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Integrin alpha-V (Vitronectin receptor) (Vitronectin receptor subunit alpha) (CD antigen CD51) [Cleaved into: Integrin alpha-V heavy chain; Integrin alpha-V light chain]

 ITAV_HUMAN              Reviewed;        1048 AA.
P06756; A0AV67; B0LPF4; B7Z883; B7ZLX0; D3DPG8; E7EWZ6; Q53SK4;
Q59EB7; Q6LD15;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
27-SEP-2017, entry version 213.
RecName: Full=Integrin alpha-V;
AltName: Full=Vitronectin receptor {ECO:0000312|HGNC:HGNC:6150};
AltName: Full=Vitronectin receptor subunit alpha;
AltName: CD_antigen=CD51;
Contains:
RecName: Full=Integrin alpha-V heavy chain;
Contains:
RecName: Full=Integrin alpha-V light chain;
Flags: Precursor;
Name=ITGAV {ECO:0000312|HGNC:HGNC:6150};
Synonyms=MSK8 {ECO:0000312|HGNC:HGNC:6150},
VNRA {ECO:0000312|HGNC:HGNC:6150}, VTNR {ECO:0000312|HGNC:HGNC:6150};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-783.
PubMed=2443500;
Suzuki S., Argraves W.S., Arai H., Languino L.R., Pierschbacher M.D.,
Ruoslahti E.;
"Amino acid sequence of the vitronectin receptor alpha subunit and
comparative expression of adhesion receptor mRNAs.";
J. Biol. Chem. 262:14080-14085(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10965141;
Sims M.A., Field S., Barnes M.R., Shaikh N., Ellington K.,
Murphy K.E., Spurr N.K., Campbell D.A.;
"Cloning and characterisation of ITGAV, the genomic sequence for human
cell adhesion protein (vitronectin) receptor alpha subunit, CD51.";
Cytogenet. Cell Genet. 89:268-271(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ILE-783.
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ILE-783.
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-783.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-783.
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ILE-783.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
PubMed=7522056; DOI=10.1016/0167-4781(94)90278-X;
Donahue J.P., Sugg N., Hawiger J.;
"The integrin alpha v gene: identification and characterization of the
promoter region.";
Biochim. Biophys. Acta 1219:228-232(1994).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 413-1048, AND VARIANT ILE-783.
PubMed=2430295; DOI=10.1073/pnas.83.22.8614;
Suzuki S., Argraves W.S., Pytela R., Arai H., Krusius T.,
Pierschbacher M.D., Ruoslahti E.;
"cDNA and amino acid sequences of the cell adhesion protein receptor
recognizing vitronectin reveal a transmembrane domain and homologies
with other adhesion protein receptors.";
Proc. Natl. Acad. Sci. U.S.A. 83:8614-8618(1986).
[11]
PROTEIN SEQUENCE OF 31-41.
PubMed=2467745; DOI=10.1016/0092-8674(89)90172-4;
Cheresh D.A., Smith J.W., Cooper H.M., Quaranta V.;
"A novel vitronectin receptor integrin (alpha v beta x) is responsible
for distinct adhesive properties of carcinoma cells.";
Cell 57:59-69(1989).
[12]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A9
CAPSID PROTEINS.
PubMed=7519807; DOI=10.1006/viro.1994.1494;
Roivainen M., Piirainen L., Hovi T., Virtanen I., Riikonen T.,
Heino J., Hyypiae T.;
"Entry of coxsackievirus A9 into host cells: specific interactions
with alpha v beta 3 integrin, the vitronectin receptor.";
Virology 203:357-365(1994).
[13]
INTERACTION WITH COXSACKIEVIRUS B1 CAPSID PROTEINS.
PubMed=9426447; DOI=10.1006/viro.1997.8831;
Agrez M.V., Shafren D.R., Gu X., Cox K., Sheppard D., Barry R.D.;
"Integrin alpha v beta 6 enhances coxsackievirus B1 lytic infection of
human colon cancer cells.";
Virology 239:71-77(1997).
[14]
INTERACTION WITH HIV-1 TAT.
PubMed=10397733;
Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S.,
Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.;
"The Tat protein of human immunodeficiency virus type-1 promotes
vascular cell growth and locomotion by engaging the alpha5beta1 and
alphavbeta3 integrins and by mobilizing sequestered basic fibroblast
growth factor.";
Blood 94:663-672(1999).
[15]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
PARECHOVIRUS 1 CAPSID PROTEINS.
