ITB6_HUMAN
ID ITB6_HUMAN Reviewed; 788 AA.
AC P18564; B2R9W5; C9JA97; Q0VA95; Q16500; Q53RG5; Q53RR6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Integrin beta-6;
DE Flags: Precursor;
GN Name=ITGB6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=2365683; DOI=10.1016/s0021-9258(19)38425-x;
RA Sheppard D., Rozzo C., Starr L., Quaranta V., Erle D.J., Pytela R.;
RT "Complete amino acid sequence of a novel integrin beta subunit (beta 6)
RT identified in epithelial cells using the polymerase chain reaction.";
RL J. Biol. Chem. 265:11502-11507(1990).
RN [2]
RP SEQUENCE REVISION TO 18-24; 158; 642 AND 719.
RA Askins J.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-197.
RX PubMed=1382574; DOI=10.1093/intimm/4.9.1031;
RA Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D.,
RA Krissansen G.W.;
RT "The gene organization of the human beta 7 subunit, the common beta subunit
RT of the leukocyte integrins HML-1 and LPAM-1.";
RL Int. Immunol. 4:1031-1040(1992).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS B1
RP CAPSID PROTEINS.
RX PubMed=9426447; DOI=10.1006/viro.1997.8831;
RA Agrez M.V., Shafren D.R., Gu X., Cox K., Sheppard D., Barry R.D.;
RT "Integrin alpha v beta 6 enhances coxsackievirus B1 lytic infection of
RT human colon cancer cells.";
RL Virology 239:71-77(1997).
RN [9]
RP INTERACTION WITH FLNB.
RC TISSUE=Keratinocyte, and Skeletal muscle;
RX PubMed=11807098; DOI=10.1083/jcb.200103037;
RA van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T.,
RA Shapiro S.S., Sonnenberg A.;
RT "Different splice variants of filamin-B affect myogenesis, subcellular
RT distribution, and determine binding to integrin (beta) subunits.";
RL J. Cell Biol. 156:361-376(2002).
RN [10]
RP FUNCTION.
RX PubMed=15184403; DOI=10.1083/jcb.200312172;
RA Annes J.P., Chen Y., Munger J.S., Rifkin D.B.;
RT "Integrin alphaVbeta6-mediated activation of latent TGF-beta requires the
RT latent TGF-beta binding protein-1.";
RL J. Cell Biol. 165:723-734(2004).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A9
RP CAPSID PROTEINS.
RX PubMed=15194773; DOI=10.1128/jvi.78.13.6967-6973.2004;
RA Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.;
RT "Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus
RT A9.";
RL J. Virol. 78:6967-6973(2004).
RN [12]
RP INTERACTION WITH HAX1, AND FUNCTION.
RX PubMed=17545607; DOI=10.1158/0008-5472.can-07-0318;
RA Ramsay A.G., Keppler M.D., Jazayeri M., Thomas G.J., Parsons M.,
RA Violette S., Weinreb P., Hart I.R., Marshall J.F.;
RT "HS1-associated protein X-1 regulates carcinoma cell migration and invasion
RT via clathrin-mediated endocytosis of integrin alphavbeta6.";
RL Cancer Res. 67:5275-5284(2007).
RN [13]
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 [14]
RP FUNCTION, AND INTERACTION WITH TGFB1.
RX PubMed=22278742; DOI=10.1091/mbc.e11-12-1018;
RA Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.;
RT "GARP regulates the bioavailability and activation of TGFbeta.";
RL Mol. Biol. Cell 23:1129-1139(2012).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLES-1/HHV-1
RP GH:GL PROTEINS.
RX PubMed=24367260; DOI=10.1371/journal.ppat.1003806;
RA Gianni T., Salvioli S., Chesnokova L.S., Hutt-Fletcher L.M.,
RA Campadelli-Fiume G.;
RT "alphavbeta6- and alphavbeta8-integrins serve as interchangeable receptors
RT for HSV gH/gL to promote endocytosis and activation of membrane fusion.";
RL PLoS Pathog. 9:E1003806-E1003806(2013).
