GenomeNet

Database: UniProt
Entry: P18564
LinkDB: P18564
Original site: P18564 
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   10-APR-2019, entry version 195.
DE   RecName: Full=Integrin beta-6;
DE   Flags: Precursor;
GN   Name=ITGB6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Pancreas;
RX   PubMed=2365683;
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
RT   6) identified in epithelial cells using the polymerase chain
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   subunit 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.,
RA   Takafuta T., 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
RT   the 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.,
RA   Stanway G.;
RT   "Integrin alpha v beta 6 is an RGD-dependent receptor for
RT   coxsackievirus 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
RT   invasion 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
RT   studies 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
RP   SIMPLES-1/HHV-1 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
RT   receptors for HSV gH/gL to promote endocytosis and activation of
RT   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
RT   amelogenesis 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
RT   amelogenesis imperfecta.";
RL   Hum. Mol. Genet. 23:2157-2163(2014).
RN   [18] {ECO:0000244|PDB:5FFG, ECO:0000244|PDB:5FFO}
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 128-378 IN COMPLEX WITH
RP   TGFB1 AND ITGAV, INTERACTION WITH TGFB1, CALCIUM-BINDING, FUNCTION,
RP   DISULFIDE BONDS, 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-
RT   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). Internalisation 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
CC       for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion
CC       to FBN1 (PubMed:17158881). Integrin alpha-V:beta-6 (ITGAV:ITGB6)
CC       mediates R-G-D-dependent release of transforming growth factor
CC       beta-1 (TGF-beta-1) from regulatory Latency-associated peptide
CC       (LAP), thereby playing a key role in TGF-beta-1 activation
CC       (PubMed:15184403, PubMed:22278742, PubMed:28117447).
CC       {ECO:0000269|PubMed:15184403, ECO:0000269|PubMed:17158881,
CC       ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:22278742,
CC       ECO:0000269|PubMed:28117447}.
CC   -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB6 acts as a
CC       receptor 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
CC       receptor for Herpes simplex virus-1/HHV-1 (PubMed:24367260).
CC       {ECO:0000269|PubMed:24367260}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit
CC       (PubMed:11807098, PubMed:17545607, PubMed:17158881). Interacts
CC       with FLNB (PubMed:11807098). Interacts with HAX1
CC       (PubMed:17545607). ITGAV:ITGB6 interacts with FBN1
CC       (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
CC       (PubMed:9426447, 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       P06756:ITGAV; NbExp=7; IntAct=EBI-2568070, EBI-298282;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Cell junction, focal adhesion
CC       {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         Note=No experimental confirmation available. Gene prediction
CC         confirmed by EST data.;
CC   -!- DISEASE: Amelogenesis imperfecta 1H (AI1H) [MIM:616221]: A
CC       disorder characterized by defective enamel formation, resulting in
CC       hypoplastic and hypomineralized tooth enamel that may be rough,
CC       pitted, and/or discolored. {ECO:0000269|PubMed:24305999,
CC       ECO:0000269|PubMed:24319098}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
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   UniGene; Hs.470399; -.
DR   PDB; 1LH9; Model; -; A=76-546.
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; 1LH9; -.
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   ProteinModelPortal; P18564; -.
DR   SMR; P18564; -.
DR   BioGrid; 109900; 5.
DR   ComplexPortal; CPX-1820; Integrin alphav-beta6 complex.
DR   CORUM; P18564; -.
DR   DIP; DIP-59187N; -.
DR   ELM; P18564; -.
DR   IntAct; P18564; 2.
DR   STRING; 9606.ENSP00000283249; -.
DR   BindingDB; P18564; -.
DR   ChEMBL; CHEMBL2111416; -.
DR   GlyConnect; 1419; -.
DR   iPTMnet; P18564; -.
DR   PhosphoSitePlus; P18564; -.
DR   BioMuta; ITGB6; -.
DR   DMDM; 13432176; -.
DR   EPD; P18564; -.
DR   jPOST; P18564; -.
DR   MaxQB; P18564; -.
DR   PaxDb; P18564; -.
DR   PeptideAtlas; P18564; -.
DR   PRIDE; P18564; -.
DR   ProteomicsDB; 53577; -.
DR   DNASU; 3694; -.
