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-NOV-2024, entry version 246. 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 IGFBP1. RX PubMed=7504269; DOI=10.1073/pnas.90.22.10553; RA Jones J.I., Gockerman A., Busby W.H. Jr., Wright G., Clemmons D.R.; RT "Insulin-like growth factor binding protein 1 stimulates cell migration and RT binds to the alpha 5 beta 1 integrin by means of its Arg-Gly-Asp RT sequence."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10553-10557(1993). RN [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] RP INTERACTION WITH IGFBP2. RX PubMed=16569642; DOI=10.1074/jbc.m513686200; RA Wang G.K., Hu L., Fuller G.N., Zhang W.; RT "An interaction between insulin-like growth factor-binding protein 2 RT (IGFBP2) and integrin alpha5 is essential for IGFBP2-induced cell RT mobility."; RL J. Biol. Chem. 281:14085-14091(2006). RN [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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 [27] 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 [28] RP INTERACTION WITH IGFBP2. RX PubMed=26076738; DOI=10.1007/s12031-015-0589-3; RA Feng N., Zhang Z., Wang Z., Zheng H., Qu F., He X., Wang C.; RT "Insulin-Like Growth Factor Binding Protein-2 Promotes Adhesion of RT Endothelial Progenitor Cells to Endothelial Cells via Integrin RT alpha5beta1."; RL J. Mol. Neurosci. 57:426-434(2015). RN [29] 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 [30] 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 [31] 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 [32] 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 [33] 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 [34] 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 [35] RP INTERACTION WITH SELP. RX PubMed=37184585; DOI=10.26508/lsa.202201747; RA Takada Y.K., Simon S.I., Takada Y.; RT "The C-type lectin domain of CD62P (P-selectin) functions as an integrin RT ligand."; RL Life. Sci Alliance 6:0-0(2023). RN [36] {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 [37] {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). ITGA5:ITGB1 CC interacts with SELP (PubMed:37184585). Interacts with ANGPT2 CC (PubMed:32908006). ITGA5:ITGB1 interacts with IGFBP2 (PubMed:16569642, CC PubMed:26076738). ITGA5:ITGB1 interacts with IGFBP1 (PubMed:7504269). CC {ECO:0000269|PubMed:10094488, ECO:0000269|PubMed:11912194, CC ECO:0000269|PubMed:12695522, ECO:0000269|PubMed:12807887, CC ECO:0000269|PubMed:16051604, ECO:0000269|PubMed:16569642, CC ECO:0000269|PubMed:16754960, ECO:0000269|PubMed:17158881, CC ECO:0000269|PubMed:22451694, ECO:0000269|PubMed:24011356, CC ECO:0000269|PubMed:26076738, ECO:0000269|PubMed:29030430, CC ECO:0000269|PubMed:32908006, ECO:0000269|PubMed:33102950, CC ECO:0000269|PubMed:33962943, ECO:0000269|PubMed:37184585, CC ECO:0000269|PubMed:7504269}. 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=9; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 9CKV; EM; 3.19 A; A=1-996. 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 PDBsum; 9CKV; -. DR AlphaFoldDB; P08648; -. DR EMDB; EMD-12634; -. DR EMDB; EMD-12637; -. DR EMDB; EMD-45655; -. 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; 66. 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, 107 N-linked glycans (8 sites), 2 O-linked glycans (2 sites). DR iPTMnet; P08648; -. DR PhosphoSitePlus; P08648; -. DR SwissPalm; P08648; -. DR BioMuta; ITGA5; -. DR DMDM; 23831237; -. DR jPOST; P08648; -. DR MassIVE; 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; 1166 antibodies from 48 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 EvolutionaryTrace; P08648; -. 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:0038023; F:signaling receptor activity; IEA:Ensembl. 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:0014850; P:response to muscle activity; IEA:Ensembl. DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEP:BHF-UCL. DR FunFam; 2.130.10.130:FF:000003; Integrin alpha V; 1. DR FunFam; 2.60.40.1510:FF:000001; Integrin alpha V; 1. DR FunFam; 2.60.40.1530:FF:000006; Integrin subunit alpha 5; 1. DR FunFam; 1.20.5.930:FF:000001; Integrin subunit alpha V; 1. DR FunFam; 2.60.40.1460:FF:000001; Integrin, alpha V; 1. 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. 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 Proteomics identification; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; 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 //