RN [16]
RP INVOLVEMENT IN AI1H, AND VARIANT AI1H THR-196.
RX PubMed=24319098; DOI=10.1093/hmg/ddt616;
RA Poulter J.A., Brookes S.J., Shore R.C., Smith C.E., Abi Farraj L.,
RA Kirkham J., Inglehearn C.F., Mighell A.J.;
RT "A missense mutation in ITGB6 causes pitted hypomineralized amelogenesis
RT imperfecta.";
RL Hum. Mol. Genet. 23:2189-2197(2014).
RN [17]
RP INVOLVEMENT IN AI1H, AND VARIANTS AI1H THR-143 AND GLN-275.
RX PubMed=24305999; DOI=10.1093/hmg/ddt611;
RA Wang S.K., Choi M., Richardson A.S., Reid B.M., Lin B.P., Wang S.J.,
RA Kim J.W., Simmer J.P., Hu J.C.;
RT "ITGB6 loss-of-function mutations cause autosomal recessive amelogenesis
RT imperfecta.";
RL Hum. Mol. Genet. 23:2157-2163(2014).
RN [18] {ECO:0007744|PDB:5FFG, ECO:0007744|PDB:5FFO}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 128-378 IN COMPLEX WITH TGFB1 AND
RP ITGAV, INTERACTION WITH TGFB1, CALCIUM-BINDING, FUNCTION, DISULFIDE BONDS,
RP AND GLYCOSYLATION AT ASN-260.
RX PubMed=28117447; DOI=10.1038/nature21035;
RA Dong X., Zhao B., Iacob R.E., Zhu J., Koksal A.C., Lu C., Engen J.R.,
RA Springer T.A.;
RT "Force interacts with macromolecular structure in activation of TGF-beta.";
RL Nature 542:55-59(2017).
CC -!- FUNCTION: Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for
CC fibronectin and cytotactin (PubMed:17545607, PubMed:17158881). It
CC recognizes the sequence R-G-D in its ligands (PubMed:17545607,
CC PubMed:17158881). Internalization of integrin alpha-V/beta-6 via
CC clathrin-mediated endocytosis promotes carcinoma cell invasion
CC (PubMed:17545607, PubMed:17158881). ITGAV:ITGB6 acts as a receptor for
CC fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1
CC (PubMed:17158881). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-
CC D-dependent release of transforming growth factor beta-1 (TGF-beta-1)
CC from regulatory Latency-associated peptide (LAP), thereby playing a key
CC role in TGF-beta-1 activation (PubMed:15184403, PubMed:22278742,
CC PubMed:28117447). {ECO:0000269|PubMed:15184403,
CC ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17545607,
CC ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:28117447}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB6 acts as a receptor
CC for Coxsackievirus A9 and Coxsackievirus B1.
CC {ECO:0000269|PubMed:15194773, ECO:0000269|PubMed:9426447}.
CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB6 acts as a receptor
CC for Herpes simplex virus-1/HHV-1 (PubMed:24367260).
CC {ECO:0000269|PubMed:24367260}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:11807098,
CC PubMed:17545607, PubMed:17158881). Interacts with FLNB
CC (PubMed:11807098). Interacts with HAX1 (PubMed:17545607). ITGAV:ITGB6
CC interacts with FBN1 (PubMed:17158881). ITGAV:ITGB6 interacts with TGFB1
CC (PubMed:22278742, PubMed:28117447). {ECO:0000269|PubMed:11807098,
CC ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:17545607,
CC ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:28117447}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB6 interacts with
CC coxsackievirus A9, coxsackievirus B1 capsid proteins (PubMed:9426447,
CC PubMed:15194773). {ECO:0000269|PubMed:15194773,
CC ECO:0000269|PubMed:9426447}.
CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB6 interacts with
CC herpes simplex virus-1/HHV-1 gH:gL proteins.
CC {ECO:0000269|PubMed:24367260}.