PubMed=11160695; DOI=10.1128/JVI.75.4.1958-1967.2001;
Joki-Korpela P., Marjomaki V., Krogerus C., Heino J., Hyypia T.;
"Entry of human parechovirus 1.";
J. Virol. 75:1958-1967(2001).
[16]
INTERACTION WITH NOV.
PubMed=12695522; DOI=10.1074/jbc.M302028200;
Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y.,
Lau L.F.;
"CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
family.";
J. Biol. Chem. 278:24200-24208(2003).
[17]
FUNCTION, AND INTERACTION WITH FBN1.
PubMed=12807887; DOI=10.1074/jbc.M303159200;
Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
Shuttleworth C.A., Humphries M.J., Kielty C.M.;
"Cell adhesion to fibrillin-1 molecules and microfibrils is mediated
by alpha 5 beta 1 and alpha v beta 3 integrins.";
J. Biol. Chem. 278:34605-34616(2003).
[18]
GLYCOSYLATION AT ASN-615.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[19]
DISULFIDE BONDS.
PubMed=14596610; DOI=10.1021/bi034726u;
Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G.,
Wilkins J.A.;
"Mass spectrometric based mapping of the disulfide bonding patterns of
integrin alpha chains.";
Biochemistry 42:12950-12959(2003).
[20]
INTERACTION WITH COXSACKIEVIRUS A9 CAPSID PROTEINS.
PubMed=15194773; DOI=10.1128/JVI.78.13.6967-6973.2004;
Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D.,
Stanway G.;
"Integrin alpha v beta 6 is an RGD-dependent receptor for
coxsackievirus A9.";
J. Virol. 78:6967-6973(2004).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[22]
INTERACTION WITH ADGRA2.
PubMed=16982628; DOI=10.1074/jbc.M605291200;
Vallon M., Essler M.;
"Proteolytically processed soluble tumor endothelial marker (TEM) 5
mediates endothelial cell survival during angiogenesis by linking
integrin alpha(v)beta3 to glycosaminoglycans.";
J. Biol. Chem. 281:34179-34188(2006).
[23]
INTERACTION WITH RAB25.
PubMed=17925226; DOI=10.1016/j.devcel.2007.08.012;
Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K.,
Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I.,
McCaffrey M.W., Ozanne B.W., Norman J.C.;
"Rab25 associates with alpha5beta1 integrin to promote invasive
migration in 3D microenvironments.";
Dev. Cell 13:496-510(2007).
[24]
FUNCTION, INTERACTION WITH FBN1, AND SUBCELLULAR LOCATION.
PubMed=17158881; DOI=10.1074/jbc.M607008200;
Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I.,
van der Merwe P.A., Mardon H.J., Handford P.A.;
"alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative
studies of molecular determinants underlying integrin-rgd affinity and
specificity.";
J. Biol. Chem. 282:6743-6751(2007).
[25]
FUNCTION, BINDING TO FGF1, AND IDENTIFICATION IN A COMPLEX WITH FGF1
AND FGFR1.
PubMed=18441324; DOI=10.1074/jbc.M801213200;
Mori S., Wu C.Y., Yamaji S., Saegusa J., Shi B., Ma Z., Kuwabara Y.,
Lam K.S., Isseroff R.R., Takada Y.K., Takada Y.;
"Direct binding of integrin alphavbeta3 to FGF1 plays a role in FGF1
signaling.";
J. Biol. Chem. 283:18066-18075(2008).
[26]
FUNCTION.
PubMed=18635536; DOI=10.1074/jbc.M804835200;
Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S.,
Liu F.T., Takada Y.K., Takada Y.;
"Pro-inflammatory secretory phospholipase A2 type IIA binds to
integrins alphavbeta3 and alpha4beta1 and induces proliferation of
monocytic cells in an integrin-dependent manner.";
J. Biol. Chem. 283:26107-26115(2008).
[27]
INTERACTION WITH HHV-8 GLYCOPROTEIN B.
PubMed=18045938; DOI=10.1128/JVI.01673-07;
Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.;
"Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of
Kaposi's sarcoma-associated herpesvirus and functions as an RGD-
dependent entry receptor.";
J. Virol. 82:1570-1580(2008).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
FUNCTION, BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH IGF1
AND IGF1R.
