ID ITB1_HUMAN Reviewed; 798 AA.
AC P05556; A8K6N2; D3DRX9; D3DRY3; D3DRY4; D3DRY5; P78466; P78467; Q13089;
AC Q13090; Q13091; Q13212; Q14622; Q14647; Q29RW2; Q7Z3V1; Q8WUM6;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 267.
DE RecName: Full=Integrin beta-1 {ECO:0000305};
DE AltName: Full=Fibronectin receptor subunit beta;
DE AltName: Full=Glycoprotein IIa;
DE Short=GPIIA;
DE AltName: Full=VLA-4 subunit beta;
DE AltName: CD_antigen=CD29;
DE Flags: Precursor;
GN Name=ITGB1 {ECO:0000312|HGNC:HGNC:6153}; Synonyms=FNRB, MDF2, MSK12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2958481; DOI=10.1083/jcb.105.3.1183;
RA Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D.,
RA Ruoslahti E.;
RT "Amino acid sequence of the human fibronectin receptor.";
RL J. Cell Biol. 105:1183-1190(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 717-757, CHARACTERIZATION OF BETA-1B,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7681433; DOI=10.1083/jcb.121.1.171;
RA Balzac F., Belkin A.M., Koteliansky V.E., Balabanov Y.V., Altruda F.,
RA Silengo L., Tarone G.;
RT "Expression and functional analysis of a cytoplasmic domain variant of the
RT beta 1 integrin subunit.";
RL J. Cell Biol. 121:171-178(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 717-757, AND FUNCTION.
RX PubMed=7523423; DOI=10.1083/jcb.127.2.557;
RA Balzac F., Retta S.F., Albini A., Melchiorri A., Koteliansky V.E.,
RA Geuna M., Silengo L., Tarone G.;
RT "Expression of beta 1B integrin isoform in CHO cells results in a dominant
RT negative effect on cell adhesion and motility.";
RL J. Cell Biol. 127:557-565(1994).
RN [9]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=2249781; DOI=10.1016/0378-1119(90)90369-3;
RA Altruda F., Cervella P., Tarone G., Botta C., Balzac F., Stefanuto G.,
RA Silengo L.;
RT "A human integrin beta 1 subunit with a unique cytoplasmic domain generated
RT by alternative mRNA processing.";
RL Gene 95:261-266(1990).
RN [10]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=1551917; DOI=10.1016/s0021-9258(19)50545-2;
RA Languino L.R., Ruoslahti E.;
RT "An alternative form of the integrin beta 1 subunit with a variant
RT cytoplasmic domain.";
RL J. Biol. Chem. 267:7116-7120(1992).
RN [11]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=7545396; DOI=10.1006/bbrc.1995.2285;
RA Zhidkova N.I., Belkin A.M., Mayne R.;
RT "Novel isoform of beta 1 integrin expressed in skeletal and cardiac
RT muscle.";
RL Biochem. Biophys. Res. Commun. 214:279-285(1995).
RN [12]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE SPECIFICITY.
RX PubMed=7544298; DOI=10.1016/0014-5793(95)00814-p;
RA van der Flier A., Kuikman I., Baudoin C., van der Neut R., Sonnenberg A.;
RT "A novel beta 1 integrin isoform produced by alternative splicing: unique
RT expression in cardiac and skeletal muscle.";
RL FEBS Lett. 369:340-344(1995).
RN [13]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=9494094; DOI=10.1042/bj3301255;
RA Svineng G., Faessler R., Johansson S.;
RT "Identification of beta1C-2, a novel variant of the integrin beta1 subunit
RT generated by utilization of an alternative splice acceptor site in exon
RT C.";
RL Biochem. J. 330:1255-1263(1998).
RN [14]
RP PROTEIN SEQUENCE OF 775-784 (ISOFORM 5), IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH ACE2.
RX PubMed=15276642; DOI=10.1016/j.bbadis.2004.05.005;
RA Lin Q., Keller R.S., Weaver B., Zisman L.S.;
RT "Interaction of ACE2 and integrin beta1 in failing human heart.";
RL Biochim. Biophys. Acta 1689:175-178(2004).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ECHOVIRUS 1 AND
RP HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
RX PubMed=8411387; DOI=10.1128/jvi.67.11.6847-6852.1993;
RA Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H., Modlin J.,
RA Finberg R.W.;
RT "Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human
RT VLA-2.";
RL J. Virol. 67:6847-6852(1993).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=8567725; DOI=10.1083/jcb.132.1.211;
RA Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D., Maier A.,
RA Tarone G., Koteliansky V.E., Burridge K.;
RT "Beta 1D integrin displaces the beta 1A isoform in striated muscles:
RT localization at junctional structures and signaling potential in nonmuscle
RT cells.";
RL J. Cell Biol. 132:211-226(1996).
RN [17]
RP INTERACTION WITH LGALS3BP.
RX PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
RA Sasaki T., Brakebusch C., Engel J., Timpl R.;
RT "Mac-2 binding protein is a cell-adhesive protein of the extracellular
RT matrix which self-assembles into ring-like structures and binds beta1
RT integrins, collagens and fibronectin.";
RL EMBO J. 17:1606-1613(1998).
RN [18]
RP FUNCTION (MICROBIAL INFECTION), AND 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 vascular
RT cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3
RT integrins and by mobilizing sequestered basic fibroblast growth factor.";
RL Blood 94:663-672(1999).
RN [19]
RP FUNCTION, SUBUNIT, INTERACTION WITH FAP, AND SUBCELLULAR LOCATION.
RX PubMed=10455171; DOI=10.1074/jbc.274.35.24947;
RA Mueller S.C., Ghersi G., Akiyama S.K., Sang Q.X., Howard L.,
RA Pineiro-Sanchez M., Nakahara H., Yeh Y., Chen W.T.;
RT "A novel protease-docking function of integrin at invadopodia.";
RL J. Biol. Chem. 274:24947-24952(1999).
RN [20]
RP INTERACTION WITH NMRK2.
RC TISSUE=Heart;
RX PubMed=10613898; DOI=10.1083/jcb.147.7.1391;
RA Li J., Mayne R., Wu C.;
RT "A novel muscle-specific beta 1 integrin binding protein (MIBP) that
RT modulates myogenic differentiation.";
RL J. Cell Biol. 147:1391-1398(1999).
RN [21]
RP INTERACTION WITH ITGB1BP1.
RX PubMed=11741838; DOI=10.1093/hmg/10.25.2953;
RA Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.;
RT "Interaction between krit1 and icap1alpha infers perturbation of integrin
RT beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous
RT malformation.";
RL Hum. Mol. Genet. 10:2953-2960(2001).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=11919189; DOI=10.1074/jbc.m200200200;
RA Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C.,
RA Block M.R., Albiges-Rizo C.;
RT "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha)
RT interacts directly with the metastasis suppressor nm23-H2, and both
RT proteins are targeted to newly formed cell adhesion sites upon integrin
RT engagement.";
RL J. Biol. Chem. 277:20895-20902(2002).
RN [23]
RP INTERACTION WITH FLNA AND FLNB, AND MUTAGENESIS OF GLY-778 AND ALA-786.
RX PubMed=11807098; DOI=10.1083/jcb.200103037;
RA van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T.,
RA Shapiro S.S., Sonnenberg A.;
RT "Different splice variants of filamin-B affect myogenesis, subcellular
RT distribution, and determine binding to integrin (beta) subunits.";
RL J. Cell Biol. 156:361-376(2002).
RN [24]
RP INTERACTION WITH ITGB1BP1, AND MUTAGENESIS OF 786-ALA--VAL-791.
RX PubMed=11807099; DOI=10.1083/jcb.200108030;
RA Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L.,
RA Eva A., Tarone G.;
RT "The integrin cytoplasmic domain-associated protein ICAP-1 binds and
RT regulates Rho family GTPases during cell spreading.";
RL J. Cell Biol. 156:377-387(2002).
RN [25]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN PARVOVIRUS B19
RP CAPSID PROTEIN.
