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   27-MAR-2024, entry version 242.
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 HPS5.
RX   PubMed=10094488; DOI=10.1016/s0014-5793(99)00151-9;
RA   Wixler V., Laplantine E., Geerts D., Sonnenberg A., Petersohn D., Eckes B.,
RA   Paulsson M., Aumailley M.;
RT   "Identification of novel interaction partners for the conserved membrane
RT   proximal region of alpha-integrin cytoplasmic domains.";
RL   FEBS Lett. 445:351-355(1999).
RN   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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   [22]
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   [23]
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   [24]
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   [25]
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   [26]
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   [27]
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   [28]
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   [29]
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   [30]
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   [31]
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   [32] {ECO:0007744|PDB:3VI3, ECO:0007744|PDB:3VI4}
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 42-664 IN COMPLEX WITH ANTIBODY;
RP   ITGB1; CALCIUM AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-84;
RP   ASN-182; ASN-297; ASN-307; ASN-316 AND ASN-609, SUBSTRATE-BINDING SITES,
RP   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   [33] {ECO:0007744|PDB:7NWL, ECO:0007744|PDB:7NXD}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 42-1049 IN COMPLEX
RP   WITH FN1 (FN7-10 DOMAINS); ITGB1; ANTIBODY AND CALCIUM, FUNCTION, TISSUE
RP   SPECIFICITY, GLYCOSYLATION AT ASN-84; ASN-182; ASN-297; ASN-307; ASN-316;
RP   ASN-524 AND ASN-609, 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: 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 acts
CC       as a receptor for fibronectin (FN1) and mediates R-G-D-dependent cell
CC       adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B
CC       and binding is essential for IL1B signaling (PubMed:29030430).
CC       ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for
CC       CD40/CD40LG signaling (PubMed:31331973). {ECO:0000269|PubMed:12807887,
CC       ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18635536,
CC       ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:29030430,
CC       ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:33962943}.
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       ITGA5/Alpha-5 associates with ITGB1/beta-1 (PubMed:33962943). Interacts
CC       with NISCH (PubMed:11912194). Interacts with HPS5 (PubMed:10094488).
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:10094488,
CC       ECO:0000269|PubMed:11912194, ECO:0000269|PubMed:12695522,
CC       ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16051604,
CC       ECO:0000269|PubMed:16754960, ECO:0000269|PubMed:17158881,
CC       ECO:0000269|PubMed:22451694, ECO:0000269|PubMed:24011356,
CC       ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:32908006,
CC       ECO:0000269|PubMed:33102950, ECO:0000269|PubMed:33962943}.
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: Cell membrane {ECO:0000269|PubMed:17158881};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal
CC       adhesion {ECO:0000269|PubMed:17158881}.
CC   -!- TISSUE SPECIFICITY: Expressed in placenta (at protein level).
CC       {ECO:0000269|PubMed:33962943}.
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   EMDB; EMD-12634; -.
DR   EMDB; EMD-12637; -.
DR   SMR; P08648; -.
DR   BioGRID; 109884; 122.
DR   ComplexPortal; CPX-1794; Integrin alpha5-beta1 complex.
DR   CORUM; P08648; -.
DR   DIP; DIP-40037N; -.
DR   ELM; P08648; -.
DR   IntAct; P08648; 34.
DR   MINT; P08648; -.
DR   STRING; 9606.ENSP00000293379; -.
DR   BindingDB; P08648; -.
DR   ChEMBL; CHEMBL3955; -.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugBank; DB08834; Tauroursodeoxycholic acid.
DR   GuidetoPHARMACOLOGY; 2444; -.
DR   TCDB; 8.A.54.1.8; the integrin (integrin) family.
DR   GlyConnect; 1407; 21 N-Linked glycans (6 sites).
DR   GlyConnect; 283; 35 N-Linked glycans.
DR   GlyCosmos; P08648; 15 sites, 75 glycans.
DR   GlyGen; P08648; 17 sites, 75 N-linked glycans (7 sites), 2 O-linked glycans (2 sites).
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; 9606-ENSP00000293379; -.
DR   PeptideAtlas; P08648; -.
DR   ProteomicsDB; 52147; -.
DR   Pumba; P08648; -.
DR   TopDownProteomics; P08648; -.
DR   ABCD; P08648; 10 sequenced antibodies.
DR   Antibodypedia; 1221; 1275 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   AGR; HGNC:6141; -.
DR   CTD; 3678; -.
DR   DisGeNET; 3678; -.
DR   GeneCards; ITGA5; -.
DR   HGNC; HGNC:6141; ITGA5.
DR   HPA; ENSG00000161638; Tissue enhanced (intestine, 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; VIKMDSY; -.
DR   OrthoDB; 3816176at2759; -.
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; 25 hits in 1157 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 187 other cell types or tissues.
DR   ExpressionAtlas; P08648; baseline and differential.
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:0098978; C:glutamatergic synapse; IEA:Ensembl.
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:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0001726; C:ruffle; TAS:HGNC-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
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: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; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF3; INTEGRIN ALPHA-5; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF20806; Integrin_A_Ig_3; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 3.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   Genevisible; P08648; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
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                   /evidence="ECO:0000269|PubMed:10094488"
FT   MOTIF           1024..1028
FT                   /note="GFFKR motif"
FT                   /evidence="ECO:0000305"
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                   /evidence="ECO:0000269|PubMed:22451694"
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                   /evidence="ECO:0000269|PubMed:22451694"
FT   BINDING         280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         282
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         286
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         288
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         334
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         338
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         340
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         342
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         401
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         403
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         405
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         407
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         409
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         465
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         467
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         469
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         471
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
FT   BINDING         473
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0000312|PDB:7NXD, ECO:0007744|PDB:3VI3,
FT                   ECO:0007744|PDB:3VI4, ECO:0007744|PDB:7NWL"
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                   ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
FT                   ECO:0007744|PDB:7NXD"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22451694,
FT                   ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
FT                   ECO:0007744|PDB:7NXD"
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                   ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
FT                   ECO:0007744|PDB:7NXD"
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                   ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
FT                   ECO:0007744|PDB:7NXD"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22451694,
FT                   ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
FT                   ECO:0007744|PDB:7NXD"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0007744|PDB:7NXD"
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                   ECO:0000269|PubMed:33962943, ECO:0007744|PDB:7NWL,
FT                   ECO:0007744|PDB:7NXD"
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                   /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        156..176
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        192..205
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        513..522
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        528..584
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        645..651
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0007744|PDB:7NXD"
FT   DISULFID        718..731
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0007744|PDB:7NXD"
FT   DISULFID        849..957
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0007744|PDB:7NXD"
FT   DISULFID        869..921
FT                   /note="Interchain (between heavy and light chains)"
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0007744|PDB:7NXD"
FT   DISULFID        911..916
FT                   /evidence="ECO:0000269|PubMed:33962943,
FT                   ECO:0007744|PDB:7NXD"
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
//