CC -!- INTERACTION:
CC P18564; P06756: ITGAV; NbExp=8; IntAct=EBI-2568070, EBI-298282;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P18564-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P18564-2; Sequence=VSP_055189;
CC -!- DISEASE: Amelogenesis imperfecta 1H (AI1H) [MIM:616221]: A disorder
CC characterized by defective enamel formation, resulting in hypoplastic
CC and hypomineralized tooth enamel that may be rough, pitted, and/or
CC discolored. {ECO:0000269|PubMed:24305999, ECO:0000269|PubMed:24319098}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; M35198; AAA36122.2; -; mRNA.
DR EMBL; AC092153; AAX93093.1; -; Genomic_DNA.
DR EMBL; AK313944; BAG36662.1; -; mRNA.
DR EMBL; AC080166; AAY24053.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11390.1; -; Genomic_DNA.
DR EMBL; BC121178; AAI21179.1; -; mRNA.
DR EMBL; S49380; AAB23690.1; -; Genomic_DNA.
DR CCDS; CCDS2212.1; -. [P18564-1]
DR CCDS; CCDS63040.1; -. [P18564-2]
DR PIR; A37057; A37057.
DR RefSeq; NP_000879.2; NM_000888.4. [P18564-1]
DR RefSeq; NP_001269282.1; NM_001282353.1. [P18564-1]
DR RefSeq; NP_001269284.1; NM_001282355.1. [P18564-2]
DR RefSeq; NP_001269317.1; NM_001282388.1.
DR PDB; 4UM8; X-ray; 2.85 A; B/D=1-788.
DR PDB; 4UM9; X-ray; 2.50 A; B/D=18-491.
DR PDB; 5FFG; X-ray; 2.25 A; B=128-378.
DR PDB; 5FFO; X-ray; 3.49 A; B/F=128-378.
DR PDB; 5NEM; EM; 3.10 A; B=22-491.
DR PDB; 5NER; EM; 3.10 A; B=22-491.
DR PDB; 5NET; EM; 3.10 A; B=22-491.
DR PDB; 5NEU; EM; 3.10 A; B=22-491.
DR PDBsum; 4UM8; -.
DR PDBsum; 4UM9; -.
DR PDBsum; 5FFG; -.
DR PDBsum; 5FFO; -.
DR PDBsum; 5NEM; -.
DR PDBsum; 5NER; -.
DR PDBsum; 5NET; -.
DR PDBsum; 5NEU; -.
DR AlphaFoldDB; P18564; -.
DR SMR; P18564; -.
DR BioGRID; 109900; 9.
DR ComplexPortal; CPX-1820; Integrin alphav-beta6 complex.
DR CORUM; P18564; -.
DR DIP; DIP-59187N; -.
DR ELM; P18564; -.
DR IntAct; P18564; 3.
DR STRING; 9606.ENSP00000283249; -.
DR BindingDB; P18564; -.
DR ChEMBL; CHEMBL2111416; -.
DR GuidetoPHARMACOLOGY; 2460; -.
DR GlyConnect; 1419; 7 N-Linked glycans (2 sites).
DR GlyGen; P18564; 10 sites, 7 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P18564; -.
DR PhosphoSitePlus; P18564; -.
DR BioMuta; ITGB6; -.
DR DMDM; 13432176; -.
DR EPD; P18564; -.
DR jPOST; P18564; -.
DR MassIVE; P18564; -.
DR MaxQB; P18564; -.
DR PaxDb; P18564; -.
DR PeptideAtlas; P18564; -.
DR PRIDE; P18564; -.
DR ProteomicsDB; 53577; -. [P18564-1]
DR ProteomicsDB; 9297; -.
DR ABCD; P18564; 49 sequenced antibodies.
DR Antibodypedia; 33727; 350 antibodies from 28 providers.
DR DNASU; 3694; -.
DR Ensembl; ENST00000283249.7; ENSP00000283249.2; ENSG00000115221.12. [P18564-1]
DR Ensembl; ENST00000409872.1; ENSP00000386367.1; ENSG00000115221.12. [P18564-1]
DR Ensembl; ENST00000409967.6; ENSP00000386828.2; ENSG00000115221.12. [P18564-2]
DR GeneID; 3694; -.