DR   Ensembl; ENST00000283249; ENSP00000283249; ENSG00000115221. [P18564-1]
DR   Ensembl; ENST00000409872; ENSP00000386367; ENSG00000115221. [P18564-1]
DR   Ensembl; ENST00000409967; ENSP00000386828; ENSG00000115221. [P18564-2]
DR   GeneID; 3694; -.
DR   KEGG; hsa:3694; -.
DR   UCSC; uc010fou.4; human. [P18564-1]
DR   CTD; 3694; -.
DR   DisGeNET; 3694; -.
DR   EuPathDB; HostDB:ENSG00000115221.10; -.
DR   GeneCards; ITGB6; -.
DR   HGNC; HGNC:6161; ITGB6.
DR   HPA; CAB073536; -.
DR   HPA; HPA023626; -.
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   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P18564; -.
DR   KO; K06589; -.
DR   OMA; VSIPNCE; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P18564; -.
DR   TreeFam; TF105392; -.
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-3000178; ECM proteoglycans.
DR   SignaLink; P18564; -.
DR   SIGNOR; P18564; -.
DR   ChiTaRS; ITGB6; human.
DR   GeneWiki; Integrin,_beta_6; -.
DR   GenomeRNAi; 3694; -.
DR   PRO; PR:P18564; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000115221; Expressed in 152 organ(s), highest expression level in visceral pleura.
DR   ExpressionAtlas; P18564; baseline and differential.
DR   Genevisible; P18564; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
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; IBA:GO_Central.
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: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:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:1901388; P:regulation of transforming growth factor beta activation; IDA:UniProtKB.
DR   GO; GO:0038044; P:transforming growth factor-beta secretion; IEA:Ensembl.
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;
KW   Cell adhesion; Cell junction; Complete proteome; Disease mutation;
KW   Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Integrin; Membrane; Polymorphism; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    788       Integrin beta-6.
FT                                /FTId=PRO_0000016350.
FT   TOPO_DOM     22    709       Extracellular. {ECO:0000255}.
FT   TRANSMEM    710    730       Helical. {ECO:0000255}.
FT   TOPO_DOM    731    788       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      131    371       VWFA.
FT   REPEAT      456    501       I.
FT   REPEAT      502    543       II.
FT   REPEAT      544    582       III.
FT   REPEAT      583    619       IV.
FT   REGION      456    619       Cysteine-rich tandem repeats.
FT   REGION      731    758       Interaction with HAX1.
FT                                {ECO:0000269|PubMed:17545607}.
FT   CARBOHYD     48     48       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     97     97       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    260    260       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:28117447}.
FT   CARBOHYD    387    387       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    396    396       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    463    463       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    471    471       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    541    541       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    575    575       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     23    454       {ECO:0000250}.
FT   DISULFID     31     41       {ECO:0000250}.
FT   DISULFID     34     70       {ECO:0000250}.
FT   DISULFID     44     59       {ECO:0000250}.
FT   DISULFID    197    204       {ECO:0000269|PubMed:28117447}.
FT   DISULFID    252    293       {ECO:0000269|PubMed:28117447}.
FT   DISULFID    394    406       {ECO:0000250}.
FT   DISULFID    426    670       {ECO:0000250}.
FT   DISULFID    452    456       {ECO:0000250}.
FT   DISULFID    467    479       {ECO:0000250}.
FT   DISULFID    476    511       {ECO:0000250}.
FT   DISULFID    481    490       {ECO:0000250}.
FT   DISULFID    492    502       {ECO:0000250}.
FT   DISULFID    517    522       {ECO:0000250}.
FT   DISULFID    519    552       {ECO:0000250}.
FT   DISULFID    524    537       {ECO:0000250}.
FT   DISULFID    539    544       {ECO:0000250}.
FT   DISULFID    558    563       {ECO:0000250}.
FT   DISULFID    560    591       {ECO:0000250}.
FT   DISULFID    565    574       {ECO:0000250}.
FT   DISULFID    576    583       {ECO:0000250}.
FT   DISULFID    597    602       {ECO:0000250}.
FT   DISULFID    599    645       {ECO:0000250}.
FT   DISULFID    604    614       {ECO:0000250}.
FT   DISULFID    617    620       {ECO:0000250}.
FT   DISULFID    624    633       {ECO:0000250}.