RX PubMed=12907437; DOI=10.1182/blood-2003-05-1522;
RA Weigel-Kelley K.A., Yoder M.C., Srivastava A.;
RT "Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19:
RT requirement of functional activation of beta1 integrin for viral entry.";
RL Blood 102:3927-3933(2003).
RN [26]
RP FUNCTION, AND INTERACTION WITH ITGB1BP1.
RX PubMed=12473654; DOI=10.1074/jbc.m211258200;
RA Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N.,
RA Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.;
RT "Disruption of focal adhesions by integrin cytoplasmic domain-associated
RT protein-1 alpha.";
RL J. Biol. Chem. 278:6567-6574(2003).
RN [27]
RP INTERACTION WITH CCN3.
RX PubMed=12695522; DOI=10.1074/jbc.m302028200;
RA Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y., Lau L.F.;
RT "CCN3 (NOV) is a novel angiogenic regulator of the CCN protein family.";
RL J. Biol. Chem. 278:24200-24208(2003).
RN [28]
RP FUNCTION, AND INTERACTION WITH FBN1.
RX PubMed=12807887; DOI=10.1074/jbc.m303159200;
RA Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
RA Shuttleworth C.A., Humphries M.J., Kielty C.M.;
RT "Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by
RT alpha 5 beta 1 and alpha v beta 3 integrins.";
RL J. Biol. Chem. 278:34605-34616(2003).
RN [29]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ROTAVIRUS VP4
RP PROTEIN.
RX PubMed=12941907; DOI=10.1128/jvi.77.18.9969-9978.2003;
RA Graham K.L., Halasz P., Tan Y., Hewish M.J., Takada Y., Mackow E.R.,
RA Robinson M.K., Coulson B.S.;
RT "Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via
RT VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7
RT during cell entry.";
RL J. Virol. 77:9969-9978(2003).
RN [30]
RP INTERACTION WITH RANBP9.
RX PubMed=14722085; DOI=10.1074/jbc.m313515200;
RA Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
RA Fabbri M., Pardi R., Bianchi E.;
RT "RanBPM is a phosphoprotein that associates with the plasma membrane and
RT interacts with the integrin LFA-1.";
RL J. Biol. Chem. 279:13027-13034(2004).
RN [31]
RP INTERACTION WITH MDK.
RX PubMed=15466886; DOI=10.1242/jcs.01423;
RA Muramatsu H., Zou P., Suzuki H., Oda Y., Chen G.Y., Sakaguchi N.,
RA Sakuma S., Maeda N., Noda M., Takada Y., Muramatsu T.;
RT "alpha4beta1- and alpha6beta1-integrins are functional receptors for
RT midkine, a heparin-binding growth factor.";
RL J. Cell Sci. 117:5405-5415(2004).
RN [32]
RP INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
RX PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT engagement of galectin-3 and alpha3beta1 integrin.";
RL Mol. Biol. Cell 15:3580-3590(2004).
RN [33]
RP INTERACTION WITH MYO10.
RX PubMed=15156152; DOI=10.1038/ncb1136;
RA Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
RA Cheney R.E., Stromblad S.;
RT "Myosin-X provides a motor-based link between integrins and the
RT cytoskeleton.";
RL Nat. Cell Biol. 6:523-531(2004).
RN [34]
RP FUNCTION, INTERACTION WITH ACAP1, AND SUBCELLULAR LOCATION.
RX PubMed=16256741; DOI=10.1016/j.devcel.2005.09.012;
RA Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.;
RT "Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent
RT recycling of integrin beta1 to control cell migration.";
RL Dev. Cell 9:663-673(2005).
RN [35]
RP INTERACTION WITH FLNB AND FLNC.
RX PubMed=16076904; DOI=10.1242/jcs.02484;
RA Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A.,
RA Carpen O., Faulkner G., Borradori L.;
RT "The Z-disc proteins myotilin and FATZ-1 interact with each other and are
RT connected to the sarcolemma via muscle-specific filamins.";
RL J. Cell Sci. 118:3739-3749(2005).
RN [36]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [37]
RP INTERACTION WITH RAB21.
RX PubMed=16754960; DOI=10.1083/jcb.200509019;
RA Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
RA Ivaska J.;
RT "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic
RT of beta1-integrins.";
RL J. Cell Biol. 173:767-780(2006).
RN [38]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [39]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MAMMALIAN REOVIRUS
RP CAPSID PROTEINS.
RX PubMed=16501085; DOI=10.1128/jvi.80.6.2760-2770.2006;
RA Maginnis M.S., Forrest J.C., Kopecky-Bromberg S.A., Dickeson S.K.,
RA Santoro S.A., Zutter M.M., Nemerow G.R., Bergelson J.M., Dermody T.S.;
RT "Beta1 integrin mediates internalization of mammalian reovirus.";
RL J. Virol. 80:2760-2770(2006).
RN [40]
RP FUNCTION, INTERACTION WITH KRT1, AND SUBCELLULAR LOCATION.
RX PubMed=17956333; DOI=10.1042/bst0351292;
RA Chuang N.N., Huang C.C.;
RT "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7
RT cells.";
RL Biochem. Soc. Trans. 35:1292-1294(2007).
RN [41]
RP INTERACTION WITH RAB25.
RX PubMed=17925226; DOI=10.1016/j.devcel.2007.08.012;
RA Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W.,
RA Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W.,
RA Ozanne B.W., Norman J.C.;
RT "Rab25 associates with alpha5beta1 integrin to promote invasive migration
RT in 3D microenvironments.";
RL Dev. Cell 13:496-510(2007).
RN [42]
RP FUNCTION, INTERACTION WITH FBN1, AND SUBCELLULAR LOCATION.
RX PubMed=17158881; DOI=10.1074/jbc.m607008200;
RA Jovanovic J., Takagi J., Choulier L., Abrescia N.G., Stuart D.I.,
RA van der Merwe P.A., Mardon H.J., Handford P.A.;
RT "alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative studies
RT of molecular determinants underlying integrin-rgd affinity and
RT specificity.";
RL J. Biol. Chem. 282:6743-6751(2007).
RN [43]
RP INTERACTION WITH TNS4.
RX PubMed=17643115; DOI=10.1038/ncb1622;
RA Katz M., Amit I., Citri A., Shay T., Carvalho S., Lavi S., Milanezi F.,
RA Lyass L., Amariglio N., Jacob-Hirsch J., Ben-Chetrit N., Tarcic G.,
RA Lindzen M., Avraham R., Liao Y.C., Trusk P., Lyass A., Rechavi G.,
RA Spector N.L., Lo S.H., Schmitt F., Bacus S.S., Yarden Y.;
RT "A reciprocal tensin-3-cten switch mediates EGF-driven mammary cell
RT migration.";
RL Nat. Cell Biol. 9:961-969(2007).
RN [44]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
RA Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R.,
RA Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M.,
RA Ivaska J.;
RT "Integrin trafficking regulated by Rab21 is necessary for cytokinesis.";
RL Dev. Cell 15:371-385(2008).
RN [45]
RP FUNCTION.
RX PubMed=18635536; DOI=10.1074/jbc.m804835200;
RA Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S., Liu F.T.,
RA Takada Y.K., Takada Y.;
RT "Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins
RT alphavbeta3 and alpha4beta1 and induces proliferation of monocytic cells in
RT an integrin-dependent manner.";
RL J. Biol. Chem. 283:26107-26115(2008).
RN [46]
RP FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, AND INTERACTION WITH
RP JAML.
RX PubMed=19064666; DOI=10.1083/jcb.200805061;
RA Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.;
RT "JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis
RT by alpha4beta1 integrin activation.";
RL J. Cell Biol. 183:1159-1173(2008).
RN [47]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR
RP VIRUS/HHV-4 GB PROTEIN.
RX PubMed=17945327; DOI=10.1016/j.virol.2007.09.012;
RA Xiao J., Palefsky J.M., Herrera R., Berline J., Tugizov S.M.;
RT "The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to oral
RT epithelial cells.";
RL Virology 370:430-442(2008).