DR KEGG; hsa:3694; -.
DR MANE-Select; ENST00000283249.7; ENSP00000283249.2; NM_000888.5; NP_000879.2.
DR UCSC; uc010fou.4; human. [P18564-1]
DR CTD; 3694; -.
DR DisGeNET; 3694; -.
DR GeneCards; ITGB6; -.
DR HGNC; HGNC:6161; ITGB6.
DR HPA; ENSG00000115221; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; ITGB6; -.
DR MIM; 147558; gene.
DR MIM; 616221; phenotype.
DR neXtProt; NX_P18564; -.
DR OpenTargets; ENSG00000115221; -.
DR Orphanet; 2850; Alopecia-intellectual disability syndrome.
DR Orphanet; 100032; Hypocalcified amelogenesis imperfecta.
DR Orphanet; 100031; Hypoplastic amelogenesis imperfecta.
DR PharmGKB; PA29960; -.
DR VEuPathDB; HostDB:ENSG00000115221; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR InParanoid; P18564; -.
DR OMA; LSGPHCA; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P18564; -.
DR TreeFam; TF105392; -.
DR PathwayCommons; P18564; -.
DR Reactome; R-HSA-1566948; Elastic fibre formation.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR SignaLink; P18564; -.
DR SIGNOR; P18564; -.
DR BioGRID-ORCS; 3694; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; ITGB6; human.
DR GeneWiki; Integrin,_beta_6; -.
DR GenomeRNAi; 3694; -.
DR Pharos; P18564; Tbio.
DR PRO; PR:P18564; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P18564; protein.
DR Bgee; ENSG00000115221; Expressed in visceral pleura and 133 other tissues.
DR ExpressionAtlas; P18564; baseline and differential.
DR Genevisible; P18564; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0060435; P:bronchiole development; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0061520; P:Langerhans cell differentiation; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR GO; GO:0071604; P:transforming growth factor beta production; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR DisProt; DP02530; -.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015436; Integrin_bsu-6.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF11; PTHR10082:SF11; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 2.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amelogenesis imperfecta; Cell adhesion;
KW Cell junction; Disease variant; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Integrin;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..788
FT /note="Integrin beta-6"
FT /id="PRO_0000016350"
FT TOPO_DOM 22..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 131..371
FT /note="VWFA"
FT REPEAT 456..501
FT /note="I"
FT REPEAT 502..543
FT /note="II"
FT REPEAT 544..582
FT /note="III"
FT REPEAT 583..619
FT /note="IV"
FT REGION 456..619
FT /note="Cysteine-rich tandem repeats"
FT REGION 731..758
FT /note="Interaction with HAX1"
FT /evidence="ECO:0000269|PubMed:17545607"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28117447"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..454
FT /evidence="ECO:0000250"
FT DISULFID 31..41
FT /evidence="ECO:0000250"
FT DISULFID 34..70
FT /evidence="ECO:0000250"
FT DISULFID 44..59
FT /evidence="ECO:0000250"
FT DISULFID 197..204
FT /evidence="ECO:0000269|PubMed:28117447"
FT DISULFID 252..293
FT /evidence="ECO:0000269|PubMed:28117447"
FT DISULFID 394..406
FT /evidence="ECO:0000250"
FT DISULFID 426..670
FT /evidence="ECO:0000250"
FT DISULFID 452..456
FT /evidence="ECO:0000250"
FT DISULFID 467..479
FT /evidence="ECO:0000250"
FT DISULFID 476..511
FT /evidence="ECO:0000250"