PubMed=19578119; DOI=10.1074/jbc.M109.013201;
Saegusa J., Yamaji S., Ieguchi K., Wu C.Y., Lam K.S., Liu F.T.,
Takada Y.K., Takada Y.;
"The direct binding of insulin-like growth factor-1 (IGF-1) to
integrin alphavbeta3 is involved in IGF-1 signaling.";
J. Biol. Chem. 284:24106-24114(2009).
[30]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615; ASN-704 AND
ASN-874.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-874.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[32]
FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1
AND ERBB3.
PubMed=20682778; DOI=10.1074/jbc.M110.113878;
Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
Wang B., Takada Y.K., Takada Y.;
"Direct binding of the EGF-like domain of neuregulin-1 to integrins
({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
signaling.";
J. Biol. Chem. 285:31388-31398(2010).
[33]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS TYPE C
PENTON PROTEIN.
PubMed=20615244; DOI=10.1186/1743-422X-7-148;
Lyle C., McCormick F.;
"Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-
negative cells.";
Virol. J. 7:148-148(2010).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[35]
FUNCTION, BINDING TO CX3CL1, AND IDENTIFICATION IN A COMPLEX WITH
CX3CR1 AND CX3CL1.
PubMed=23125415; DOI=10.4049/jimmunol.1200889;
Fujita M., Takada Y.K., Takada Y.;
"Integrins alphavbeta3 and alpha4beta1 act as coreceptors for
fractalkine, and the integrin-binding defective mutant of fractalkine
is an antagonist of CX3CR1.";
J. Immunol. 189:5809-5819(2012).
[36]
INTERACTION WITH CIB1.
PubMed=24011356; DOI=10.1021/bi400678y;
Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I.,
Tripathy A., Dokholyan N.V., Leisner T.M., Parise L.V.;
"Identification of novel integrin binding partners for calcium and
integrin binding protein 1 (CIB1): structural and thermodynamic basis
of CIB1 promiscuity.";
Biochemistry 52:7082-7090(2013).
[37]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLEX
VIRUS 1 ENVELOPE GLYCOPROTEIN H.
PubMed=24367260; DOI=10.1371/journal.ppat.1003806;
Gianni T., Salvioli S., Chesnokova L.S., Hutt-Fletcher L.M.,
Campadelli-Fiume G.;
"alphavbeta6- and alphavbeta8-integrins serve as interchangeable
receptors for HSV gH/gL to promote endocytosis and activation of
membrane fusion.";
PLoS Pathog. 9:E1003806-E1003806(2013).
[38]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH WEST NILE VIRUS
ENVELOPE PROTEIN E.
PubMed=23658209; DOI=10.1099/vir.0.052613-0;
Schmidt K., Keller M., Bader B.L., Korytar T., Finke S., Ziegler U.,
Groschup M.H.;
"Integrins modulate the infection efficiency of West Nile virus into
cells.";
J. Gen. Virol. 94:1723-1733(2013).
[39]
FUNCTION.
PubMed=25398877; DOI=10.1074/jbc.M114.579946;
Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J.,
Takada Y.K., Takada Y.;
"Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
integrin activation through direct binding to a newly identified
binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
alpha5beta1.";
J. Biol. Chem. 290:259-271(2015).
[40]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 31-987.
PubMed=11546839; DOI=10.1126/science.1064535;
Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L.,
Joachimiak A., Goodman S.L., Arnaout M.A.;
"Crystal structure of the extracellular segment of integrin alpha
Vbeta3.";
Science 294:339-345(2001).
-!- FUNCTION: The alpha-V (ITGAV) integrins are receptors for
vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix
metalloproteinase-2, osteopontin, osteomodulin, prothrombin,
thrombospondin and vWF. They recognize the sequence R-G-D in a
wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1)
and may act as its coreceptor in CX3CR1-dependent fractalkine
signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF
domain) and this binding is essential for NRG1-ERBB signaling
(PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is
essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds
to IGF1 and this binding is essential for IGF1 signaling
(PubMed:19578119). ITGAV:ITGB3 binds to PLA2G2A via a site (site
2) which is distinct from the classical ligand-binding site (site
1) and this induces integrin conformational changes and enhanced
ligand binding to site 1 (PubMed:18635536, PubMed:25398877).
ITGAV:ITGB3 and ITGAV:ITGB6 act as a receptor for fibrillin-1
(FBN1) and mediate R-G-D-dependent cell adhesion to FBN1
(PubMed:12807887, PubMed:17158881). {ECO:0000269|PubMed:12807887,
ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18441324,
ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:19578119,
ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:23125415,
ECO:0000269|PubMed:25398877}.
