GenomeNet

Database: UniProt
Entry: P23229
LinkDB: P23229
Original site: P23229 
ID   ITA6_HUMAN              Reviewed;        1130 AA.
AC   P23229; B2RMU9; B4DG69; B4DKB8; C4AM96; G5E9H1; Q08443; Q0MRC7;
AC   Q14646; Q16508; Q53RX7; Q59HB7; Q86VL6; Q9UCT1; Q9UN03;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 5.
DT   03-SEP-2014, entry version 165.
DE   RecName: Full=Integrin alpha-6;
DE   AltName: Full=CD49 antigen-like family member F;
DE   AltName: Full=VLA-6;
DE   AltName: CD_antigen=CD49f;
DE   Contains:
DE     RecName: Full=Integrin alpha-6 heavy chain;
DE   Contains:
DE     RecName: Full=Integrin alpha-6 light chain;
DE   Contains:
DE     RecName: Full=Processed integrin alpha-6;
DE              Short=Alpha6p;
DE   Flags: Precursor;
GN   Name=ITGA6;
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 ALPHA-6X1A).
RC   TISSUE=Pancreas;
RX   PubMed=1976638; DOI=10.1083/jcb.111.4.1593;
RA   Tamura R.N., Rozzo C., Starr L., Chambers J., Reichardt L.F.,
RA   Cooper H.M., Quaranta V.;
RT   "Epithelial integrin alpha 6 beta 4: complete primary structure of
RT   alpha 6 and variant forms of beta 4.";
RL   J. Cell Biol. 111:1593-1604(1990).
RN   [2]
RP   SEQUENCE REVISION TO 78 AND 362.
RA   Quaranta V.;
RL   Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-6X1A).
RA   Pulkkinen L., Uitto J.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 266-1130 (ISOFORM ALPHA-6X1X2A).
RC   TISSUE=Amygdala, and Thalamus;
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   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-6X1A), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 412-1130 (ISOFORM 9).
RC   TISSUE=Brain, and Skin;
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   [8]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-6X1A).
RC   TISSUE=Keratinocyte;
RX   PubMed=2070796; DOI=10.1111/j.1432-1033.1991.tb16140.x;
RA   Hogervorst F., Kuikman I., Geurts van Kessel A., Sonnenberg A.;
RT   "Molecular cloning of the human alpha 6 integrin subunit. Alternative
RT   splicing of alpha 6 mRNA and chromosomal localization of the alpha 6
RT   and beta 4 genes.";
RL   Eur. J. Biochem. 199:425-433(1991).
RN   [9]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-6X1A AND
RP   ALPHA-6X1B).
RX   PubMed=1946438; DOI=10.1073/pnas.88.22.10183;
RA   Tamura R.N., Cooper H.M., Collo G., Quaranta V.;
RT   "Cell type-specific integrin variants with alternative alpha chain
RT   cytoplasmic domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10183-10187(1991).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 748-849.
RX   PubMed=1476731;
RA   Starr L., Quaranta V.;
RT   "An efficient and reliable method for cloning PCR-amplification
RT   products: a survey of point mutations in integrin cDNA.";
RL   BioTechniques 13:612-618(1992).
RN   [11]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-6X1A).
RX   PubMed=8496190;
RA   Shaw L.M., Lotz M.M., Mercurio A.M.;
RT   "Inside-out integrin signaling in macrophages. Analysis of the role of
RT   the alpha 6A beta 1 and alpha 6B beta 1 integrin variants in laminin
RT   adhesion by cDNA expression in an alpha 6 integrin-deficient
RT   macrophage cell line.";
RL   J. Biol. Chem. 268:11401-11408(1993).
RN   [12]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leukocyte;
RX   PubMed=8253814;
RA   Ziober B.L., Vu M.P., Waleh N., Crawford J., Lin C.-S., Kramer R.H.;
RT   "Alternative extracellular and cytoplasmic domains of the integrin
RT   alpha 7 subunit are differentially expressed during development.";
RL   J. Biol. Chem. 268:26773-26783(1993).