FT DISULFID 481..490
FT /evidence="ECO:0000250"
FT DISULFID 492..502
FT /evidence="ECO:0000250"
FT DISULFID 517..522
FT /evidence="ECO:0000250"
FT DISULFID 519..552
FT /evidence="ECO:0000250"
FT DISULFID 524..537
FT /evidence="ECO:0000250"
FT DISULFID 539..544
FT /evidence="ECO:0000250"
FT DISULFID 558..563
FT /evidence="ECO:0000250"
FT DISULFID 560..591
FT /evidence="ECO:0000250"
FT DISULFID 565..574
FT /evidence="ECO:0000250"
FT DISULFID 576..583
FT /evidence="ECO:0000250"
FT DISULFID 597..602
FT /evidence="ECO:0000250"
FT DISULFID 599..645
FT /evidence="ECO:0000250"
FT DISULFID 604..614
FT /evidence="ECO:0000250"
FT DISULFID 617..620
FT /evidence="ECO:0000250"
FT DISULFID 624..633
FT /evidence="ECO:0000250"
FT DISULFID 630..702
FT /evidence="ECO:0000250"
FT DISULFID 649..678
FT /evidence="ECO:0000250"
FT VAR_SEQ 554..660
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055189"
FT VARIANT 143
FT /note="A -> T (in AI1H; dbSNP:rs140015315)"
FT /evidence="ECO:0000269|PubMed:24305999"
FT /id="VAR_073328"
FT VARIANT 196
FT /note="P -> T (in AI1H; dbSNP:rs730880298)"
FT /evidence="ECO:0000269|PubMed:24319098"
FT /id="VAR_073329"
FT VARIANT 275
FT /note="H -> Q (in AI1H; dbSNP:rs730882118)"
FT /evidence="ECO:0000269|PubMed:24305999"
FT /id="VAR_073330"
FT VARIANT 437
FT /note="P -> T (in dbSNP:rs2305820)"
FT /id="VAR_049636"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4UM9"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4UM9"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:4UM9"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:4UM9"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:5FFG"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:4UM9"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:5FFG"
FT TURN 196..201
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4UM9"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:5FFG"
FT TURN 302..306
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:5FFG"
FT HELIX 360..371
FT /evidence="ECO:0007829|PDB:5FFG"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:4UM9"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:4UM8"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 414..422
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:4UM9"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:4UM8"
FT STRAND 467..475
FT /evidence="ECO:0007829|PDB:4UM9"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:4UM9"
SQ SEQUENCE 788 AA; 85936 MW; EDB7D533EC4C8C4D CRC64;
MGIELLCLFF LFLGRNDHVQ GGCALGGAET CEDCLLIGPQ CAWCAQENFT HPSGVGERCD
TPANLLAKGC QLNFIENPVS QVEILKNKPL SVGRQKNSSD IVQIAPQSLI LKLRPGGAQT
LQVHVRQTED YPVDLYYLMD LSASMDDDLN TIKELGSRLS KEMSKLTSNF RLGFGSFVEK
PVSPFVKTTP EEIANPCSSI PYFCLPTFGF KHILPLTNDA ERFNEIVKNQ KISANIDTPE
GGFDAIMQAA VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDSKNE
YSMSTVLEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV GLLQKDSGNI
LQLIISAYEE LRSEVELEVL GDTEGLNLSF TAICNNGTLF QHQKKCSHMK VGDTASFSVT
VNIPHCERRS RHIIIKPVGL GDALELLVSP ECNCDCQKEV EVNSSKCHHG NGSFQCGVCA
CHPGHMGPRC ECGEDMLSTD SCKEAPDHPS CSGRGDCYCG QCICHLSPYG NIYGPYCQCD
NFSCVRHKGL LCGGNGDCDC GECVCRSGWT GEYCNCTTST DSCVSEDGVL CSGRGDCVCG
KCVCTNPGAS GPTCERCPTC GDPCNSKRSC IECHLSAAGQ AREECVDKCK LAGATISEEE
DFSKDGSVSC SLQGENECLI TFLITTDNEG KTIIHSINEK DCPKPPNIPM IMLGVSLAIL
LIGVVLLCIW KLLVSFHDRK EVAKFEAERS KAKWQTGTNP LYRGSTSTFK NVTYKHREKQ
KVDLSTDC