RN [48]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [49]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [50]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [51]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-794, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [52]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HHV-5 GB.
RX PubMed=20660204; DOI=10.1128/jvi.00710-10;
RA Feire A.L., Roy R.M., Manley K., Compton T.;
RT "The glycoprotein B disintegrin-like domain binds beta 1 integrin to
RT mediate cytomegalovirus entry.";
RL J. Virol. 84:10026-10037(2010).
RN [53]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [54]
RP POSSIBLE FUNCTION AS A RECEPTOR (MICROBIAL INFECTION), AND INTERACTION WITH
RP N.MENINGITIDIS ADHESIN A (MICROBIAL INFECTION).
RX PubMed=21471204; DOI=10.1074/jbc.m110.188326;
RA Naegele V., Heesemann J., Schielke S., Jimenez-Soto L.F., Kurzai O.,
RA Ackermann N.;
RT "Neisseria meningitidis adhesin NadA targets beta1 integrins: functional
RT similarity to Yersinia invasin.";
RL J. Biol. Chem. 286:20536-20546(2011).
RN [55]
RP INTERACTION WITH ASAP3.
RX PubMed=22027826; DOI=10.1074/jbc.m111.278770;
RA Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X., Fan L.,
RA Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X.;
RT "ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal growth
RT factor-stimulated integrin beta1 recycling in cell migration.";
RL J. Biol. Chem. 286:43735-43747(2011).
RN [56]
RP FUNCTION, INTERACTION WITH FERMT2 AND TLN1, AND MUTAGENESIS OF VAL-787.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [57]
RP INTERACTION WITH FERMT2.
RX PubMed=21325030; DOI=10.1242/jcs.076976;
RA Qu H., Tu Y., Shi X., Larjava H., Saleem M.A., Shattil S.J., Fukuda K.,
RA Qin J., Kretzler M., Wu C.;
RT "Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition
RT through interactions with phosphoinositides and integrins.";
RL J. Cell Sci. 124:879-891(2011).
RN [58]
RP INTERACTION WITH TNC.
RX PubMed=22654117; DOI=10.1074/jbc.m112.355016;
RA Sato-Nishiuchi R., Nakano I., Ozawa A., Sato Y., Takeichi M., Kiyozumi D.,
RA Yamazaki K., Yasunaga T., Futaki S., Sekiguchi K.;
RT "Polydom/SVEP1 is a ligand for integrin alpha9beta1.";
RL J. Biol. Chem. 287:25615-25630(2012).
RN [59]
RP FUNCTION, BINDING TO CX3CL1, IDENTIFICATION IN A COMPLEX WITH CX3CR1 AND
RP CX3CL1, AND CX3CL1-BINDING REGION.
RX PubMed=23125415; DOI=10.4049/jimmunol.1200889;
RA Fujita M., Takada Y.K., Takada Y.;
RT "Integrins alphavbeta3 and alpha4beta1 act as coreceptors for fractalkine,
RT and the integrin-binding defective mutant of fractalkine is an antagonist
RT of CX3CR1.";
RL J. Immunol. 189:5809-5819(2012).
RN [60]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [61]
RP INTERACTION WITH TNS4.
RX PubMed=24814316; DOI=10.1016/j.devcel.2014.03.024;
RA Muharram G., Sahgal P., Korpela T., De Franceschi N., Kaukonen R.,
RA Clark K., Tulasne D., Carpen O., Ivaska J.;
RT "Tensin-4-dependent MET stabilization is essential for survival and
RT proliferation in carcinoma cells.";
RL Dev. Cell 29:421-436(2014).
RN [62]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785 AND THR-789, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [63]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-794, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [64]
RP FUNCTION.
RX PubMed=25398877; DOI=10.1074/jbc.m114.579946;
RA Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J., Takada Y.K.,
RA Takada Y.;
RT "Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
RT integrin activation through direct binding to a newly identified binding
RT site (site 2) in integrins alphavbeta3, alpha4beta1, and alpha5beta1.";
RL J. Biol. Chem. 290:259-271(2015).
RN [65]
RP BINDING TO CX3CL1, AND CX3CL1-BINDING REGION.
RX PubMed=24789099; DOI=10.1371/journal.pone.0096372;
RA Fujita M., Takada Y.K., Takada Y.;
RT "The chemokine fractalkine can activate integrins without CX3CR1 through
RT direct binding to a ligand-binding site distinct from the classical RGD-
RT binding site.";
RL PLoS ONE 9:E96372-E96372(2014).
RN [66]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [67]
RP FUNCTION, AND INTERACTION WITH IL1B.
RX PubMed=29030430; DOI=10.1074/jbc.m117.818302;
RA Takada Y.K., Yu J., Fujita M., Saegusa J., Wu C.Y., Takada Y.;
RT "Direct binding to integrins and loss of disulfide linkage in interleukin-
RT 1beta (IL-1beta) are involved in the agonistic action of IL-1beta.";
RL J. Biol. Chem. 292:20067-20075(2017).
RN [68]
RP FUNCTION.
RX PubMed=31331973; DOI=10.4049/jimmunol.1801630;
RA Takada Y.K., Yu J., Shimoda M., Takada Y.;
RT "Integrin Binding to the Trimeric Interface of CD40L Plays a Critical Role
RT in CD40/CD40L Signaling.";
RL J. Immunol. 203:1383-1391(2019).
RN [69]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH R.DELEMAR COTH7 (MICROBIAL
RP INFECTION), SUBCELLULAR LOCATION, INDUCTION, AND BIOTECHNOLOGY.
RX PubMed=32487760; DOI=10.1128/mbio.01087-20;
RA Alqarihi A., Gebremariam T., Gu Y., Swidergall M., Alkhazraji S.,
RA Soliman S.S.M., Bruno V.M., Edwards J.E. Jr., Filler S.G., Uppuluri P.,
RA Ibrahim A.S.;
RT "GRP78 and Integrins Play Different Roles in Host Cell Invasion during
RT Mucormycosis.";
RL MBio 11:e01087-e01087(2020).
RN [70]
RP INTERACTION WITH ACE2, AND INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN
RP (MICROBIAL INFECTION).
RX PubMed=33102950; DOI=10.1016/j.jacbts.2020.10.003;
RA Beddingfield B.J., Iwanaga N., Chapagain P.P., Zheng W., Roy C.J., Hu T.Y.,
RA Kolls J.K., Bix G.J.;
RT "The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2
RT Infection.";
RL JACC Basic Transl. Sci. 6:1-8(2021).
RN [71]
RP FUNCTION, INTERACTION WITH SVEP1, AND TISSUE SPECIFICITY.
RX PubMed=35802072; DOI=10.1111/bph.15921;
RA Morris G.E., Denniff M.J., Karamanavi E., Andrews S.A., Kostogrys R.B.,
RA Bountziouka V., Ghaderi-Najafabadi M., Shamkhi N., McConnell G.,
RA Kaiser M.A., Carleton L., Schofield C., Kessler T., Rainbow R.D.,
RA Samani N.J., Webb T.R.;
RT "The integrin ligand SVEP1 regulates GPCR-mediated vasoconstriction via
RT integrins alpha9beta1 and alpha4beta1.";
RL Br. J. Pharmacol. 179:4958-4973(2022).
RN [72]
RP INTERACTION WITH TNS3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-783 AND
RP TYR-795.
RX PubMed=35687021; DOI=10.1083/jcb.202108027;
RA Zuidema A., Atherton P., Kreft M., Hoekman L., Bleijerveld O.B.,
RA Nagaraj N., Chen N., Faessler R., Sonnenberg A.;
RT "PEAK1 Y635 phosphorylation regulates cell migration through association
RT with Tensin3 and integrins.";
RL J. Cell Biol. 221:0-0(2022).
