ITA5_HUMAN
ID ITA5_HUMAN Reviewed; 1049 AA.
AC P08648; Q96HA5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Integrin alpha-5 {ECO:0000305};
DE AltName: Full=CD49 antigen-like family member E;
DE AltName: Full=Fibronectin receptor subunit alpha;
DE AltName: Full=Integrin alpha-F;
DE AltName: Full=VLA-5;
DE AltName: CD_antigen=CD49e;
DE Contains:
DE RecName: Full=Integrin alpha-5 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-5 light chain;
DE Flags: Precursor;
GN Name=ITGA5 {ECO:0000312|HGNC:HGNC:6141}; Synonyms=FNRA;
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].
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].
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
RX PubMed=1834647; DOI=10.1016/s0021-9258(18)54959-0;
RA Birkenmeier T.M., McQuillan J.J., Boedeker E.D., Argraves W.S.,
RA Ruoslahti E., Dean D.C.;
RT "The alpha 5 beta 1 fibronectin receptor. Characterization of the alpha 5
RT gene promoter.";
RL J. Biol. Chem. 266:20544-20549(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-1049.
RX PubMed=2450560; DOI=10.1021/bi00399a021;
RA Fitzgerald L.A., Poncz M., Steiner B., Rall S.C., Bennett J.S.,
RA Phillips D.R.;
RT "Comparison of cDNA-derived protein sequences of the human fibronectin and
RT vitronectin receptor alpha-subunits and platelet glycoprotein IIb.";
RL Biochemistry 26:8158-8165(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 821-1049.
RX PubMed=2944883; DOI=10.1016/s0021-9258(18)69249-x;
RA Argraves W.S., Pytela R., Suzuki S., Millan J.L., Pierschbacher M.D.,
RA Ruoslahti E.;
RT "cDNA sequences from the alpha subunit of the fibronectin receptor predict
RT a transmembrane domain and a short cytoplasmic peptide.";
RL J. Biol. Chem. 261:12922-12924(1986).
RN [6]
RP PROTEIN SEQUENCE OF 42-55.
RX PubMed=3033641; DOI=10.1073/pnas.84.10.3239;
RA Takada Y., Strominger J.L., Hemler M.E.;
RT "The very late antigen family of heterodimers is part of a superfamily of
RT molecules involved in adhesion and embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3239-3243(1987).
RN [7]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=10397733;
RA Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S.,
RA Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.;
RT "The Tat protein of human immunodeficiency virus type-1 promotes 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 [8]
RP INTERACTION WITH NISCH.
RX PubMed=11912194; DOI=10.1074/jbc.m111838200;
RA Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.;
RT "Insulin receptor substrate 4 associates with the protein IRAS.";
RL J. Biol. Chem. 277:19439-19447(2002).
RN [9]
RP DISULFIDE BONDS.
RX PubMed=14596610; DOI=10.1021/bi034726u;
RA Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G., Wilkins J.A.;
RT "Mass spectrometric based mapping of the disulfide bonding patterns of
RT integrin alpha chains.";
RL Biochemistry 42:12950-12959(2003).
RN [10]
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 [11]
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 [12]
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 [13]
RP INTERACTION WITH COMP.
RX PubMed=16051604; DOI=10.1074/jbc.m504778200;
RA Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.;
RT "Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte
RT attachment through interaction with integrins.";
RL J. Biol. Chem. 280:32655-32661(2005).
RN [14]
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 [15]
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 [16]
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 [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-307; ASN-675 AND
RP ASN-773.
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 [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-307 AND ASN-773.
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 [19]
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 [20]
RP PROTEOLYTIC CLEAVAGE BY PCSK5.
RX PubMed=22740495; DOI=10.1093/humrep/des203;
RA Paule S., Aljofan M., Simon C., Rombauts L.J., Nie G.;
RT "Cleavage of endometrial alpha-integrins into their functional forms is
RT mediated by proprotein convertase 5/6.";
RL Hum. Reprod. 27:2766-2774(2012).
RN [21]
RP INTERACTION WITH CIB1.
RX PubMed=24011356; DOI=10.1021/bi400678y;
RA Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I., Tripathy A.,
RA Dokholyan N.V., Leisner T.M., Parise L.V.;
RT "Identification of novel integrin binding partners for calcium and integrin
RT binding protein 1 (CIB1): structural and thermodynamic basis of CIB1
RT promiscuity.";
RL Biochemistry 52:7082-7090(2013).
RN [22]
RP IDENTIFICATION BY 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP 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 [24]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN METAPNEUMOVIRUS
RP FUSION PROTEIN.
