrid; 109891; 75.
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; 21.
DR   MINT; P06756; -.
DR   STRING; 9606.ENSP00000261023; -.
DR   BindingDB; P06756; -.
DR   ChEMBL; CHEMBL3660; -.
DR   DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
DR   GuidetoPHARMACOLOGY; 2453; -.
DR   TCDB; 8.A.54.1.4; the integrin (integrin) family.
DR   GlyConnect; 1412; -.
DR   iPTMnet; P06756; -.
DR   PhosphoSitePlus; P06756; -.
DR   BioMuta; ITGAV; -.
DR   DMDM; 143811408; -.
DR   EPD; P06756; -.
DR   jPOST; P06756; -.
DR   MaxQB; P06756; -.
DR   PaxDb; P06756; -.
DR   PeptideAtlas; P06756; -.
DR   PRIDE; P06756; -.
DR   ProteomicsDB; 51933; -.
DR   ProteomicsDB; 51934; -. [P06756-2]
DR   Ensembl; ENST00000261023; ENSP00000261023; ENSG00000138448. [P06756-1]
DR   Ensembl; ENST00000374907; ENSP00000364042; ENSG00000138448. [P06756-2]
DR   Ensembl; ENST00000433736; ENSP00000404291; ENSG00000138448. [P06756-3]
DR   GeneID; 3685; -.
DR   KEGG; hsa:3685; -.
DR   UCSC; uc002upq.5; human. [P06756-1]
DR   CTD; 3685; -.
DR   DisGeNET; 3685; -.
DR   GeneCards; ITGAV; -.
DR   HGNC; HGNC:6150; ITGAV.
DR   HPA; CAB002499; -.
DR   HPA; HPA004856; -.
DR   MIM; 193210; gene.
DR   neXtProt; NX_P06756; -.
DR   OpenTargets; ENSG00000138448; -.
DR   PharmGKB; PA37336; -.
DR   eggNOG; ENOG410IPB5; Eukaryota.
DR   eggNOG; ENOG410YR19; LUCA.
DR   GeneTree; ENSGT00940000158361; -.
DR   HOGENOM; HOG000231603; -.
DR   InParanoid; P06756; -.
DR   KO; K06487; -.
DR   OMA; APLYQWS; -.
DR   OrthoDB; 135910at2759; -.
DR   PhylomeDB; P06756; -.
DR   TreeFam; TF105391; -.
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-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   ChiTaRS; ITGAV; human.
DR   EvolutionaryTrace; P06756; -.
DR   GeneWiki; ITGAV; -.
DR   GenomeRNAi; 3685; -.
DR   PRO; PR:P06756; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000138448; Expressed in 247 organ(s), highest expression level in pigmented layer of retina.
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; IEA:Ensembl.
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:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
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: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:0052066; P:entry of symbiont into host cell by promotion of host phagocytosis; NAS:BHF-UCL.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
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; NAS:UniProtKB.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
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:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
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:0038044; P:transforming growth factor-beta secretion; IEA:Ensembl.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   GO; GO:0046718; P:viral entry into host cell; IMP:UniProtKB.
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   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;
KW   Cell junction; Cell membrane; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Integrin; Membrane; Metal-binding;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       {ECO:0000269|PubMed:2467745}.
FT   CHAIN        31   1048       Integrin alpha-V.
FT                                /FTId=PRO_0000016301.
FT   CHAIN        31    889       Integrin alpha-V heavy chain.
FT                                /FTId=PRO_0000016302.
FT   CHAIN       891   1048       Integrin alpha-V light chain.
FT                                /FTId=PRO_0000016303.
FT   TOPO_DOM     31    992       Extracellular. {ECO:0000255}.
FT   TRANSMEM    993   1016       Helical. {ECO:0000255}.
FT   TOPO_DOM   1017   1048       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       32     98       FG-GAP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00803}.
FT   REPEAT      109    170       FG-GAP 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00803}.