RN [73] {ECO:0007744|PDB:3T9K}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 758-769 IN COMPLEX WITH ACAP1,
RP INTERACTION WITH ACAP1 AND ITGA5, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 760-ARG-ARG-761; 762-GLU--PHE-767 AND 768-LYS-GLU-769.
RX PubMed=22645133; DOI=10.1074/jbc.m112.378810;
RA Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F., Hsu V.W.;
RT "Mechanistic insights into regulated cargo binding by ACAP1 protein.";
RL J. Biol. Chem. 287:28675-28685(2012).
RN [74] {ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-465 IN COMPLEX WITH ANTIBODY;
RP ITGA5; RGD PEPTIDE; CALCIUM AND MAGNESIUM, DOMAIN, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-269 AND ASN-406, AND SUBUNIT.
RX PubMed=22451694; DOI=10.1083/jcb.201111077;
RA Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J.;
RT "Crystal structure of alpha5beta1 integrin ectodomain: atomic details of
RT the fibronectin receptor.";
RL J. Cell Biol. 197:131-140(2012).
RN [75] {ECO:0007744|PDB:4DX9}
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 784-798 IN COMPLEX WITH ITGB1BP1,
RP INTERACTION WITH ITGB1BP1, AND MUTAGENESIS OF THR-788; VAL-790; ASN-792 AND
RP TYR-795.
RX PubMed=23317506; DOI=10.1016/j.molcel.2012.12.005;
RA Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.;
RT "Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin
RT activation.";
RL Mol. Cell 49:719-729(2013).
RN [76] {ECO:0007744|PDB:7NWL, ECO:0007744|PDB:7NXD}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 21-798 IN COMPLEX WITH
RP FN1 (FN7-10 DOMAINS); ITGA5; ANTIBODY; CALCIUM AND MAGNESIUM, FUNCTION,
RP SUBUNIT, TISSUE SPECIFICITY, DOMAIN, GLYCOSYLATION AT ASN-269; ASN-363;
RP ASN-406; ASN-417 AND ASN-481, AND DISULFIDE BONDS.
RX PubMed=33962943; DOI=10.1126/sciadv.abe9716;
RA Schumacher S., Dedden D., Nunez R.V., Matoba K., Takagi J.,
RA Biertuempfel C., Mizuno N.;
RT "Structural insights into integrin alpha5beta1 opening by fibronectin
RT ligand.";
RL Sci. Adv. 7:0-0(2021).
CC -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and
CC alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1
CC and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-
CC E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-
CC 4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-
CC 11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-
CC 4/beta-1 recognizes one or more domains within the alternatively
CC spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1
CC is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1,
CC alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin
CC alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in
CC sperm-egg fusion (By similarity). Integrin alpha-4/beta-1 is a receptor
CC for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-
CC 9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It
CC recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-
CC 3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-
CC 3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of
CC endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for
CC vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide
CC array of ligands. When associated with alpha-7 integrin, regulates cell
CC adhesion and laminin matrix deposition. Involved in promoting
CC endothelial cell motility and angiogenesis. Involved in osteoblast
CC compaction through the fibronectin fibrillogenesis cell-mediated matrix
CC assembly process and the formation of mineralized bone nodules. May be
CC involved in up-regulation of the activity of kinases such as PKC via
CC binding to KRT1. Together with KRT1 and RACK1, serves as a platform for
CC SRC activation or inactivation. Plays a mechanistic adhesive role
CC during telophase, required for the successful completion of
CC cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP
CC (seprase) at invadopodia plasma membranes in a collagen-dependent
CC manner and hence may participate in the adhesion, formation of
CC invadopodia and matrix degradation processes, promoting cell invasion.
CC ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor
CC in CX3CR1-dependent fractalkine signaling (PubMed:23125415,
CC PubMed:24789099). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a
CC site (site 2) which is distinct from the classical ligand-binding site
CC (site 1) and this induces integrin conformational changes and enhanced
CC ligand binding to site 1 (PubMed:18635536, PubMed:25398877).
CC ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-
CC D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881).
CC ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-
CC dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a
CC receptor for IL1B and binding is essential for IL1B signaling
CC (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is
CC required for CD40/CD40LG signaling (PubMed:31331973). Plays an
CC important role in myoblast differentiation and fusion during skeletal
CC myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in
CC SVEP1/polydom-mediated myoblast cell adhesion (By similarity).
CC Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type
CC voltage-gated channel Ca(2+) influx and ROCK-mediated calcium
CC sensitivity in vascular smooth muscle cells via their interaction with
CC SVEP1, thereby inhibit vasocontraction (PubMed:35802072).
CC {ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055,
CC ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654,
CC ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16256741,
CC ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18635536,
CC ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666,
CC ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:23125415,
CC ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877,
CC ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:31331973,
CC ECO:0000269|PubMed:33962943, ECO:0000269|PubMed:35802072,
CC ECO:0000269|PubMed:7523423}.
CC -!- FUNCTION: [Isoform 2]: Interferes with isoform 1 resulting in a
CC dominant negative effect on cell adhesion and migration (in vitro).
CC {ECO:0000305|PubMed:2249781}.
CC -!- FUNCTION: [Isoform 5]: Isoform 5 displaces isoform 1 in striated
CC muscles. {ECO:0000250|UniProtKB:P09055}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor
CC for Human echoviruses 1 and 8. {ECO:0000269|PubMed:8411387}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for
CC Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:20660204}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr
CC virus/HHV-4. {ECO:0000269|PubMed:17945327}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor
CC for Human parvovirus B19. {ECO:0000269|PubMed:12907437}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor
CC for Human rotavirus. {ECO:0000269|PubMed:12941907}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Mammalian
CC reovirus. {ECO:0000269|PubMed:16501085}.
CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, integrin
CC ITGA5:ITGB1 binding to extracellular viral Tat protein seems to enhance
CC angiogenesis in Kaposi's sarcoma lesions.
CC {ECO:0000269|PubMed:10397733}.
CC -!- FUNCTION: (Microbial infection) Interacts with CotH proteins expressed
CC by fungi of the order mucorales, the causative agent of mucormycosis,
CC which plays an important role in epithelial cell invasion by the fungi
CC (PubMed:32487760). Integrin ITGA3:ITGB1 may act as a receptor for
CC R.delemar CotH7 in alveolar epithelial cells, which may be an early
CC step in pulmonary mucormycosis disease progression (PubMed:32487760).
CC {ECO:0000269|PubMed:32487760}.
CC -!- FUNCTION: (Microbial infection) May serve as a receptor for adhesin A
CC (nadA) of N.meningitidis. {ECO:0000305|PubMed:21471204}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:33962943).
CC Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4,
CC alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
CC alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes
CC place in oocytes and is involved in sperm-egg fusion (By similarity).
CC Interacts with seprase FAP (seprase); the interaction occurs at the
CC cell surface of invadopodia membrane in a collagen-dependent manner.
CC Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with
CC alpha-5. Interacts with FGR and HCK. Interacts (via the cytoplasmic
CC region) with RAB25 (via the hypervariable C-terminal region). Interacts
CC with RAB21. Interacts with KRT1 in the presence of RACK1 and SRC.
CC Interacts with JAML; integrin alpha-4/beta-1 may regulate leukocyte to
CC endothelial cells adhesion by controlling JAML homodimerization.
CC Interacts with FLNA, FLNB and RANBP9. Interacts with MYO10. Interacts
CC with DAB2. Interacts with FERMT2; the interaction is inhibited in
CC presence of ITGB1BP1. Interacts with ITGB1BP1 (via C-terminal region);
CC the interaction is a prerequisite for focal adhesion disassembly.
CC Interacts with TLN1; the interaction is prevented by competitive
CC binding of ITGB1BP1. Interacts with ACAP1; required for ITGB1
CC recycling. Interacts with ASAP3. Interacts with EMP2; the interaction
CC may be direct or indirect and ITGB1 has a heterodimer form (By
CC similarity). ITGA5:ITGB1 interacts with CCN3. ITGA4:ITGB1 is found in a
CC ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415). ITGA5:ITGB1
CC interacts with FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1
CC interacts with IL1B (PubMed:29030430). ITGA4:ITGB1 interacts with MDK;
CC this interaction mediates MDK-induced osteoblast cells migration
CC through PXN phosphorylation (PubMed:15466886). ITGA6:ITGB1 interacts
CC with MDK; this interaction mediates MDK-induced neurite-outgrowth
CC (PubMed:15466886). ITGA5:ITGB1 interacts with ACE2 (PubMed:33102950).