RX PubMed=24478423; DOI=10.1128/jvi.03491-13;
RA Wei Y., Zhang Y., Cai H., Mirza A.M., Iorio R.M., Peeples M.E.,
RA Niewiesk S., Li J.;
RT "Roles of the putative integrin-binding motif of the human metapneumovirus
RT fusion (f) protein in cell-cell fusion, viral infectivity, and
RT pathogenesis.";
RL J. Virol. 88:4338-4352(2014).
RN [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
RP INTERACTION WITH ANGPT2.
RX PubMed=32908006; DOI=10.1126/scitranslmed.aax8013;
RA Leppaenen V.M., Brouillard P., Korhonen E.A., Sipilae T., Jha S.K.,
RA Revencu N., Labarque V., Fastre E., Schloegel M., Ravoet M., Singer A.,
RA Luzzatto C., Angelone D., Crichiutti G., D'Elia A., Kuurne J., Elamaa H.,
RA Koh G.Y., Saharinen P., Vikkula M., Alitalo K.;
RT "Characterization of ANGPT2 mutations associated with primary lymphedema.";
RL Sci. Transl. Med. 12:0-0(2020).
RN [31] {ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 42-664 IN COMPLEX WITH ANTIBODY;
RP ITGB1 AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-84; ASN-182;
RP ASN-297; ASN-307; ASN-316 AND ASN-609, SUBSTRATE-BINDING SITES,
RP CALCIUM-BINDING SITES, 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).
CC -!- FUNCTION: Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for
CC fibronectin and fibrinogen. It recognizes the sequence R-G-D in its
CC ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is
CC distinct from the classical ligand-binding site (site 1) and this
CC induces integrin conformational changes and enhanced ligand binding to
CC site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a
CC receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell
CC adhesion to FBN1 (PubMed:12807887, PubMed:17158881). 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).
CC {ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:17158881,
CC ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:25398877,
CC ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:31331973}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor
CC for Human metapneumovirus. {ECO:0000269|PubMed:12907437}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor
CC for Human parvovirus B19. {ECO:0000269|PubMed:24478423}.
CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, the
CC interaction with extracellular viral Tat protein seems to enhance
CC angiogenesis in Kaposi's sarcoma lesions.
CC {ECO:0000269|PubMed:10397733}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond.
CC Alpha-5 associates with beta-1. Interacts with HPS5 and NISCH.
CC Interacts with RAB21 and COMP. Interacts with CIB1. ITGA5:ITGB1
CC interacts with CCN3. ITGA5:ITGB1 interacts with FBN1 (PubMed:12807887,
CC PubMed:17158881). ITGA5:ITGB1 interacts with IL1B (PubMed:29030430).
CC ITGA5:ITGB1 interacts with ACE2 (PubMed:33102950). Interacts with
CC ANGPT2 (PubMed:32908006). {ECO:0000269|PubMed:11912194,
CC ECO:0000269|PubMed:12695522, ECO:0000269|PubMed:12807887,
CC ECO:0000269|PubMed:16051604, ECO:0000269|PubMed:16754960,
CC ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:22451694,
CC ECO:0000269|PubMed:24011356, ECO:0000269|PubMed:29030430,
CC ECO:0000269|PubMed:32908006, ECO:0000269|PubMed:33102950}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
CC human metapneumovirus fusion protein. {ECO:0000269|PubMed:12907437}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB1 interacts with
CC human parvovirus B19 capsid proteins. {ECO:0000269|PubMed:24478423}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {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 -!- INTERACTION:
CC P08648; P17813: ENG; NbExp=4; IntAct=EBI-1382311, EBI-2834630;
CC P08648; P05556: ITGB1; NbExp=7; IntAct=EBI-1382311, EBI-703066;
CC P08648; O14786: NRP1; NbExp=2; IntAct=EBI-1382311, EBI-1187100;
CC P08648; Q9H0F6: SHARPIN; NbExp=4; IntAct=EBI-1382311, EBI-3942966;
CC P08648; P97333: Nrp1; Xeno; NbExp=3; IntAct=EBI-1382311, EBI-1555129;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}. Cell
CC surface {ECO:0000269|PubMed:17158881}.
CC -!- PTM: Proteolytic cleavage by PCSK5 mediates activation of the
CC precursor. {ECO:0000269|PubMed:22740495}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; X06256; CAA29601.1; -; mRNA.
DR EMBL; BC008786; AAH08786.1; -; mRNA.
DR EMBL; M13918; AAA52467.1; ALT_SEQ; mRNA.
DR CCDS; CCDS8880.1; -.
DR PIR; A27079; A27079.
DR RefSeq; NP_002196.4; NM_002205.4.
DR PDB; 3VI3; X-ray; 2.90 A; A/C=42-664.
DR PDB; 3VI4; X-ray; 2.90 A; A/C=42-664.