FT   REPEAT      173    225       FG-GAP 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00803}.
FT   REPEAT      237    291       FG-GAP 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00803}.
FT   REPEAT      292    357       FG-GAP 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00803}.
FT   REPEAT      358    415       FG-GAP 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00803}.
FT   REPEAT      419    482       FG-GAP 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00803}.
FT   CA_BIND     260    268       {ECO:0000255,
FT                                ECO:0000269|PubMed:28117447}.
FT   CA_BIND     314    322       {ECO:0000255,
FT                                ECO:0000269|PubMed:28117447}.
FT   CA_BIND     379    387       {ECO:0000255,
FT                                ECO:0000269|PubMed:28117447}.
FT   CA_BIND     443    451       {ECO:0000255,
FT                                ECO:0000269|PubMed:28117447}.
FT   MOTIF      1019   1023       GFFKR motif.
FT   CARBOHYD     74     74       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:28117447}.
FT   CARBOHYD    290    290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:28117447}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:28117447}.
FT   CARBOHYD    488    488       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:28117447}.
FT   CARBOHYD    554    554       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:28117447}.
FT   CARBOHYD    615    615       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754519,
FT                                ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:28117447}.
FT   CARBOHYD    704    704       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    835    835       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    851    851       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    874    874       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:19349973}.
FT   CARBOHYD    945    945       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    973    973       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    980    980       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     89     97       {ECO:0000269|PubMed:14596610,
FT                                ECO:0000269|PubMed:28117447}.
FT   DISULFID    138    158       {ECO:0000269|PubMed:14596610,
FT                                ECO:0000269|PubMed:28117447}.
FT   DISULFID    172    185       {ECO:0000269|PubMed:14596610,
FT                                ECO:0000269|PubMed:28117447}.
FT   DISULFID    491    502       {ECO:0000269|PubMed:14596610}.
FT   DISULFID    508    565       {ECO:0000269|PubMed:14596610}.
FT   DISULFID    626    632       {ECO:0000269|PubMed:14596610}.
FT   DISULFID    698    711       {ECO:0000269|PubMed:14596610}.
FT   DISULFID    852    914       Interchain (between heavy and light
FT                                chains). {ECO:0000269|PubMed:14596610}.
FT   DISULFID    904    909       {ECO:0000269|PubMed:14596610}.
FT   VAR_SEQ       1     62       MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEY
FT                                SGPEGSYFGFAVDFFVPSASS -> MLLGTLLLILYILMLC
FT                                (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_044914.
FT   VAR_SEQ     175    211       QDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQG ->
FT                                R (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_024351.
FT   VARIANT     405    405       I -> V (in dbSNP:rs3738918).
FT                                /FTId=VAR_024289.
FT   VARIANT     548    548       S -> A (in dbSNP:rs2230615).
FT                                /FTId=VAR_055970.
FT   VARIANT     783    783       V -> I (in dbSNP:rs2230616).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:2430295,
FT                                ECO:0000269|PubMed:2443500,
FT                                ECO:0000269|Ref.4, ECO:0000269|Ref.6,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_031547.
FT   CONFLICT    425    425       W -> R (in Ref. 2; AAG03000).
FT                                {ECO:0000305}.
FT   CONFLICT    700    700       F -> L (in Ref. 8; AAI44101).
FT                                {ECO:0000305}.
FT   CONFLICT   1039   1039       H -> R (in Ref. 2; AAG03000).
FT                                {ECO:0000305}.
FT   STRAND       39     42       {ECO:0000244|PDB:5FFG}.
FT   TURN         45     50       {ECO:0000244|PDB:5FFG}.
FT   STRAND       51     56       {ECO:0000244|PDB:5FFG}.
FT   STRAND       60     62       {ECO:0000244|PDB:4UM9}.
FT   STRAND       65     70       {ECO:0000244|PDB:5FFG}.
FT   STRAND       85     95       {ECO:0000244|PDB:5FFG}.