CC Interacts with TMEM182 and LAMB1 (By similarity). Interacts with tensin
CC TNS3; TNS3 also interacts with PEAK1, thus acting as an adapter
CC molecule to bridge the association of PEAK1 with ITGB1
CC (PubMed:35687021). Interacts with tensin TNS4; the interaction
CC displaces tensin TNS3 from the ITGB1 cytoplasmic tail and promotes
CC ITGB1 stability (PubMed:17643115, PubMed:24814316). Integrin
CC ITGA9:ITGB1 interacts with SPP1/OPN (via N-terminus) (By similarity).
CC Integrin ITGA9:ITGB1 interacts with TNC/TNFN3 (via the 3rd Fibronectin
CC type-III domain) (PubMed:22654117). Integrins ITGA4:ITGB1 and
CC ITGA9:ITGB1 interact with SVEP1 (via Sushi domain 21); thereby inhibit
CC Ca(2+) intracellular signaling and as a result repress vasocontraction
CC (PubMed:35802072). {ECO:0000250|UniProtKB:P07228,
CC ECO:0000250|UniProtKB:P09055, ECO:0000269|PubMed:10455171,
CC ECO:0000269|PubMed:10613898, ECO:0000269|PubMed:11741838,
CC ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:11807099,
CC ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:12695522,
CC ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:14722085,
CC ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:15181153,
CC ECO:0000269|PubMed:15276642, ECO:0000269|PubMed:15466886,
CC ECO:0000269|PubMed:16076904, ECO:0000269|PubMed:16256741,
CC ECO:0000269|PubMed:16754960, ECO:0000269|PubMed:17158881,
CC ECO:0000269|PubMed:17643115, ECO:0000269|PubMed:17925226,
CC ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21325030,
CC ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:22027826,
CC ECO:0000269|PubMed:22451694, ECO:0000269|PubMed:22645133,
CC ECO:0000269|PubMed:22654117, ECO:0000269|PubMed:23125415,
CC ECO:0000269|PubMed:23317506, ECO:0000269|PubMed:24814316,
CC ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:33102950,
CC ECO:0000269|PubMed:33962943, ECO:0000269|PubMed:35687021,
CC ECO:0000269|PubMed:35802072, ECO:0000269|PubMed:9501082}.
CC -!- SUBUNIT: [Isoform 5]: Interacts with ACE2 (PubMed:15276642). Interacts
CC with alpha-7B in cardiomyocytes of adult heart and alpha-7A and alpha-
CC 7B in adult skeletal muscle (By similarity).
CC {ECO:0000250|UniProtKB:P09055, ECO:0000269|PubMed:15276642}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with the C-terminal region of FLNC.
CC {ECO:0000269|PubMed:16076904}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
CC human echoviruses 1 and 8 capsid proteins.
CC {ECO:0000269|PubMed:8411387}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 envelope glycoprotein B/gB.
CC {ECO:0000269|PubMed:20660204}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus/HHV-4
CC gB protein. {ECO:0000269|PubMed:17945327}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
CC human parvovirus B19 capsid protein. {ECO:0000269|PubMed:12907437}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA2:ITGB1 interacts with
CC human rotavirus VP4 protein. {ECO:0000269|PubMed:12941907}.
CC -!- SUBUNIT: (Microbial infection) Interacts with mammalian reovirus capsid
CC proteins. {ECO:0000269|PubMed:16501085}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with HIV-
CC 1 Tat. {ECO:0000269|PubMed:10397733}.
CC -!- SUBUNIT: (Microbial infection) ITGA5:ITGB1 interacts with SARS
CC coronavirus-2/SARS-CoV-2 spike protein. {ECO:0000269|PubMed:33102950}.
CC -!- SUBUNIT: (Microbial infection) Interacts with R.delemar CotH7 on the
CC surface of alveolar epithelial cells. {ECO:0000269|PubMed:32487760}.
CC -!- SUBUNIT: (Microbial infection) Interacts with N.meningitidis serogroup
CC B adhesin A (nadA). {ECO:0000269|PubMed:21471204}.
CC -!- INTERACTION:
CC P05556; P12821-3: ACE; NbExp=2; IntAct=EBI-703066, EBI-25497695;
CC P05556; Q9BYF1: ACE2; NbExp=4; IntAct=EBI-703066, EBI-7730807;
CC P05556; P78536: ADAM17; NbExp=2; IntAct=EBI-703066, EBI-78188;
CC P05556; Q9BY76: ANGPTL4; NbExp=2; IntAct=EBI-703066, EBI-2968146;
CC P05556; P05067: APP; NbExp=3; IntAct=EBI-703066, EBI-77613;
CC P05556; P46109: CRKL; NbExp=2; IntAct=EBI-703066, EBI-910;
CC P05556; P32927: CSF2RB; NbExp=5; IntAct=EBI-703066, EBI-1809771;
CC P05556; P78423: CX3CL1; NbExp=2; IntAct=EBI-703066, EBI-15188013;
CC P05556; P17813: ENG; NbExp=3; IntAct=EBI-703066, EBI-2834630;
CC P05556; P21333: FLNA; NbExp=5; IntAct=EBI-703066, EBI-350432;
CC P05556; P08069: IGF1R; NbExp=2; IntAct=EBI-703066, EBI-475981;
CC P05556; P17301: ITGA2; NbExp=5; IntAct=EBI-703066, EBI-702960;
CC P05556; P13612: ITGA4; NbExp=4; IntAct=EBI-703066, EBI-703044;
CC P05556; P08648: ITGA5; NbExp=7; IntAct=EBI-703066, EBI-1382311;
CC P05556; P07948: LYN; NbExp=4; IntAct=EBI-703066, EBI-79452;
CC P05556; Q13387-4: MAPK8IP2; NbExp=3; IntAct=EBI-703066, EBI-12345753;
CC P05556; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-703066, EBI-9090282;
CC P05556; P18031: PTPN1; NbExp=2; IntAct=EBI-703066, EBI-968788;
CC P05556; Q9Y490: TLN1; NbExp=2; IntAct=EBI-703066, EBI-2462036;
CC P05556; O60784-2: TOM1; NbExp=3; IntAct=EBI-703066, EBI-12117154;
CC P05556; P03192: BMRF2; Xeno; NbExp=2; IntAct=EBI-703066, EBI-9348955;
CC P05556; P35282: Rab21; Xeno; NbExp=3; IntAct=EBI-703066, EBI-1993555;
CC P05556; P26039: Tln1; Xeno; NbExp=2; IntAct=EBI-703066, EBI-1039593;
CC P05556-1; P21333: FLNA; NbExp=2; IntAct=EBI-6082935, EBI-350432;
CC P05556-5; Q71LX4: Tln2; Xeno; NbExp=3; IntAct=EBI-7208579, EBI-2255655;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158881,
CC ECO:0000269|PubMed:32487760, ECO:0000269|PubMed:35687021,
CC ECO:0000303|PubMed:10455171}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell projection, invadopodium membrane
CC {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:11919189}; Single-pass
CC type I membrane protein {ECO:0000255}. Recycling endosome
CC {ECO:0000269|PubMed:16256741}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Cleavage furrow
CC {ECO:0000269|PubMed:17956333}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:11919189}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:35687021}. Note=Highly
CC enriched in stage I melanosomes. Located on plasma membrane of
CC neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase
CC and metaphase, localizes diffusely at the membrane and in a few
CC intracellular vesicles. In early telophase, detected mainly on the
CC matrix-facing side of the cells. By mid-telophase, concentrated to the
CC ingressing cleavage furrow, mainly to the basal side of the furrow. In
CC late telophase, concentrated to the extending protrusions formed at the
CC opposite ends of the spreading daughter cells, in vesicles at the base
CC of the lamellipodia formed by the separating daughter cells.