-!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a
receptor for adenovirus type C (PubMed:20615244). Integrin
ITGAV:ITGB5 and ITGAV:ITGB3 act as receptors for coxsackievirus A9
and B1 (PubMed:9426447, PubMed:15194773, PubMed:7519807). Integrin
ITGAV:ITGB3 acts as a receptor for herpes virus 8/HHV-8
(PubMed:18045938). Integrin ITGAV:ITGB6 acts as a receptor for
herpes simplex 1/HHV-1 (PubMed:24367260). Integrin ITGAV:ITGB3
acts as a receptor for Human parechovirus 1 (PubMed:11160695).
Integrin ITGAV:ITGB3 acts as a receptor for West nile virus
(PubMed:23658209). In case of HIV-1 infection, the interaction
with extracellular viral Tat protein seems to enhance angiogenesis
in Kaposi's sarcoma lesions (PubMed:10397733).
{ECO:0000269|PubMed:10397733, ECO:0000269|PubMed:11160695,
ECO:0000269|PubMed:15194773, ECO:0000269|PubMed:18045938,
ECO:0000269|PubMed:20615244, ECO:0000269|PubMed:23658209,
ECO:0000269|PubMed:24367260, ECO:0000269|PubMed:7519807,
ECO:0000269|PubMed:9426447}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit is composed of a heavy and a light chain linked by a
disulfide bond. Alpha-V (ITGAV) associates with either beta-1
(ITGB1), beta-3 (ITGB3), beta-5 (ITGB5), beta-6 (ITGB6) or beta-8
(ITGB8). Interacts with CIB1 (PubMed:24011356). Interacts with
RAB25 (PubMed:17925226). Integrins ITGAV:ITGB3 and ITGAV:ITGB5
interact with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB3
and ITGAV:ITGB5 interact with NOV (PubMed:12695522). ITGAV:ITGB3
interacts with ADGRA2 (PubMed:16982628). ITGAV:ITGB3 is found in a
ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415).
ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3
(PubMed:20682778). ITGAV:ITGB3 is found in a ternary complex with
FGF1 and FGFR1 (PubMed:18441324). ITGAV:ITGB3 is found in a
ternary complex with IGF1 and IGF1R (PubMed:19578119). ITGAV:ITGB3
and ITGAV:ITGB6 interact with FBN1 (PubMed:12807887,
PubMed:17158881). {ECO:0000250|UniProtKB:P43406,
ECO:0000250|UniProtKB:P80746, ECO:0000269|PubMed:12695522,
ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16982628,
ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17925226,
ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:19578119,
ECO:0000269|PubMed:20615244, ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:23658209,
ECO:0000269|PubMed:24011356}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
herpes virus 8/HHV-8 envelope glycoprotein B.
{ECO:0000269|PubMed:18045938}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 and
ITGAV:ITGB6 bind to coxsackievirus A9 and coxsackievirus B1 capsid
proteins (PubMed:9426447, PubMed:15194773, PubMed:7519807).
{ECO:0000269|PubMed:15194773, ECO:0000269|PubMed:7519807,
ECO:0000269|PubMed:9426447}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB6 interacts with
herpes simplex 1/HHV-1 envelope glycoprotein H.
{ECO:0000269|PubMed:24367260}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB5 interacts with
adenovirus type C penton protein. {ECO:0000269|PubMed:20615244}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
Human parechovirus 1 capsid proteins.
{ECO:0000269|PubMed:11160695}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
West nile virus envelope protein E. {ECO:0000269|PubMed:23658209}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
{ECO:0000269|PubMed:10397733}.
-!- INTERACTION:
P05106:ITGB3; NbExp=11; IntAct=EBI-298282, EBI-702847;
P18084:ITGB5; NbExp=2; IntAct=EBI-298282, EBI-1223434;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell junction, focal adhesion
{ECO:0000269|PubMed:17158881}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P06756-1; Sequence=Displayed;
Name=2;
IsoId=P06756-2; Sequence=VSP_024351;
Note=No experimental confirmation available.;
Name=3;
IsoId=P06756-3; Sequence=VSP_044914;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93131.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M14648; AAA36808.1; -; mRNA.
EMBL; AF251841; AAG03000.1; -; Genomic_DNA.
EMBL; AF251818; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251819; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251820; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251821; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251822; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251823; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251824; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251825; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251826; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251827; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251828; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251829; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251830; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251831; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251832; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251833; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251834; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251835; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251836; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251837; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251838; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251839; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AF251840; AAG03000.1; JOINED; Genomic_DNA.