DR PDB; 4WJK; X-ray; 1.85 A; A=42-491.
DR PDB; 4WK0; X-ray; 1.78 A; A=42-491.
DR PDB; 4WK2; X-ray; 2.50 A; A=42-491.
DR PDB; 4WK4; X-ray; 2.50 A; A=42-491.
DR PDB; 7NWL; EM; 3.10 A; A=42-1049.
DR PDB; 7NXD; EM; 4.60 A; A=42-1049.
DR PDBsum; 3VI3; -.
DR PDBsum; 3VI4; -.
DR PDBsum; 4WJK; -.
DR PDBsum; 4WK0; -.
DR PDBsum; 4WK2; -.
DR PDBsum; 4WK4; -.
DR PDBsum; 7NWL; -.
DR PDBsum; 7NXD; -.
DR AlphaFoldDB; P08648; -.
DR SMR; P08648; -.
DR BioGRID; 109884; 115.
DR ComplexPortal; CPX-1794; Integrin alpha5-beta1 complex.
DR CORUM; P08648; -.
DR DIP; DIP-40037N; -.
DR ELM; P08648; -.
DR IntAct; P08648; 32.
DR MINT; P08648; -.
DR STRING; 9606.ENSP00000293379; -.
DR BindingDB; P08648; -.
DR ChEMBL; CHEMBL3955; -.
DR DrugBank; DB02709; Resveratrol.
DR GuidetoPHARMACOLOGY; 2444; -.
DR GlyConnect; 1407; 21 N-Linked glycans (6 sites).
DR GlyConnect; 283; 35 N-Linked glycans.
DR GlyGen; P08648; 16 sites, 75 N-linked glycans (7 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P08648; -.
DR PhosphoSitePlus; P08648; -.
DR SwissPalm; P08648; -.
DR BioMuta; ITGA5; -.
DR DMDM; 23831237; -.
DR EPD; P08648; -.
DR jPOST; P08648; -.
DR MassIVE; P08648; -.
DR MaxQB; P08648; -.
DR PaxDb; P08648; -.
DR PeptideAtlas; P08648; -.
DR PRIDE; P08648; -.
DR ProteomicsDB; 52147; -.
DR TopDownProteomics; P08648; -.
DR ABCD; P08648; 10 sequenced antibodies.
DR Antibodypedia; 1221; 1177 antibodies from 47 providers.
DR DNASU; 3678; -.
DR Ensembl; ENST00000293379.9; ENSP00000293379.4; ENSG00000161638.11.
DR GeneID; 3678; -.
DR KEGG; hsa:3678; -.
DR MANE-Select; ENST00000293379.9; ENSP00000293379.4; NM_002205.5; NP_002196.4.
DR UCSC; uc001sga.4; human.
DR CTD; 3678; -.
DR DisGeNET; 3678; -.
DR GeneCards; ITGA5; -.
DR HGNC; HGNC:6141; ITGA5.
DR HPA; ENSG00000161638; Tissue enhanced (smooth muscle, urinary bladder).
DR MIM; 135620; gene.
DR neXtProt; NX_P08648; -.
DR OpenTargets; ENSG00000161638; -.
DR PharmGKB; PA29941; -.
DR VEuPathDB; HostDB:ENSG00000161638; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000158061; -.
DR HOGENOM; CLU_004111_4_0_1; -.
DR InParanoid; P08648; -.
DR OMA; KPPLYQP; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; P08648; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; P08648; -.
DR Reactome; R-HSA-1566948; Elastic fibre formation.
DR Reactome; R-HSA-1566977; Fibronectin matrix formation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-8941332; RUNX2 regulates genes involved in cell migration.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR SignaLink; P08648; -.
DR SIGNOR; P08648; -.
DR BioGRID-ORCS; 3678; 23 hits in 1077 CRISPR screens.
DR ChiTaRS; ITGA5; human.
DR GeneWiki; ITGA5; -.
DR GenomeRNAi; 3678; -.
DR Pharos; P08648; Tbio.
DR PRO; PR:P08648; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P08648; protein.
DR Bgee; ENSG00000161638; Expressed in tibial artery and 185 other tissues.
DR ExpressionAtlas; P08648; baseline and differential.
DR Genevisible; P08648; HS.