CC Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the
CC edge or peripheral ruffles and lamellipodia during the early stages of
CC cell spreading on fibronectin or collagen. Translocates from peripheral
CC focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent
CC manner. Enriched preferentially at invadopodia, cell membrane
CC protrusions that correspond to sites of cell invasion, in a collagen-
CC dependent manner. Localized at plasma and ruffle membranes in a
CC collagen-independent manner. {ECO:0000269|PubMed:10455171}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Note=Does not localize to focal
CC adhesions. {ECO:0000269|PubMed:10455171}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P09055}. Cell junction
CC {ECO:0000250|UniProtKB:P09055}. Note=In cardiac muscle, found in
CC costameres and intercalated disks. {ECO:0000250|UniProtKB:P09055}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Beta-1A;
CC IsoId=P05556-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-1B;
CC IsoId=P05556-2; Sequence=VSP_002741;
CC Name=3; Synonyms=Beta-1C;
CC IsoId=P05556-3; Sequence=VSP_002742;
CC Name=4; Synonyms=Beta-1C-2;
CC IsoId=P05556-4; Sequence=VSP_002743;
CC Name=5; Synonyms=Beta-1D;
CC IsoId=P05556-5; Sequence=VSP_002744;
CC -!- TISSUE SPECIFICITY: Expressed in vascular smooth muscle cells (at
CC protein level). {ECO:0000269|PubMed:35802072}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in placenta (at protein
CC level) (PubMed:33962943). Widely expressed, other isoforms are
CC generally coexpressed with a more restricted distribution
CC (PubMed:1551917, PubMed:7545396, PubMed:7681433).
CC {ECO:0000269|PubMed:1551917, ECO:0000269|PubMed:33962943,
CC ECO:0000269|PubMed:7545396, ECO:0000269|PubMed:7681433}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in skin, liver, skeletal
CC muscle, cardiac muscle, placenta, umbilical vein endothelial cells,
CC neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma
CC cells. {ECO:0000269|PubMed:2249781}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Together with isoform 4, is expressed
CC in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein
CC endothelial cells, fibroblast cells, embryonal kidney cells, platelets
CC and several blood cell lines. Expressed in non-proliferating and
CC differentiated prostate gland epithelial cells and in platelets, on the
CC surface of erythroleukemia cells and in various hematopoietic cell
CC lines. {ECO:0000269|PubMed:1551917, ECO:0000269|PubMed:9494094}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Together with isoform 3, is expressed
CC in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein
CC endothelial cells, fibroblast cells, embryonal kidney cells, platelets
CC and several blood cell lines. Rather than isoform 3, is selectively
CC expressed in peripheral T-cells. {ECO:0000269|PubMed:9494094}.
CC -!- TISSUE SPECIFICITY: [Isoform 5]: Expressed specifically in striated
CC muscle (skeletal and cardiac muscle). {ECO:0000269|PubMed:7544298,
CC ECO:0000269|PubMed:7545396}.
CC -!- INDUCTION: Induced in alveolar epithelial cells during exposure to the
CC fungus R.delemar, a causative agent of mucormycosis.
CC {ECO:0000269|PubMed:32487760}.
CC -!- DOMAIN: The VWFA domain (or beta I domain) contains three cation-
CC binding sites: the ligand-associated metal ion-binding site (LIMBS or
CC SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent
CC MIDAS site (ADMIDAS). This domain is also part of the ligand-binding
CC site. {ECO:0000269|PubMed:22451694, ECO:0000269|PubMed:33962943}.
CC -!- BIOTECHNOLOGY: Antibodies against integrin beta-1 ITGB1 protects
CC epithelial cells from invasion by the fungus R.delemar, a causative
CC agent of mucormycosis, and could thus potentially be used to treat
CC mucormycosis disease (PubMed:32487760). Antibodies against the protein
CC also protect a neutropenic mouse model against mucormycosis
CC (PubMed:32487760). {ECO:0000269|PubMed:32487760}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97649.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD29 entry;
CC URL="https://en.wikipedia.org/wiki/CD29";
CC ---------------------------------------------------------------------------
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DR EMBL; X07979; CAA30790.1; -; mRNA.
DR EMBL; AK291697; BAF84386.1; -; mRNA.
DR EMBL; BX537407; CAD97649.1; ALT_INIT; mRNA.
DR EMBL; AL365203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW85948.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85949.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85950.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85951.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85952.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85953.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85954.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85955.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85957.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85958.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85959.1; -; Genomic_DNA.
DR EMBL; BC020057; AAH20057.1; -; mRNA.
DR EMBL; BC113901; AAI13902.1; -; mRNA.
DR EMBL; U33879; AAA79832.1; -; Genomic_DNA.
DR EMBL; U33880; AAA79833.1; -; Genomic_DNA.
DR EMBL; U33879; AAA79833.1; JOINED; Genomic_DNA.
DR EMBL; U33882; AAA79834.1; -; Genomic_DNA.
DR EMBL; U33879; AAA79834.1; JOINED; Genomic_DNA.
DR EMBL; U33881; AAA79834.1; JOINED; Genomic_DNA.
DR EMBL; U33882; AAA79835.1; -; Genomic_DNA.
DR EMBL; U33879; AAA79835.1; JOINED; Genomic_DNA.
DR EMBL; M34189; AAA59182.1; -; mRNA.
DR EMBL; M84237; AAA74402.1; -; mRNA.
DR EMBL; M84237; AAA74403.1; -; mRNA.
DR EMBL; U28252; AAA81366.1; -; mRNA.
DR CCDS; CCDS7174.1; -. [P05556-1]
DR PIR; B27079; B27079.
DR RefSeq; NP_002202.2; NM_002211.3. [P05556-1]
DR RefSeq; NP_391988.1; NM_033668.2. [P05556-5]
DR RefSeq; NP_596867.1; NM_133376.2. [P05556-1]
DR PDB; 3G9W; X-ray; 2.16 A; C/D=752-785.
DR PDB; 3T9K; X-ray; 2.30 A; A/B=758-769.
DR PDB; 3VI3; X-ray; 2.90 A; B/D=21-465.
DR PDB; 3VI4; X-ray; 2.90 A; B/D=21-465.
DR PDB; 4DX9; X-ray; 3.00 A; 6/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z=784-798.
DR PDB; 4WJK; X-ray; 1.85 A; B=21-465.
DR PDB; 4WK0; X-ray; 1.78 A; B=21-465.
DR PDB; 4WK2; X-ray; 2.50 A; B=21-465.
DR PDB; 4WK4; X-ray; 2.50 A; B=21-465.
DR PDB; 7CEB; X-ray; 2.89 A; B=21-465.
DR PDB; 7CEC; EM; 3.90 A; B=21-465.
DR PDB; 7NWL; EM; 3.10 A; B=21-798.
DR PDB; 7NXD; EM; 4.60 A; B=21-798.
DR PDBsum; 3G9W; -.
DR PDBsum; 3T9K; -.
DR PDBsum; 3VI3; -.
DR PDBsum; 3VI4; -.
DR PDBsum; 4DX9; -.
DR PDBsum; 4WJK; -.
DR PDBsum; 4WK0; -.
DR PDBsum; 4WK2; -.
DR PDBsum; 4WK4; -.
DR PDBsum; 7CEB; -.
DR PDBsum; 7CEC; -.
DR PDBsum; 7NWL; -.
DR PDBsum; 7NXD; -.
DR AlphaFoldDB; P05556; -.
DR BMRB; P05556; -.
DR EMDB; EMD-12634; -.
DR EMDB; EMD-12637; -.
DR EMDB; EMD-30342; -.
DR SMR; P05556; -.
DR BioGRID; 109894; 329.