FT   STRAND       97    100       {ECO:0000244|PDB:5FFG}.
FT   STRAND      109    111       {ECO:0000244|PDB:5FFG}.
FT   STRAND      114    118       {ECO:0000244|PDB:5FFG}.
FT   STRAND      126    131       {ECO:0000244|PDB:5FFG}.
FT   STRAND      134    139       {ECO:0000244|PDB:5FFG}.
FT   STRAND      147    150       {ECO:0000244|PDB:5FFG}.
FT   STRAND      157    162       {ECO:0000244|PDB:5FFG}.
FT   STRAND      165    169       {ECO:0000244|PDB:5FFG}.
FT   STRAND      174    176       {ECO:0000244|PDB:5FFG}.
FT   TURN        178    184       {ECO:0000244|PDB:5FFG}.
FT   STRAND      189    193       {ECO:0000244|PDB:5FFG}.
FT   STRAND      197    203       {ECO:0000244|PDB:5FFG}.
FT   HELIX       206    209       {ECO:0000244|PDB:5FFG}.
FT   STRAND      211    217       {ECO:0000244|PDB:5FFG}.
FT   HELIX       218    223       {ECO:0000244|PDB:5FFG}.
FT   STRAND      235    239       {ECO:0000244|PDB:4G1E}.
FT   HELIX       245    247       {ECO:0000244|PDB:5FFG}.
FT   STRAND      254    259       {ECO:0000244|PDB:5FFG}.
FT   STRAND      261    266       {ECO:0000244|PDB:5FFG}.
FT   STRAND      268    273       {ECO:0000244|PDB:5FFG}.
FT   HELIX       276    279       {ECO:0000244|PDB:5FFG}.
FT   STRAND      282    286       {ECO:0000244|PDB:5FFG}.
FT   TURN        288    290       {ECO:0000244|PDB:5FFG}.
FT   STRAND      293    298       {ECO:0000244|PDB:5FFG}.
FT   STRAND      308    313       {ECO:0000244|PDB:5FFG}.
FT   STRAND      316    319       {ECO:0000244|PDB:5FFG}.
FT   STRAND      322    327       {ECO:0000244|PDB:5FFG}.
FT   STRAND      331    333       {ECO:0000244|PDB:5FFG}.
FT   STRAND      335    337       {ECO:0000244|PDB:4G1M}.
FT   STRAND      339    341       {ECO:0000244|PDB:5FFG}.
FT   STRAND      344    350       {ECO:0000244|PDB:5FFG}.
FT   STRAND      352    354       {ECO:0000244|PDB:3IJE}.
FT   STRAND      356    362       {ECO:0000244|PDB:5FFG}.
FT   STRAND      364    368       {ECO:0000244|PDB:1JV2}.
FT   HELIX       370    372       {ECO:0000244|PDB:1U8C}.
FT   STRAND      374    378       {ECO:0000244|PDB:5FFG}.
FT   STRAND      383    385       {ECO:0000244|PDB:5FFG}.
FT   STRAND      387    392       {ECO:0000244|PDB:5FFG}.
FT   HELIX       397    399       {ECO:0000244|PDB:5FFG}.
FT   STRAND      402    409       {ECO:0000244|PDB:5FFG}.
FT   STRAND      410    413       {ECO:0000244|PDB:4UM8}.
FT   STRAND      418    422       {ECO:0000244|PDB:5FFG}.
FT   STRAND      428    430       {ECO:0000244|PDB:4UM9}.
FT   STRAND      436    442       {ECO:0000244|PDB:5FFG}.
FT   STRAND      447    449       {ECO:0000244|PDB:5FFG}.
FT   STRAND      451    456       {ECO:0000244|PDB:5FFG}.
FT   HELIX       457    459       {ECO:0000244|PDB:5FFG}.
FT   STRAND      461    465       {ECO:0000244|PDB:5FFG}.
FT   STRAND      470    485       {ECO:0000244|PDB:5FFG}.