RN   [13]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Lymphoma;
RX   PubMed=7583007;
RA   Delwel G.O., Kuikman I., Sonnenberg A.;
RT   "An alternatively spliced exon in the extracellular domain of the
RT   human alpha 6 integrin subunit -- functional analysis of the alpha 6
RT   integrin variants.";
RL   Cell Adhes. Commun. 3:143-161(1995).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-1130 (ISOFORM
RP   ALPHA-6X1X2B).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   PROTEIN SEQUENCE OF 24-44.
RX   PubMed=2649503;
RA   Hemler M.E., Crouse C., Sonnenberg A.;
RT   "Association of the VLA alpha 6 subunit with a novel protein. A
RT   possible alternative to the common VLA beta 1 subunit on certain cell
RT   lines.";
RL   J. Biol. Chem. 264:6529-6535(1989).
RN   [16]
RP   PROTEIN SEQUENCE OF 24-46.
RX   PubMed=2542022;
RA   Kajiji S., Tamura R.N., Quaranta V.;
RT   "A novel integrin (alpha E beta 4) from human epithelial cells
RT   suggests a fourth family of integrin adhesion receptors.";
RL   EMBO J. 8:673-680(1989).
RN   [17]
RP   PROTEIN SEQUENCE OF 24-36.
RC   TISSUE=Platelet;
RX   PubMed=1953640;
RA   Catimel B., Parmentier S., Leung L.L., McGregor J.L.;
RT   "Separation of important new platelet glycoproteins (GPIa, GPIc,
RT   GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal
RT   antibodies and gas-phase sequencing.";
RL   Biochem. J. 279:419-425(1991).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1001-1130.
RA   Dydensborg A.B., Herring E., Beaulieu J.-F.;
RT   "Integrin alpha6Abeta4 in human colon cancer.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [19]
RP   PHOSPHORYLATION AT SER-1059 (ISOFORM ALPHA-6X2A); SER-1064 (ISOFORM
RP   ALPHA-6X1A) AND SER-1103 (ISOFORM ALPHA-6X1X2A).
RX   PubMed=8360143;
RA   Hogervorst F., Kuikman I., Noteboom E., Sonnenberg A.;
RT   "The role of phosphorylation in activation of the alpha 6A beta 1
RT   laminin receptor.";
RL   J. Biol. Chem. 268:18427-18430(1993).
RN   [20]
RP   CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX   PubMed=7681434; DOI=10.1083/jcb.121.1.179;
RA   Hogervorst F., Admiraal L.G., Niessen C., Kuikman I., Janssen H.,
RA   Daams H., Sonnenberg A.;
RT   "Biochemical characterization and tissue distribution of the A and B
RT   variants of the integrin alpha 6 subunit.";
RL   J. Cell Biol. 121:179-191(1993).
RN   [21]
RP   PALMITOYLATION AT CYS-1078.
RX   PubMed=15611341; DOI=10.1083/jcb.200404100;
RA   Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.;
RT   "Palmitoylation supports assembly and function of integrin-tetraspanin
RT   complexes.";
RL   J. Cell Biol. 167:1231-1240(2004).
RN   [22]
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
RT   traffic of beta1-integrins.";
RL   J. Cell Biol. 173:767-780(2006).
RN   [23]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323.
RC   TISSUE=Platelet;
RX   PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
RA   Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT   "Elucidation of N-glycosylation sites on human platelet proteins: a
RT   glycoproteomic approach.";
RL   Mol. Cell. Proteomics 5:226-233(2006).
RN   [24]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-997.
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
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [25]
RP   PROTEOLYTIC PROCESSING, AND FUNCTION IN CELL MIGRATION.
RX   PubMed=17303120; DOI=10.1016/j.yexcr.2007.01.006;
RA   Pawar S.C., Demetriou M.C., Nagle R.B., Bowden G.T., Cress A.E.;
RT   "Integrin alpha6 cleavage: a novel modification to modulate cell
RT   migration.";
RL   Exp. Cell Res. 313:1080-1089(2007).
RN   [26]
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.,
RA   Buerckstuemmer T., 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   [27]
RP   PALMITOYLATION AT CYS-1078 BY DHHC3, AND SUBCELLULAR LOCATION.
RX   PubMed=22314500; DOI=10.1007/s00018-012-0924-6;
RA   Sharma C., Rabinovitz I., Hemler M.E.;
RT   "Palmitoylation by DHHC3 is critical for the function, expression, and
RT   stability of integrin alpha6beta4.";
RL   Cell. Mol. Life Sci. 69:2233-2244(2012).