DR ComplexPortal; CPX-1794; Integrin alpha5-beta1 complex.
DR ComplexPortal; CPX-1797; Integrin alpha3-beta1 complex.
DR ComplexPortal; CPX-1798; Integrin alpha1-beta1 complex.
DR ComplexPortal; CPX-1801; Integrin alpha2-beta1 complex.
DR ComplexPortal; CPX-1802; Integrin alpha4-beta1 complex.
DR ComplexPortal; CPX-1803; Integrin alpha6-beta1 complex.
DR ComplexPortal; CPX-1804; Integrin alpha7-beta1 complex.
DR ComplexPortal; CPX-1815; Integrin alpha8-beta1 complex.
DR ComplexPortal; CPX-1816; Integrin alpha9-beta1 complex.
DR ComplexPortal; CPX-1817; Integrin alpha10-beta1 complex.
DR ComplexPortal; CPX-1818; Integrin alpha11-beta1 complex.
DR ComplexPortal; CPX-1819; Integrin alphav-beta1 complex.
DR CORUM; P05556; -.
DR DIP; DIP-312N; -.
DR ELM; P05556; -.
DR IntAct; P05556; 130.
DR MINT; P05556; -.
DR STRING; 9606.ENSP00000379350; -.
DR BindingDB; P05556; -.
DR ChEMBL; CHEMBL1905; -.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR DrugBank; DB15791; MK-0668.
DR DrugBank; DB16515; PLN-74809.
DR DrugCentral; P05556; -.
DR GuidetoPHARMACOLOGY; 2455; -.
DR TCDB; 9.B.87.1.8; the selenoprotein p receptor (selp-receptor) family.
DR GlyConnect; 1414; 44 N-Linked glycans (7 sites).
DR GlyConnect; 283; 35 N-Linked glycans.
DR GlyCosmos; P05556; 13 sites, 92 glycans.
DR GlyGen; P05556; 21 sites, 91 N-linked glycans (8 sites), 2 O-linked glycans (8 sites).
DR iPTMnet; P05556; -.
DR PhosphoSitePlus; P05556; -.
DR SwissPalm; P05556; -.
DR BioMuta; ITGB1; -.
DR DMDM; 218563324; -.
DR CPTAC; CPTAC-229; -.
DR CPTAC; CPTAC-230; -.
DR EPD; P05556; -.
DR jPOST; P05556; -.
DR MassIVE; P05556; -.
DR MaxQB; P05556; -.
DR PaxDb; 9606-ENSP00000379350; -.
DR PeptideAtlas; P05556; -.
DR ProteomicsDB; 51850; -. [P05556-1]
DR ProteomicsDB; 51851; -. [P05556-2]
DR ProteomicsDB; 51852; -. [P05556-3]
DR ProteomicsDB; 51853; -. [P05556-4]
DR ProteomicsDB; 51854; -. [P05556-5]
DR Pumba; P05556; -.
DR ABCD; P05556; 59 sequenced antibodies.
DR Antibodypedia; 3126; 3334 antibodies from 52 providers.
DR DNASU; 3688; -.
DR Ensembl; ENST00000302278.8; ENSP00000303351.3; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000396033.6; ENSP00000379350.2; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000417122.7; ENSP00000404546.3; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000423113.6; ENSP00000388694.1; ENSG00000150093.20. [P05556-5]
DR Ensembl; ENST00000437302.6; ENSP00000398029.2; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000676460.1; ENSP00000504641.1; ENSG00000150093.20. [P05556-2]
DR Ensembl; ENST00000676659.1; ENSP00000502979.1; ENSG00000150093.20. [P05556-4]
DR Ensembl; ENST00000677310.1; ENSP00000504508.1; ENSG00000150093.20. [P05556-3]
DR Ensembl; ENST00000677999.1; ENSP00000503546.1; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000678701.1; ENSP00000504205.1; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000678766.1; ENSP00000503538.1; ENSG00000150093.20. [P05556-3]
DR Ensembl; ENST00000678943.1; ENSP00000503916.1; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000678952.1; ENSP00000504444.1; ENSG00000150093.20. [P05556-1]
DR Ensembl; ENST00000678989.1; ENSP00000502882.1; ENSG00000150093.20. [P05556-1]
DR GeneID; 3688; -.
DR KEGG; hsa:3688; -.
DR MANE-Select; ENST00000302278.8; ENSP00000303351.3; NM_002211.4; NP_002202.2.
DR UCSC; uc001iwr.5; human. [P05556-1]
DR AGR; HGNC:6153; -.
DR CTD; 3688; -.
DR DisGeNET; 3688; -.
DR GeneCards; ITGB1; -.
DR HGNC; HGNC:6153; ITGB1.
DR HPA; ENSG00000150093; Low tissue specificity.
DR MIM; 135630; gene.
DR neXtProt; NX_P05556; -.
DR OpenTargets; ENSG00000150093; -.
DR PharmGKB; PA29953; -.
DR VEuPathDB; HostDB:ENSG00000150093; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_2_1_1; -.
DR InParanoid; P05556; -.
DR OMA; NCVCGAC; -.
DR OrthoDB; 5475862at2759; -.
DR PhylomeDB; P05556; -.
DR TreeFam; TF105392; -.
DR PathwayCommons; P05556; -.
DR Reactome; R-HSA-1566948; Elastic fibre formation.
DR Reactome; R-HSA-1566977; Fibronectin matrix formation.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8875513; MET interacts with TNS proteins.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SABIO-RK; P05556; -.
DR SignaLink; P05556; -.
DR SIGNOR; P05556; -.
DR BioGRID-ORCS; 3688; 141 hits in 1186 CRISPR screens.
DR ChiTaRS; ITGB1; human.
DR EvolutionaryTrace; P05556; -.
DR GeneWiki; CD29; -.
DR GenomeRNAi; 3688; -.
DR Pharos; P05556; Tclin.
DR PRO; PR:P05556; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P05556; Protein.
DR Bgee; ENSG00000150093; Expressed in visceral pleura and 212 other cell types or tissues.
DR ExpressionAtlas; P05556; baseline and differential.
DR Genevisible; P05556; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0150053; C:cerebellar climbing fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; ISS:ARUK-UCL.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; IDA:UniProtKB.
DR GO; GO:0034680; C:integrin alpha10-beta1 complex; IDA:UniProtKB.
DR GO; GO:0034681; C:integrin alpha11-beta1 complex; IDA:UniProtKB.
DR GO; GO:0034666; C:integrin alpha2-beta1 complex; IDA:UniProtKB.
DR GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:UniProtKB.
DR GO; GO:0034668; C:integrin alpha4-beta1 complex; TAS:ARUK-UCL.
DR GO; GO:0034674; C:integrin alpha5-beta1 complex; IDA:UniProtKB.
DR GO; GO:0034677; C:integrin alpha7-beta1 complex; IEA:Ensembl.
DR GO; GO:0034678; C:integrin alpha8-beta1 complex; TAS:BHF-UCL.
DR GO; GO:0034679; C:integrin alpha9-beta1 complex; ISS:UniProtKB.
DR GO; GO:0034682; C:integrin alphav-beta1 complex; IPI:ComplexPortal.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; TAS:HGNC-UCL.
DR GO; GO:0032587; C:ruffle membrane; NAS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:UniProtKB.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
DR GO; GO:0001968; F:fibronectin binding; IDA:ARUK-UCL.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0098640; F:integrin binding involved in cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IC:BHF-UCL.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IGI:MGI.
DR GO; GO:0060912; P:cardiac cell fate specification; IEA:Ensembl.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IEA:Ensembl.
DR GO; GO:0023035; P:CD40 signaling pathway; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; TAS:HGNC-UCL.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0030030; P:cell projection organization; ISS:ARUK-UCL.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEP:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ARUK-UCL.
DR GO; GO:0021943; P:formation of radial glial scaffolds; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:ARUK-UCL.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0048626; P:myoblast fate specification; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; ISS:ARUK-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:ARUK-UCL.