FT   DISULFID    630    702       {ECO:0000250}.
FT   DISULFID    649    678       {ECO:0000250}.
FT   VAR_SEQ     554    660       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_055189.
FT   VARIANT     143    143       A -> T (in AI1H; dbSNP:rs140015315).
FT                                {ECO:0000269|PubMed:24305999}.
FT                                /FTId=VAR_073328.
FT   VARIANT     196    196       P -> T (in AI1H; dbSNP:rs730880298).
FT                                {ECO:0000269|PubMed:24319098}.
FT                                /FTId=VAR_073329.
FT   VARIANT     275    275       H -> Q (in AI1H; dbSNP:rs730882118).
FT                                {ECO:0000269|PubMed:24305999}.
FT                                /FTId=VAR_073330.
FT   VARIANT     437    437       P -> T (in dbSNP:rs2305820).
FT                                /FTId=VAR_049636.
FT   TURN         24     26       {ECO:0000244|PDB:4UM9}.
FT   HELIX        31     34       {ECO:0000244|PDB:4UM9}.
FT   STRAND       42     44       {ECO:0000244|PDB:4UM9}.
FT   HELIX        62     68       {ECO:0000244|PDB:4UM9}.
FT   TURN         72     74       {ECO:0000244|PDB:4UM9}.
FT   STRAND       81     86       {ECO:0000244|PDB:4UM9}.
FT   HELIX        98    100       {ECO:0000244|PDB:4UM9}.
FT   STRAND      108    113       {ECO:0000244|PDB:4UM9}.
FT   STRAND      119    126       {ECO:0000244|PDB:4UM9}.
FT   STRAND      133    140       {ECO:0000244|PDB:5FFG}.
FT   HELIX       143    145       {ECO:0000244|PDB:5FFG}.
FT   HELIX       146    151       {ECO:0000244|PDB:5FFG}.
FT   HELIX       152    154       {ECO:0000244|PDB:5FFG}.
FT   HELIX       155    166       {ECO:0000244|PDB:5FFG}.
FT   STRAND      170    177       {ECO:0000244|PDB:5FFG}.
FT   TURN        183    185       {ECO:0000244|PDB:4UM9}.
FT   HELIX       190    194       {ECO:0000244|PDB:5FFG}.
FT   TURN        196    201       {ECO:0000244|PDB:5FFG}.
FT   STRAND      209    218       {ECO:0000244|PDB:5FFG}.
FT   HELIX       220    229       {ECO:0000244|PDB:5FFG}.
FT   STRAND      236    241       {ECO:0000244|PDB:4UM9}.
FT   HELIX       242    251       {ECO:0000244|PDB:5FFG}.
FT   HELIX       253    256       {ECO:0000244|PDB:5FFG}.
FT   STRAND      262    272       {ECO:0000244|PDB:5FFG}.
FT   HELIX       277    283       {ECO:0000244|PDB:5FFG}.
FT   STRAND      297    301       {ECO:0000244|PDB:5FFG}.
FT   TURN        302    306       {ECO:0000244|PDB:5FFG}.
FT   HELIX       312    321       {ECO:0000244|PDB:5FFG}.
FT   STRAND      324    330       {ECO:0000244|PDB:5FFG}.
FT   HELIX       332    344       {ECO:0000244|PDB:5FFG}.
FT   STRAND      349    352       {ECO:0000244|PDB:5FFG}.
FT   HELIX       360    371       {ECO:0000244|PDB:5FFG}.
FT   STRAND      375    382       {ECO:0000244|PDB:4UM9}.
FT   STRAND      387    393       {ECO:0000244|PDB:4UM9}.
FT   TURN        395    397       {ECO:0000244|PDB:4UM8}.
FT   STRAND      399    401       {ECO:0000244|PDB:4UM9}.
FT   STRAND      414    422       {ECO:0000244|PDB:4UM9}.
FT   STRAND      431    437       {ECO:0000244|PDB:4UM9}.
FT   STRAND      444    450       {ECO:0000244|PDB:4UM9}.
FT   HELIX       455    457       {ECO:0000244|PDB:4UM8}.
FT   STRAND      467    475       {ECO:0000244|PDB:4UM9}.
FT   STRAND      478    481       {ECO:0000244|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
//
DBGET integrated database retrieval system