CC   -!- FUNCTION: Integrin alpha-6/beta-1 is a receptor for laminin on
CC       platelets. Integrin alpha-6/beta-4 is a receptor for laminin in
CC       epithelial cells and it plays a critical structural role in the
CC       hemidesmosome.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
CC       subunit is composed of a heavy and a light chain linked by a
CC       disulfide bond. Alpha-6 associates with either beta-1 or beta-4.
CC       Interacts with HPS5. Interacts with RAB21.
CC   -!- INTERACTION:
CC       P16144:ITGB4; NbExp=3; IntAct=EBI-2436548, EBI-948678;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell membrane; Lipid-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC         Comment=Additional isoforms seem to exist. There is a
CC         combination of at least four alternatively spliced domains, two
CC         extracellular (X1 and X2) and two cytoplasmic (A and B). So far
CC         detected are isoform Alpha-6X1A, isoform Alpha-6X1B and isoform
CC         Alpha-6X1X2A (minor). Experimental confirmation may be lacking
CC         for some isoforms;
CC       Name=Alpha-6X1X2B;
CC         IsoId=P23229-1; Sequence=Displayed;
CC       Name=Alpha-6X1A;
CC         IsoId=P23229-2; Sequence=VSP_002724, VSP_002725;
CC         Note=Contains a phosphoserine at position 1064;
CC       Name=Alpha-6X1B;
CC         IsoId=P23229-3; Sequence=VSP_002724;
CC       Name=Alpha-6X2A;
CC         IsoId=P23229-4; Sequence=VSP_002723, VSP_002725;
CC         Note=Contains a phosphoserine at position 1059;
CC       Name=Alpha-6X2B;
CC         IsoId=P23229-5; Sequence=VSP_002723;
CC       Name=Alpha-6X1X2A;
CC         IsoId=P23229-6; Sequence=VSP_002725;
CC         Note=Contains a phosphoserine at position 1103;
CC       Name=7;
CC         IsoId=P23229-7; Sequence=VSP_036406, VSP_002723, VSP_002725;
CC       Name=9;
CC         IsoId=P23229-9; Sequence=VSP_036407, VSP_002725;
CC   -!- TISSUE SPECIFICITY: Integrin alpha-6/beta-4 is predominantly
CC       expressed by epithelia. Isoforms containing segment X1 are
CC       ubiquitously expressed. Isoforms containing segment X1X2 are
CC       expressed in heart, kidney, placenta, colon, duodenum, myoblasts
CC       and myotubes, and in a limited number of cell lines; they are
CC       always coexpressed with the ubiquitous isoform containing segment
CC       X1. In some tissues (e.g. Salivary gland), isoforms containing
CC       cytoplasmic segment A and isoforms containing segment B are
CC       detected while in others, only isoforms containing one cytoplasmic
CC       segment are found (segment A in epidermis and segment B in
CC       kidney).
CC   -!- PTM: Isoforms containing segment A, but not segment B, are the
CC       major targets for PMA-induced phosphorylation. Phosphorylation
CC       occurs on 'Ser-1103' of isoform alpha-6X1X2A. Phosphorylation is
CC       not required for the induction of integrin alpha-6A/beta-1 high
CC       affinity but may reduce the affinity for ligand.
CC   -!- PTM: In invasive prostate cancer ITGA6 undergoes PLAU-mediated
CC       cleavage at residues Arg-634-635-Arg in a time-dependent manner
CC       enhancing cell invasion and migration in vitro.
CC   -!- PTM: Palmitoylation by DHHC3 enhances stability and cell surface
CC       expression.
CC   -!- DISEASE: Epidermolysis bullosa letalis, with pyloric atresia (EB-
CC       PA) [MIM:226730]: An autosomal recessive, frequently lethal,
CC       epidermolysis bullosa with variable involvement of skin, nails,
CC       mucosa, and with variable effects on the digestive system. It is
CC       characterized by mucocutaneous fragility, aplasia cutis congenita,
CC       and gastrointestinal atresia, which most commonly affects the
CC       pylorus. Pyloric atresia is a primary manifestation rather than a
CC       scarring process secondary to epidermolysis bullosa. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG57680.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; X53586; CAA37655.1; -; mRNA.