DR GO; GO:0071062; C:alphav-beta3 integrin-vitronectin complex; TAS:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0034674; C:integrin alpha5-beta1 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; TAS:HGNC-UCL.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; TAS:BHF-UCL.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; TAS:BHF-UCL.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
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:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEP:BHF-UCL.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell junction;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Integrin; Membrane; Metal-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000269|PubMed:3033641"
FT CHAIN 42..1049
FT /note="Integrin alpha-5"
FT /id="PRO_0000016249"
FT CHAIN 42..894
FT /note="Integrin alpha-5 heavy chain"
FT /id="PRO_0000016250"
FT CHAIN 895..1049
FT /note="Integrin alpha-5 light chain"
FT /id="PRO_0000016251"
FT TOPO_DOM 42..995
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1022..1049
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 43..108
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 128..188
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 192..245
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 259..311
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 312..377
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 378..437
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 441..504
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 877..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1028
FT /note="Interaction with HPS5"
FT MOTIF 1024..1028
FT /note="GFFKR motif"
FT BINDING 262
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /ligand_part_note="Arg of R-G-D sequence recognized in
FT fibronectin and fibrinogen"
FT BINDING 269
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /ligand_part_note="Arg of R-G-D sequence recognized in
FT fibronectin and fibrinogen"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:3VI3"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:3VI3"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22451694"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22451694"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:22451694"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:22451694"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22451694"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22451694"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..108
FT DISULFID 156..176
FT DISULFID 192..205
FT DISULFID 513..522
FT DISULFID 528..584
FT DISULFID 645..651
FT DISULFID 718..731
FT DISULFID 869..921
FT /note="Interchain (between heavy and light chains)"
FT DISULFID 911..916
FT VARIANT 585
FT /note="R -> I (in dbSNP:rs12318746)"
FT /id="VAR_049631"
FT CONFLICT 26
FT /note="L -> V (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="L -> V (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 56..61
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4WJK"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4WK2"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:7NWL"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 198..204
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4WK4"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 294..300
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:4WK0"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:7NWL"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:4WK0"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:4WK0"
FT STRAND 492..503
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 522..532
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 538..548
FT /evidence="ECO:0007829|PDB:3VI3"
FT TURN 549..555
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:3VI3"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 566..577
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 583..591
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:7NWL"
FT STRAND 604..612
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:3VI3"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:7NWL"
FT STRAND 634..641
FT /evidence="ECO:0007829|PDB:3VI3"
SQ SEQUENCE 1049 AA; 114536 MW; 6B4D558D4F739CBA CRC64;
MGSRTPESPL HAVQLRWGPR RRPPLLPLLL LLLPPPPRVG GFNLDAEAPA VLSGPPGSFF
GFSVEFYRPG TDGVSVLVGA PKANTSQPGV LQGGAVYLCP WGASPTQCTP IEFDSKGSRL
LESSLSSSEG EEPVEYKSLQ WFGATVRAHG SSILACAPLY SWRTEKEPLS DPVGTCYLST
DNFTRILEYA PCRSDFSWAA GQGYCQGGFS AEFTKTGRVV LGGPGSYFWQ GQILSATQEQ
IAESYYPEYL INLVQGQLQT RQASSIYDDS YLGYSVAVGE FSGDDTEDFV AGVPKGNLTY
GYVTILNGSD IRSLYNFSGE QMASYFGYAV AATDVNGDGL DDLLVGAPLL MDRTPDGRPQ
EVGRVYVYLQ HPAGIEPTPT LTLTGHDEFG RFGSSLTPLG DLDQDGYNDV AIGAPFGGET
QQGVVFVFPG GPGGLGSKPS QVLQPLWAAS HTPDFFGSAL RGGRDLDGNG YPDLIVGSFG
VDKAVVYRGR PIVSASASLT IFPAMFNPEE RSCSLEGNPV ACINLSFCLN ASGKHVADSI
GFTVELQLDW QKQKGGVRRA LFLASRQATL TQTLLIQNGA REDCREMKIY LRNESEFRDK
LSPIHIALNF SLDPQAPVDS HGLRPALHYQ SKSRIEDKAQ ILLDCGEDNI CVPDLQLEVF
GEQNHVYLGD KNALNLTFHA QNVGEGGAYE AELRVTAPPE AEYSGLVRHP GNFSSLSCDY
FAVNQSRLLV CDLGNPMKAG ASLWGGLRFT VPHLRDTKKT IQFDFQILSK NLNNSQSDVV
SFRLSVEAQA QVTLNGVSKP EAVLFPVSDW HPRDQPQKEE DLGPAVHHVY ELINQGPSSI
SQGVLELSCP QALEGQQLLY VTRVTGLNCT TNHPINPKGL ELDPEGSLHH QQKREAPSRS
SASSGPQILK CPEAECFRLR CELGPLHQQE SQSLQLHFRV WAKTFLQREH QPFSLQCEAV
YKALKMPYRI LPRQLPQKER QVATAVQWTK AEGSYGVPLW IIILAILFGL LLLGLLIYIL
YKLGFFKRSL PYGTAMEKAQ LKPPATSDA