EMBL; AK302990; BAH13869.1; -; mRNA.
EMBL; AB209894; BAD93131.1; ALT_INIT; mRNA.
EMBL; AC017101; AAY24257.1; -; Genomic_DNA.
EMBL; EU332844; ABY87533.1; -; Genomic_DNA.
EMBL; CH471058; EAX10934.1; -; Genomic_DNA.
EMBL; BC126231; AAI26232.1; -; mRNA.
EMBL; BC136442; AAI36443.1; -; mRNA.
EMBL; BC144100; AAI44101.1; -; mRNA.
EMBL; U07375; AAA61631.1; -; Genomic_DNA.
CCDS; CCDS2292.1; -. [P06756-1]
CCDS; CCDS46470.1; -. [P06756-2]
CCDS; CCDS46471.1; -. [P06756-3]
PIR; A27421; A27421.
RefSeq; NP_001138471.1; NM_001144999.2.
RefSeq; NP_001138472.1; NM_001145000.2.
RefSeq; NP_002201.1; NM_002210.4.
UniGene; Hs.436873; -.
PDB; 1JV2; X-ray; 3.10 A; A=31-987.
PDB; 1L5G; X-ray; 3.20 A; A=31-987.
PDB; 1M1X; X-ray; 3.30 A; A=31-987.
PDB; 1U8C; X-ray; 3.10 A; A=31-987.
PDB; 3IJE; X-ray; 2.90 A; A=31-997.
PDB; 4G1E; X-ray; 3.00 A; A=31-989.
PDB; 4G1M; X-ray; 2.90 A; A=31-989.
PDB; 4MMX; X-ray; 3.32 A; A=31-989.
PDB; 4MMY; X-ray; 3.18 A; A=31-989.
PDB; 4MMZ; X-ray; 3.10 A; A=31-989.
PDB; 4O02; X-ray; 3.60 A; A=31-992.
PDB; 4UM8; X-ray; 2.85 A; A/C=31-625.
PDB; 4UM9; X-ray; 2.50 A; A/C=31-625.
PDB; 5FFG; X-ray; 2.25 A; A=31-625.
PDB; 5FFO; X-ray; 3.49 A; A/E=31-625.
PDB; 5NEM; EM; 3.10 A; A=31-624.
PDB; 5NER; EM; 3.10 A; A=31-624.
PDB; 5NET; EM; 3.10 A; A=31-624.
PDB; 5NEU; EM; 3.10 A; A=31-624.
PDBsum; 1JV2; -.
PDBsum; 1L5G; -.
PDBsum; 1M1X; -.
PDBsum; 1U8C; -.
PDBsum; 3IJE; -.
PDBsum; 4G1E; -.
PDBsum; 4G1M; -.
PDBsum; 4MMX; -.
PDBsum; 4MMY; -.
PDBsum; 4MMZ; -.
PDBsum; 4O02; -.
PDBsum; 4UM8; -.
PDBsum; 4UM9; -.
PDBsum; 5FFG; -.
PDBsum; 5FFO; -.
PDBsum; 5NEM; -.
PDBsum; 5NER; -.
PDBsum; 5NET; -.
PDBsum; 5NEU; -.
ProteinModelPortal; P06756; -.
SMR; P06756; -.
BioGrid; 109891; 68.
CORUM; P06756; -.
DIP; DIP-31785N; -.
ELM; P06756; -.
IntAct; P06756; 15.
MINT; MINT-209462; -.
STRING; 9606.ENSP00000261023; -.
BindingDB; P06756; -.
ChEMBL; CHEMBL3660; -.
DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
GuidetoPHARMACOLOGY; 2453; -.
TCDB; 8.A.54.1.4; the integrin (integrin) family.
iPTMnet; P06756; -.
PhosphoSitePlus; P06756; -.
DMDM; 143811408; -.
EPD; P06756; -.
MaxQB; P06756; -.
PaxDb; P06756; -.
PeptideAtlas; P06756; -.
PRIDE; P06756; -.
Ensembl; ENST00000261023; ENSP00000261023; ENSG00000138448. [P06756-1]
Ensembl; ENST00000374907; ENSP00000364042; ENSG00000138448. [P06756-2]
Ensembl; ENST00000433736; ENSP00000404291; ENSG00000138448. [P06756-3]
GeneID; 3685; -.
KEGG; hsa:3685; -.
UCSC; uc002upq.5; human. [P06756-1]
CTD; 3685; -.
DisGeNET; 3685; -.