DR   EMBL; AF166343; AAD48469.1; -; Genomic_DNA.
DR   EMBL; AF166335; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AF166336; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AF166337; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AF166338; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AF166339; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AF166340; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AF166341; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AF166342; AAD48469.1; JOINED; Genomic_DNA.
DR   EMBL; AK294436; BAG57680.1; ALT_INIT; mRNA.
DR   EMBL; AK296496; BAG59130.1; -; mRNA.
DR   EMBL; AC078883; AAX93133.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11176.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11177.1; -; Genomic_DNA.
DR   EMBL; BC050585; AAH50585.1; -; mRNA.
DR   EMBL; BC136455; AAI36456.1; -; mRNA.
DR   EMBL; BC136456; AAI36457.1; -; mRNA.
DR   EMBL; X59512; CAA42099.1; -; mRNA.
DR   EMBL; S66213; AAB20355.1; -; mRNA.
DR   EMBL; S66196; AAB20354.1; -; mRNA.
DR   EMBL; S52135; AAB24829.1; -; Genomic_DNA.
DR   EMBL; L40385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB208842; BAD92079.1; -; mRNA.
DR   EMBL; DQ858220; ABH11650.1; -; mRNA.
DR   CCDS; CCDS2249.1; -. [P23229-2]
DR   CCDS; CCDS46451.1; -. [P23229-3]
DR   PIR; A41543; A41543.
DR   PIR; B36429; B36429.
DR   RefSeq; NP_000201.2; NM_000210.2. [P23229-2]
DR   RefSeq; NP_001073286.1; NM_001079818.1. [P23229-3]
DR   UniGene; Hs.133397; -.
DR   ProteinModelPortal; P23229; -.
DR   SMR; P23229; 24-880, 1052-1089.
DR   BioGrid; 109864; 10.
DR   IntAct; P23229; 4.
DR   MINT; MINT-5002506; -.
DR   BindingDB; P23229; -.
DR   ChEMBL; CHEMBL3716; -.
DR   PhosphoSite; P23229; -.
DR   DMDM; 519668687; -.
DR   OGP; P23229; -.
DR   MaxQB; P23229; -.
DR   PaxDb; P23229; -.
DR   PRIDE; P23229; -.
DR   Ensembl; ENST00000264106; ENSP00000264106; ENSG00000091409. [P23229-1]
DR   Ensembl; ENST00000264107; ENSP00000264107; ENSG00000091409. [P23229-2]
DR   Ensembl; ENST00000343713; ENSP00000341078; ENSG00000091409. [P23229-4]
DR   Ensembl; ENST00000375221; ENSP00000364369; ENSG00000091409. [P23229-6]
DR   Ensembl; ENST00000409080; ENSP00000386896; ENSG00000091409. [P23229-3]
DR   Ensembl; ENST00000409532; ENSP00000386614; ENSG00000091409. [P23229-7]
DR   Ensembl; ENST00000442250; ENSP00000406694; ENSG00000091409. [P23229-1]
DR   Ensembl; ENST00000458358; ENSP00000394169; ENSG00000091409. [P23229-5]
DR   GeneID; 3655; -.
DR   KEGG; hsa:3655; -.
DR   UCSC; uc002uho.1; human. [P23229-2]
DR   UCSC; uc002uhp.1; human.
DR   UCSC; uc010fqm.1; human. [P23229-9]
DR   UCSC; uc010zdy.1; human. [P23229-7]
DR   CTD; 3655; -.
DR   GeneCards; GC02P173256; -.
DR   GeneReviews; ITGA6; -.
DR   H-InvDB; HIX0023932; -.
DR   HGNC; HGNC:6142; ITGA6.
DR   HPA; CAB009009; -.
DR   HPA; HPA012696; -.
DR   HPA; HPA027582; -.
DR   MIM; 147556; gene.
DR   MIM; 226730; phenotype.
DR   neXtProt; NX_P23229; -.
DR   Orphanet; 79403; Junctional epidermolysis bullosa - pyloric atresia.
DR   PharmGKB; PA29942; -.
DR   eggNOG; NOG26407; -.