FT   STRAND      494    499       {ECO:0000244|PDB:3IJE}.
FT   STRAND      502    512       {ECO:0000244|PDB:5FFG}.
FT   STRAND      514    516       {ECO:0000244|PDB:5FFG}.
FT   STRAND      519    528       {ECO:0000244|PDB:5FFG}.
FT   TURN        529    532       {ECO:0000244|PDB:5FFG}.
FT   STRAND      535    537       {ECO:0000244|PDB:4G1M}.
FT   STRAND      541    543       {ECO:0000244|PDB:5FFG}.
FT   TURN        544    546       {ECO:0000244|PDB:5FFG}.
FT   STRAND      547    558       {ECO:0000244|PDB:5FFG}.
FT   STRAND      559    561       {ECO:0000244|PDB:4MMY}.
FT   STRAND      564    572       {ECO:0000244|PDB:5FFG}.
FT   HELIX       575    577       {ECO:0000244|PDB:5FFG}.
FT   STRAND      585    593       {ECO:0000244|PDB:5FFG}.
FT   TURN        595    597       {ECO:0000244|PDB:4UM9}.
FT   STRAND      601    603       {ECO:0000244|PDB:4G1E}.
FT   STRAND      610    612       {ECO:0000244|PDB:5FFG}.
FT   STRAND      614    623       {ECO:0000244|PDB:5FFG}.
FT   TURN        627    630       {ECO:0000244|PDB:3IJE}.
FT   STRAND      636    641       {ECO:0000244|PDB:3IJE}.
FT   STRAND      646    648       {ECO:0000244|PDB:3IJE}.
FT   STRAND      653    663       {ECO:0000244|PDB:3IJE}.
FT   STRAND      668    670       {ECO:0000244|PDB:3IJE}.
FT   STRAND      672    676       {ECO:0000244|PDB:3IJE}.
FT   STRAND      681    686       {ECO:0000244|PDB:3IJE}.
FT   STRAND      691    693       {ECO:0000244|PDB:4G1E}.
FT   STRAND      697    701       {ECO:0000244|PDB:3IJE}.
FT   STRAND      703    705       {ECO:0000244|PDB:3IJE}.
FT   STRAND      708    712       {ECO:0000244|PDB:3IJE}.
FT   STRAND      715    717       {ECO:0000244|PDB:3IJE}.
FT   STRAND      722    731       {ECO:0000244|PDB:3IJE}.
FT   STRAND      735    737       {ECO:0000244|PDB:4G1E}.
FT   STRAND      739    748       {ECO:0000244|PDB:3IJE}.
FT   STRAND      752    754       {ECO:0000244|PDB:3IJE}.
FT   STRAND      760    767       {ECO:0000244|PDB:3IJE}.
FT   STRAND      772    786       {ECO:0000244|PDB:3IJE}.
FT   TURN        798    802       {ECO:0000244|PDB:3IJE}.
FT   STRAND      805    814       {ECO:0000244|PDB:3IJE}.
FT   STRAND      816    818       {ECO:0000244|PDB:3IJE}.
FT   STRAND      820    833       {ECO:0000244|PDB:3IJE}.
FT   STRAND      839    856       {ECO:0000244|PDB:3IJE}.
FT   STRAND      900    902       {ECO:0000244|PDB:3IJE}.
FT   TURN        904    906       {ECO:0000244|PDB:3IJE}.
FT   STRAND      907    916       {ECO:0000244|PDB:3IJE}.
FT   STRAND      923    933       {ECO:0000244|PDB:3IJE}.
FT   HELIX       935    938       {ECO:0000244|PDB:3IJE}.
FT   STRAND      941    944       {ECO:0000244|PDB:3IJE}.
FT   STRAND      948    960       {ECO:0000244|PDB:3IJE}.
FT   STRAND      964    966       {ECO:0000244|PDB:4G1E}.
FT   STRAND      971    982       {ECO:0000244|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
//
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