EuPathDB; HostDB:ENSG00000138448.11; -.
GeneCards; ITGAV; -.
HGNC; HGNC:6150; ITGAV.
HPA; CAB002499; -.
HPA; HPA004856; -.
MIM; 193210; gene.
neXtProt; NX_P06756; -.
OpenTargets; ENSG00000138448; -.
PharmGKB; PA37336; -.
eggNOG; ENOG410IPB5; Eukaryota.
eggNOG; ENOG410YR19; LUCA.
GeneTree; ENSGT00760000118782; -.
HOGENOM; HOG000231603; -.
HOVERGEN; HBG006186; -.
InParanoid; P06756; -.
KO; K06487; -.
OMA; SCFNVRF; -.
OrthoDB; EOG091G05Z4; -.
PhylomeDB; P06756; -.
TreeFam; TF105391; -.
Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; P06756; -.
SIGNOR; P06756; -.
ChiTaRS; ITGAV; human.
EvolutionaryTrace; P06756; -.
GeneWiki; ITGAV; -.
GenomeRNAi; 3685; -.
PMAP-CutDB; B0LPF4; -.
PRO; PR:P06756; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138448; -.
CleanEx; HS_ITGAV; -.
ExpressionAtlas; P06756; baseline and differential.
Genevisible; P06756; HS.
GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0034683; C:integrin alphav-beta3 complex; IDA:UniProtKB.
GO; GO:0034684; C:integrin alphav-beta5 complex; IDA:UniProtKB.
GO; GO:0034685; C:integrin alphav-beta6 complex; IEA:Ensembl.
GO; GO:0034686; C:integrin alphav-beta8 complex; IDA:UniProtKB.
GO; GO:0008305; C:integrin complex; IDA:BHF-UCL.
GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISS:BHF-UCL.
GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; IDA:UniProtKB.
GO; GO:1990430; F:extracellular matrix protein binding; IDA:UniProtKB.
GO; GO:0001968; F:fibronectin binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001846; F:opsonin binding; IEA:Ensembl.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IDA:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IDA:BHF-UCL.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0016049; P:cell growth; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
GO; GO:0052066; P:entry of symbiont into host cell by promotion of host phagocytosis; NAS:BHF-UCL.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:BHF-UCL.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISS:BHF-UCL.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB.
GO; GO:2000536; P:negative regulation of entry of bacterium into host cell; IDA:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL.
GO; GO:0032369; P:negative regulation of lipid transport; IMP:BHF-UCL.
GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; IMP:BHF-UCL.
GO; GO:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
GO; GO:2000425; P:regulation of apoptotic cell clearance; ISS:BHF-UCL.
GO; GO:0050764; P:regulation of phagocytosis; IDA:BHF-UCL.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0038044; P:transforming growth factor-beta secretion; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
GO; GO:0046718; P:viral entry into host cell; IMP:UniProtKB.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR032695; Integrin_dom.
Pfam; PF01839; FG-GAP; 3.
Pfam; PF00357; Integrin_alpha; 1.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Cell junction; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Integrin;
Membrane; Metal-binding; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000269|PubMed:2467745}.
CHAIN 31 1048 Integrin alpha-V.
/FTId=PRO_0000016301.
CHAIN 31 889 Integrin alpha-V heavy chain.
/FTId=PRO_0000016302.
CHAIN 891 1048 Integrin alpha-V light chain.
/FTId=PRO_0000016303.
TOPO_DOM 31 992 Extracellular. {ECO:0000255}.
TRANSMEM 993 1016 Helical. {ECO:0000255}.
TOPO_DOM 1017 1048 Cytoplasmic. {ECO:0000255}.
REPEAT 32 98 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 109 170 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 173 225 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 237 291 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 292 357 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 358 415 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 419 482 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 260 268 {ECO:0000255}.
CA_BIND 314 322 {ECO:0000255}.
CA_BIND 379 387 {ECO:0000255}.
CA_BIND 443 451 {ECO:0000255}.
MOTIF 1019 1023 GFFKR motif.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 704 704 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 835 835 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 851 851 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 874 874 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 973 973 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 980 980 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 89 97 {ECO:0000269|PubMed:14596610}.
DISULFID 138 158 {ECO:0000269|PubMed:14596610}.
DISULFID 172 185 {ECO:0000269|PubMed:14596610}.
DISULFID 491 502 {ECO:0000269|PubMed:14596610}.
DISULFID 508 565 {ECO:0000269|PubMed:14596610}.