DR   HOVERGEN; HBG108011; -.
DR   InParanoid; P23229; -.
DR   KO; K06485; -.
DR   OMA; VYINQQG; -.
DR   OrthoDB; EOG7K3TK7; -.
DR   PhylomeDB; P23229; -.
DR   TreeFam; TF105391; -.
DR   Reactome; REACT_12560; Basigin interactions.
DR   Reactome; REACT_13552; Integrin cell surface interactions.
DR   Reactome; REACT_150180; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; REACT_163942; Syndecan interactions.
DR   Reactome; REACT_169262; Laminin interactions.
DR   Reactome; REACT_20537; Type I hemidesmosome assembly.
DR   SignaLink; P23229; -.
DR   ChiTaRS; ITGA6; human.
DR   GeneWiki; ITGA6; -.
DR   GenomeRNAi; 3655; -.
DR   NextBio; 14297; -.
DR   PMAP-CutDB; Q53RX7; -.
DR   PRO; PR:P23229; -.
DR   ArrayExpress; P23229; -.
DR   Bgee; P23229; -.
DR   CleanEx; HS_ITGA6; -.
DR   Genevestigator; P23229; -.
DR   GO; GO:0034676; C:alpha6-beta4 integrin complex; IEA:Ensembl.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR   GO; GO:0030056; C:hemidesmosome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0007044; P:cell-substrate junction assembly; TAS:ProtInc.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR   GO; GO:0031581; P:hemidesmosome assembly; TAS:Reactome.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0016337; P:single organismal cell-cell adhesion; IEA:Ensembl.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Epidermolysis bullosa;
KW   Glycoprotein; Integrin; Lipoprotein; Membrane; Metal-binding;
KW   Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23
FT   CHAIN        24   1130       Integrin alpha-6.
FT                                /FTId=PRO_0000016258.
FT   CHAIN        24    938       Integrin alpha-6 heavy chain (Potential).
FT                                /FTId=PRO_0000016259.
FT   CHAIN       636   1130       Processed integrin alpha-6.
FT                                /FTId=PRO_0000425742.
FT   CHAIN       942   1130       Integrin alpha-6 light chain (Potential).
FT                                /FTId=PRO_0000016260.
FT   TOPO_DOM     24   1050       Extracellular (Potential).
FT   TRANSMEM   1051   1076       Helical; (Potential).
FT   TOPO_DOM   1077   1130       Cytoplasmic (Potential).
FT   REPEAT       30     95       FG-GAP 1.
FT   REPEAT      101    166       FG-GAP 2.
FT   REPEAT      176    229       FG-GAP 3.
FT   REPEAT      283    340       FG-GAP 4.
FT   REPEAT      341    402       FG-GAP 5.
FT   REPEAT      403    458       FG-GAP 6.
FT   REPEAT      459    518       FG-GAP 7.
FT   CA_BIND     363    371       Potential.
FT   CA_BIND     425    433       Potential.
FT   CA_BIND     480    488       Potential.
FT   REGION     1077   1083       Interaction with HPS5.
FT   MOTIF      1079   1083       GFFKR motif.
FT   SITE        634    635       Cleavage; by PLAU in invasive prostate
FT                                cancer.
FT   LIPID      1078   1078       S-palmitoyl cysteine; by DHHC3.
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    223    223       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    323    323       N-linked (GlcNAc...).
FT   CARBOHYD    409    409       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    770    770       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    787    787       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    930    930       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    966    966       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    997    997       N-linked (GlcNAc...).
FT   DISULFID     86     94       By similarity.
FT   DISULFID    131    154       By similarity.
FT   DISULFID    175    188       By similarity.
FT   DISULFID    528    535       By similarity.
FT   DISULFID    541    601       By similarity.
FT   DISULFID    665    671       By similarity.
FT   DISULFID    765    776       By similarity.
FT   DISULFID    920    967       Interchain (between heavy and light
FT                                chains) (By similarity).
FT   DISULFID    973    978       By similarity.
FT   VAR_SEQ       1    114       Missing (in isoform 7).
FT                                /FTId=VSP_036406.
FT   VAR_SEQ     215    258       Missing (in isoform Alpha-6X2A, isoform
FT                                Alpha-6X2B and isoform 7).