DR GO; GO:0051951; P:positive regulation of glutamate uptake involved in transmission of nerve impulse; ISS:ARUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:BHF-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0090303; P:positive regulation of wound healing; IDA:ARUK-UCL.
DR GO; GO:0150103; P:reactive gliosis; ISS:ARUK-UCL.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0010710; P:regulation of collagen catabolic process; IDA:UniProtKB.
DR GO; GO:1901979; P:regulation of inward rectifier potassium channel activity; ISS:ARUK-UCL.
DR GO; GO:0150003; P:regulation of spontaneous synaptic transmission; ISS:ARUK-UCL.
DR GO; GO:1905806; P:regulation of synapse pruning; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; NAS:ComplexPortal.
DR DisProt; DP01748; -.
DR Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF28; INTEGRIN BETA-1; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium; Cell adhesion;
KW Cell junction; Cell membrane; Cell projection; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Endosome; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Integrin;
KW Isopeptide bond; Magnesium; Membrane; Metal-binding; Myogenesis;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..20
FT CHAIN 21..798
FT /note="Integrin beta-1"
FT /id="PRO_0000016334"
FT TOPO_DOM 21..728
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..76
FT /note="PSI"
FT /evidence="ECO:0000255"
FT DOMAIN 140..378
FT /note="VWFA"
FT /evidence="ECO:0000305|PubMed:22451694,
FT ECO:0000305|PubMed:33962943"
FT DOMAIN 439..501
FT /note="EGF-like 1"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DOMAIN 502..554
FT /note="EGF-like 2"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DOMAIN 555..591
FT /note="EGF-like 3"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DOMAIN 592..635
FT /note="EGF-like 4"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..213
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000269|PubMed:23125415"
FT REGION 295..314
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000269|PubMed:24789099"
FT REGION 383..465
FT /note="Interaction with TMEM182"
FT /evidence="ECO:0000250|UniProtKB:P07228"
FT REGION 762..767
FT /note="Signal for sorting from recycling endosomes;
FT interaction with ACAP1"
FT REGION 785..792
FT /note="Interaction with ITGB1BP1"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NXD"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0007744|PDB:3VI3"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0007744|PDB:3VI4"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:7NXD"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:7NXD"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NXD"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NXD"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NXD"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NXD"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NXD"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:7NXD"
FT MOD_RES 777
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 783
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 789
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 794
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NWL, ECO:0007744|PDB:7NXD"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NWL, ECO:0007744|PDB:7NXD"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NXD"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 27..45
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 35..464
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 38..64
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 48..75
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT DISULFID 207..213
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 261..301
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 401..415
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 435..462
FT /evidence="ECO:0000269|PubMed:22451694,
FT ECO:0000269|PubMed:33962943, ECO:0007744|PDB:3VI3,
FT ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 466..486
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 477..489
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 491..500
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 502..533
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 516..531
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 525..536
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 538..553
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 555..576
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 560..574
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 568..579
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 581..590
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 592..615
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 599..613
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 607..618
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 620..630
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 633..636
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 640..691
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 646..665
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 649..661
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT DISULFID 699..723
FT /evidence="ECO:0000269|PubMed:33962943,
FT ECO:0007744|PDB:7NXD"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 778..798
FT /note="GENPIYKSAVTTVVNPKYEGK -> VSYKTSKKQSGL (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002741"
FT VAR_SEQ 778..798
FT /note="GENPIYKSAVTTVVNPKYEGK -> SLSVAQPGVQWCDISSLQPLTSRFQQF
FT SCLSLPSTWDYRVKILFIRVP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_002742"
FT VAR_SEQ 778..798
FT /note="GENPIYKSAVTTVVNPKYEGK -> PGVQWCDISSLQPLTSRFQQFSCLSLP
FT STWDYRVKILFIRVP (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_002743"
FT VAR_SEQ 778..798
FT /note="GENPIYKSAVTTVVNPKYEGK -> QENPIYKSPINNFKNPNYGRKAGL
FT (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_002744"
FT MUTAGEN 760..761
FT /note="RR->AA: No effect on interaction with ACAP1."
FT /evidence="ECO:0000269|PubMed:22645133"
FT MUTAGEN 762..767
FT /note="EFAKFE->AAAAAA: Strongly reduces interaction with
FT ACAP1 and ability to recycle; does not affect
FT heterodimerization with ITGA5."
FT /evidence="ECO:0000269|PubMed:22645133"
FT MUTAGEN 762..763
FT /note="EF->AA: Slightly reduces interaction with ACAP1."
FT MUTAGEN 765
FT /note="K->A: Reduces interaction with ACAP1."
FT MUTAGEN 766..767
FT /note="FE->AA: Slightly reduces interaction with ACAP1."
FT MUTAGEN 768..769
FT /note="KE->AA: No effect on interaction with ACAP1."
FT /evidence="ECO:0000269|PubMed:22645133"
FT MUTAGEN 778
FT /note="G->Q: Loss of beta-1A interaction with FLNA and
FT FLNB."
FT /evidence="ECO:0000269|PubMed:11807098"
FT MUTAGEN 783
FT /note="Y->A: No effect on cell surface location but impairs
FT interaction with TNS3 and PEAK1."
FT /evidence="ECO:0000269|PubMed:35687021"
FT MUTAGEN 786..791
FT /note="AVTTVV->PINNFK: Does not interact with ITGB1BP1."
FT /evidence="ECO:0000269|PubMed:11807099"
FT MUTAGEN 786
FT /note="A->P: Loss of beta-1A interaction with FLNA and
FT FLNB."
FT /evidence="ECO:0000269|PubMed:11807098"
FT MUTAGEN 787
FT /note="V->T: Reduces interaction with ITGB1BP1, but not
FT with FERMT2 or TLN1. Inhibits fibronectin deposition and
FT mineralized bone nodules formation."
FT /evidence="ECO:0000269|PubMed:21768292"
FT MUTAGEN 788
FT /note="T->D: Strongly reduces ITGB1BP1 binding; when
FT associated with D-790."
FT /evidence="ECO:0000269|PubMed:23317506"
FT MUTAGEN 790
FT /note="V->D: Strongly reduces ITGB1BP1 binding; when
FT associated with D-788."
FT /evidence="ECO:0000269|PubMed:23317506"
FT MUTAGEN 792
FT /note="N->A: Strongly reduces ITGB1BP1 binding; when
FT associated with A-795."
FT /evidence="ECO:0000269|PubMed:23317506"
FT MUTAGEN 795
FT /note="Y->A: No effect on cell surface location but impairs
FT interaction with TNS3 and PEAK1. Strongly reduces ITGB1BP1
FT binding; when associated with A-792."
FT /evidence="ECO:0000269|PubMed:23317506,
FT ECO:0000269|PubMed:35687021"
FT CONFLICT 112
FT /note="T -> H (in Ref. 1; CAA30790)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> T (in Ref. 1; CAA30790)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..265
FT /note="CGSLI -> VWMLL (in Ref. 6; AAI13902)"
FT /evidence="ECO:0000305"
FT CONFLICT 385..386
FT /note="EN -> DG (in Ref. 6; AAI13902)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="E -> V (in Ref. 2; BAF84386)"
FT /evidence="ECO:0000305"
FT TURN 26..31
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7NWL"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7NWL"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:7NWL"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:7NWL"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 269..280
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:7NWL"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 319..328
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:4WK4"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4WJK"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 423..432
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:4WJK"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 752..769
FT /evidence="ECO:0007829|PDB:3G9W"
FT HELIX 770..772
FT /evidence="ECO:0007829|PDB:3G9W"
SQ SEQUENCE 798 AA; 88415 MW; DE35979C1625578C CRC64;
MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT
SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLKPED ITQIQPQQLV
LRLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TSNKCPKKDS DSFKIRPLGF TEEVEVILQY ICECECQSEG IPESPKCHEG
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE
ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT
CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW FYFTYSVNGN NEVMVHVVEN
PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK
//