DISULFID 626 632 {ECO:0000269|PubMed:14596610}.
DISULFID 698 711 {ECO:0000269|PubMed:14596610}.
DISULFID 852 914 Interchain (between heavy and light
chains). {ECO:0000269|PubMed:14596610}.
DISULFID 904 909 {ECO:0000269|PubMed:14596610}.
VAR_SEQ 1 62 MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEY
SGPEGSYFGFAVDFFVPSASS -> MLLGTLLLILYILMLC
(in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044914.
VAR_SEQ 175 211 QDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQG ->
R (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_024351.
VARIANT 405 405 I -> V (in dbSNP:rs3738918).
/FTId=VAR_024289.
VARIANT 548 548 S -> A (in dbSNP:rs2230615).
/FTId=VAR_055970.
VARIANT 783 783 V -> I (in dbSNP:rs2230616).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2430295,
ECO:0000269|PubMed:2443500,
ECO:0000269|Ref.4, ECO:0000269|Ref.6,
ECO:0000269|Ref.7}.
/FTId=VAR_031547.
CONFLICT 425 425 W -> R (in Ref. 2; AAG03000).
{ECO:0000305}.
CONFLICT 700 700 F -> L (in Ref. 8; AAI44101).
{ECO:0000305}.
CONFLICT 1039 1039 H -> R (in Ref. 2; AAG03000).
{ECO:0000305}.
STRAND 39 42 {ECO:0000244|PDB:5FFG}.
TURN 45 50 {ECO:0000244|PDB:5FFG}.
STRAND 51 56 {ECO:0000244|PDB:5FFG}.
STRAND 60 62 {ECO:0000244|PDB:4UM9}.
STRAND 65 70 {ECO:0000244|PDB:5FFG}.
STRAND 85 95 {ECO:0000244|PDB:5FFG}.
STRAND 97 100 {ECO:0000244|PDB:5FFG}.
STRAND 109 111 {ECO:0000244|PDB:5FFG}.
STRAND 114 118 {ECO:0000244|PDB:5FFG}.
STRAND 126 131 {ECO:0000244|PDB:5FFG}.
STRAND 134 139 {ECO:0000244|PDB:5FFG}.
STRAND 147 150 {ECO:0000244|PDB:5FFG}.
STRAND 157 162 {ECO:0000244|PDB:5FFG}.
STRAND 165 169 {ECO:0000244|PDB:5FFG}.
STRAND 174 176 {ECO:0000244|PDB:5FFG}.
TURN 178 184 {ECO:0000244|PDB:5FFG}.
STRAND 189 193 {ECO:0000244|PDB:5FFG}.
STRAND 197 203 {ECO:0000244|PDB:5FFG}.
HELIX 206 209 {ECO:0000244|PDB:5FFG}.
STRAND 211 217 {ECO:0000244|PDB:5FFG}.
HELIX 218 223 {ECO:0000244|PDB:5FFG}.
STRAND 235 239 {ECO:0000244|PDB:4G1E}.
HELIX 245 247 {ECO:0000244|PDB:5FFG}.
STRAND 254 259 {ECO:0000244|PDB:5FFG}.
STRAND 261 266 {ECO:0000244|PDB:5FFG}.
STRAND 268 273 {ECO:0000244|PDB:5FFG}.
HELIX 276 279 {ECO:0000244|PDB:5FFG}.
STRAND 282 286 {ECO:0000244|PDB:5FFG}.
TURN 288 290 {ECO:0000244|PDB:5FFG}.
STRAND 293 298 {ECO:0000244|PDB:5FFG}.
STRAND 308 313 {ECO:0000244|PDB:5FFG}.
STRAND 316 319 {ECO:0000244|PDB:5FFG}.
STRAND 322 327 {ECO:0000244|PDB:5FFG}.
STRAND 331 333 {ECO:0000244|PDB:5FFG}.
STRAND 335 337 {ECO:0000244|PDB:4G1M}.
STRAND 339 341 {ECO:0000244|PDB:5FFG}.
STRAND 344 350 {ECO:0000244|PDB:5FFG}.
STRAND 352 354 {ECO:0000244|PDB:3IJE}.
STRAND 356 362 {ECO:0000244|PDB:5FFG}.
STRAND 364 368 {ECO:0000244|PDB:1JV2}.
HELIX 370 372 {ECO:0000244|PDB:1U8C}.
STRAND 374 378 {ECO:0000244|PDB:5FFG}.
STRAND 383 385 {ECO:0000244|PDB:5FFG}.