FT                                /FTId=VSP_002723.
FT   VAR_SEQ     259    297       Missing (in isoform Alpha-6X1A and
FT                                isoform Alpha-6X1B).
FT                                /FTId=VSP_002724.
FT   VAR_SEQ     918    932       Missing (in isoform 9).
FT                                /FTId=VSP_036407.
FT   VAR_SEQ    1084   1130       SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWN
FT                                ENESYS -> NKKDHYDATYHKAEIHAQPSDKERLTSDA
FT                                (in isoform Alpha-6X1A, isoform Alpha-
FT                                6X2A, isoform Alpha-6X1X2A, isoform 7 and
FT                                isoform 9).
FT                                /FTId=VSP_002725.
FT   CONFLICT     69     69       A -> G (in Ref. 1; CAA37655 and 8;
FT                                CAA42099).
FT   CONFLICT    419    419       A -> T (in Ref. 4; BAG59130 and 7;
FT                                AAI36456/AAI36457).
FT   CONFLICT    501    501       F -> L (in Ref. 8; CAA42099).
FT   CONFLICT    805    805       D -> Y (in Ref. 1; CAA37655 and 3;
FT                                AAD48469).
FT   CONFLICT   1125   1125       E -> R (in Ref. 1; AAB20355).
SQ   SEQUENCE   1130 AA;  126606 MW;  B53712888B7FE3B6 CRC64;
     MAAAGQLCLL YLSAGLLSRL GAAFNLDTRE DNVIRKYGDP GSLFGFSLAM HWQLQPEDKR
     LLLVGAPRAE ALPLQRANRT GGLYSCDITA RGPCTRIEFD NDADPTSESK EDQWMGVTVQ
     SQGPGGKVVT CAHRYEKRQH VNTKQESRDI FGRCYVLSQN LRIEDDMDGG DWSFCDGRLR
     GHEKFGSCQQ GVAATFTKDF HYIVFGAPGT YNWKGIVRVE QKNNTFFDMN IFEDGPYEVG
     GETEHDESLV PVPANSYLGL LFLTSVSYTD PDQFVYKTRP PREQPDTFPD VMMNSYLGFS
     LDSGKGIVSK DEITFVSGAP RANHSGAVVL LKRDMKSAHL LPEHIFDGEG LASSFGYDVA
     VVDLNKDGWQ DIVIGAPQYF DRDGEVGGAV YVYMNQQGRW NNVKPIRLNG TKDSMFGIAV
     KNIGDINQDG YPDIAVGAPY DDLGKVFIYH GSANGINTKP TQVLKGISPY FGYSIAGNMD
     LDRNSYPDVA VGSLSDSVTI FRSRPVINIQ KTITVTPNRI DLRQKTACGA PSGICLQVKS
     CFEYTANPAG YNPSISIVGT LEAEKERRKS GLSSRVQFRN QGSEPKYTQE LTLKRQKQKV
     CMEETLWLQD NIRDKLRPIP ITASVEIQEP SSRRRVNSLP EVLPILNSDE PKTAHIDVHF
     LKEGCGDDNV CNSNLKLEYK FCTREGNQDK FSYLPIQKGV PELVLKDQKD IALEITVTNS
     PSNPRNPTKD GDDAHEAKLI ATFPDTLTYS AYRELRAFPE KQLSCVANQN GSQADCELGN
     PFKRNSNVTF YLVLSTTEVT FDTPDLDINL KLETTSNQDN LAPITAKAKV VIELLLSVSG
     VAKPSQVYFG GTVVGEQAMK SEDEVGSLIE YEFRVINLGK PLTNLGTATL NIQWPKEISN
     GKWLLYLVKV ESKGLEKVTC EPQKEINSLN LTESHNSRKK REITEKQIDD NRKFSLFAER
     KYQTLNCSVN VNCVNIRCPL RGLDSKASLI LRSRLWNSTF LEEYSKLNYL DILMRAFIDV
     TAAAENIRLP NAGTQVRVTV FPSKTVAQYS GVPWWIILVA ILAGILMLAL LVFILWKCGF
     FKRSRYDDSV PRYHAVRIRK EEREIKDEKY IDNLEKKQWI TKWNENESYS
//
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