STRAND 387 392 {ECO:0000244|PDB:5FFG}.
HELIX 397 399 {ECO:0000244|PDB:5FFG}.
STRAND 402 409 {ECO:0000244|PDB:5FFG}.
STRAND 410 413 {ECO:0000244|PDB:4UM8}.
STRAND 418 422 {ECO:0000244|PDB:5FFG}.
STRAND 428 430 {ECO:0000244|PDB:4UM9}.
STRAND 436 442 {ECO:0000244|PDB:5FFG}.
STRAND 447 449 {ECO:0000244|PDB:5FFG}.
STRAND 451 456 {ECO:0000244|PDB:5FFG}.
HELIX 457 459 {ECO:0000244|PDB:5FFG}.
STRAND 461 465 {ECO:0000244|PDB:5FFG}.
STRAND 470 485 {ECO:0000244|PDB:5FFG}.
STRAND 494 499 {ECO:0000244|PDB:3IJE}.
STRAND 502 512 {ECO:0000244|PDB:5FFG}.
STRAND 514 516 {ECO:0000244|PDB:5FFG}.
STRAND 519 528 {ECO:0000244|PDB:5FFG}.
TURN 529 532 {ECO:0000244|PDB:5FFG}.
STRAND 535 537 {ECO:0000244|PDB:4G1M}.
STRAND 541 543 {ECO:0000244|PDB:5FFG}.
TURN 544 546 {ECO:0000244|PDB:5FFG}.
STRAND 547 558 {ECO:0000244|PDB:5FFG}.
STRAND 559 561 {ECO:0000244|PDB:4MMY}.
STRAND 564 572 {ECO:0000244|PDB:5FFG}.
HELIX 575 577 {ECO:0000244|PDB:5FFG}.
STRAND 585 593 {ECO:0000244|PDB:5FFG}.
TURN 595 597 {ECO:0000244|PDB:4UM9}.
STRAND 601 603 {ECO:0000244|PDB:4G1E}.
STRAND 610 612 {ECO:0000244|PDB:5FFG}.
STRAND 614 623 {ECO:0000244|PDB:5FFG}.
TURN 627 630 {ECO:0000244|PDB:3IJE}.
STRAND 636 641 {ECO:0000244|PDB:3IJE}.
STRAND 646 648 {ECO:0000244|PDB:3IJE}.
STRAND 653 663 {ECO:0000244|PDB:3IJE}.
STRAND 668 670 {ECO:0000244|PDB:3IJE}.
STRAND 672 676 {ECO:0000244|PDB:3IJE}.
STRAND 681 686 {ECO:0000244|PDB:3IJE}.
STRAND 691 693 {ECO:0000244|PDB:4G1E}.
STRAND 697 701 {ECO:0000244|PDB:3IJE}.
STRAND 703 705 {ECO:0000244|PDB:3IJE}.
STRAND 708 712 {ECO:0000244|PDB:3IJE}.
STRAND 715 717 {ECO:0000244|PDB:3IJE}.
STRAND 722 731 {ECO:0000244|PDB:3IJE}.
STRAND 735 737 {ECO:0000244|PDB:4G1E}.
STRAND 739 748 {ECO:0000244|PDB:3IJE}.
STRAND 752 754 {ECO:0000244|PDB:3IJE}.
STRAND 760 767 {ECO:0000244|PDB:3IJE}.
STRAND 772 786 {ECO:0000244|PDB:3IJE}.
TURN 798 802 {ECO:0000244|PDB:3IJE}.
STRAND 805 814 {ECO:0000244|PDB:3IJE}.
STRAND 816 818 {ECO:0000244|PDB:3IJE}.
STRAND 820 833 {ECO:0000244|PDB:3IJE}.
STRAND 839 856 {ECO:0000244|PDB:3IJE}.
STRAND 900 902 {ECO:0000244|PDB:3IJE}.
TURN 904 906 {ECO:0000244|PDB:3IJE}.
STRAND 907 916 {ECO:0000244|PDB:3IJE}.
STRAND 923 933 {ECO:0000244|PDB:3IJE}.
HELIX 935 938 {ECO:0000244|PDB:3IJE}.
STRAND 941 944 {ECO:0000244|PDB:3IJE}.
STRAND 948 960 {ECO:0000244|PDB:3IJE}.
STRAND 964 966 {ECO:0000244|PDB:4G1E}.
STRAND 971 982 {ECO:0000244|PDB:3IJE}.
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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