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Integrin alpha-6 (CD49 antigen-like family member F) (VLA-6) (CD antigen CD49f) [Cleaved into: Integrin alpha-6 heavy chain; Integrin alpha-6 light chain; Processed integrin alpha-6 (Alpha6p)]

 ITA6_HUMAN              Reviewed;        1130 AA.
P23229; B2RMU9; B4DG69; B4DKB8; C4AM96; G5E9H1; Q08443; Q0MRC7;
Q14646; Q16508; Q53RX7; Q59HB7; Q86VL6; Q9UCT1; Q9UN03;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 5.
22-NOV-2017, entry version 195.
RecName: Full=Integrin alpha-6;
AltName: Full=CD49 antigen-like family member F;
AltName: Full=VLA-6;
AltName: CD_antigen=CD49f;
Contains:
RecName: Full=Integrin alpha-6 heavy chain;
Contains:
RecName: Full=Integrin alpha-6 light chain;
Contains:
RecName: Full=Processed integrin alpha-6;
Short=Alpha6p;
Flags: Precursor;
Name=ITGA6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-6X1A).
TISSUE=Pancreas;
PubMed=1976638; DOI=10.1083/jcb.111.4.1593;
Tamura R.N., Rozzo C., Starr L., Chambers J., Reichardt L.F.,
Cooper H.M., Quaranta V.;
"Epithelial integrin alpha 6 beta 4: complete primary structure of
alpha 6 and variant forms of beta 4.";
J. Cell Biol. 111:1593-1604(1990).
[2]
SEQUENCE REVISION TO 78 AND 362.
Quaranta V.;
Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-6X1A).
Pulkkinen L., Uitto J.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 266-1130 (ISOFORM ALPHA-6X1X2A).
TISSUE=Amygdala, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-6X1A), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 412-1130 (ISOFORM 9).
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-6X1A).
TISSUE=Keratinocyte;
PubMed=2070796; DOI=10.1111/j.1432-1033.1991.tb16140.x;
Hogervorst F., Kuikman I., Geurts van Kessel A., Sonnenberg A.;
"Molecular cloning of the human alpha 6 integrin subunit. Alternative
splicing of alpha 6 mRNA and chromosomal localization of the alpha 6
and beta 4 genes.";
Eur. J. Biochem. 199:425-433(1991).
[9]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-6X1A AND
ALPHA-6X1B).
PubMed=1946438; DOI=10.1073/pnas.88.22.10183;
Tamura R.N., Cooper H.M., Collo G., Quaranta V.;
"Cell type-specific integrin variants with alternative alpha chain
cytoplasmic domains.";
Proc. Natl. Acad. Sci. U.S.A. 88:10183-10187(1991).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 748-849.
PubMed=1476731;
Starr L., Quaranta V.;
"An efficient and reliable method for cloning PCR-amplification
products: a survey of point mutations in integrin cDNA.";
BioTechniques 13:612-618(1992).
[11]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-6X1A).
PubMed=8496190;
Shaw L.M., Lotz M.M., Mercurio A.M.;
"Inside-out integrin signaling in macrophages. Analysis of the role of
the alpha 6A beta 1 and alpha 6B beta 1 integrin variants in laminin
adhesion by cDNA expression in an alpha 6 integrin-deficient
macrophage cell line.";
J. Biol. Chem. 268:11401-11408(1993).
[12]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=8253814;
Ziober B.L., Vu M.P., Waleh N., Crawford J., Lin C.-S., Kramer R.H.;
"Alternative extracellular and cytoplasmic domains of the integrin
alpha 7 subunit are differentially expressed during development.";
J. Biol. Chem. 268:26773-26783(1993).
[13]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymphoma;
PubMed=7583007;
Delwel G.O., Kuikman I., Sonnenberg A.;
"An alternatively spliced exon in the extracellular domain of the
human alpha 6 integrin subunit -- functional analysis of the alpha 6
integrin variants.";
Cell Adhes. Commun. 3:143-161(1995).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-1130 (ISOFORM
ALPHA-6X1X2B).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[15]
PROTEIN SEQUENCE OF 24-44.
PubMed=2649503;
Hemler M.E., Crouse C., Sonnenberg A.;
"Association of the VLA alpha 6 subunit with a novel protein. A
possible alternative to the common VLA beta 1 subunit on certain cell
lines.";
J. Biol. Chem. 264:6529-6535(1989).
[16]
PROTEIN SEQUENCE OF 24-46.
PubMed=2542022;
Kajiji S., Tamura R.N., Quaranta V.;
"A novel integrin (alpha E beta 4) from human epithelial cells
suggests a fourth family of integrin adhesion receptors.";
EMBO J. 8:673-680(1989).
[17]
PROTEIN SEQUENCE OF 24-36.
TISSUE=Platelet;
PubMed=1953640; DOI=10.1042/bj2790419;
Catimel B., Parmentier S., Leung L.L., McGregor J.L.;
"Separation of important new platelet glycoproteins (GPIa, GPIc,
GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal
antibodies and gas-phase sequencing.";
Biochem. J. 279:419-425(1991).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 1001-1130.
Dydensborg A.B., Herring E., Beaulieu J.-F.;
"Integrin alpha6Abeta4 in human colon cancer.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[19]
PHOSPHORYLATION AT SER-1059 (ISOFORM ALPHA-6X2A), PHOSPHORYLATION AT
SER-1064 (ISOFORM ALPHA-6X1A), AND PHOSPHORYLATION AT SER-1103
(ISOFORM ALPHA-6X1X2A).
PubMed=8360143;
Hogervorst F., Kuikman I., Noteboom E., Sonnenberg A.;
"The role of phosphorylation in activation of the alpha 6A beta 1
laminin receptor.";
J. Biol. Chem. 268:18427-18430(1993).
[20]
CHARACTERIZATION, AND TISSUE SPECIFICITY.
PubMed=7681434; DOI=10.1083/jcb.121.1.179;
Hogervorst F., Admiraal L.G., Niessen C., Kuikman I., Janssen H.,
Daams H., Sonnenberg A.;
"Biochemical characterization and tissue distribution of the A and B
variants of the integrin alpha 6 subunit.";
J. Cell Biol. 121:179-191(1993).
[21]
PALMITOYLATION AT CYS-1078.
PubMed=15611341; DOI=10.1083/jcb.200404100;
Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.;
"Palmitoylation supports assembly and function of integrin-tetraspanin
complexes.";
J. Cell Biol. 167:1231-1240(2004).
[22]
INTERACTION WITH RAB21.
PubMed=16754960; DOI=10.1083/jcb.200509019;
Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
Ivaska J.;
"Small GTPase Rab21 regulates cell adhesion and controls endosomal
traffic of beta1-integrins.";
J. Cell Biol. 173:767-780(2006).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-997.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[25]
PROTEOLYTIC PROCESSING.
PubMed=17303120; DOI=10.1016/j.yexcr.2007.01.006;
Pawar S.C., Demetriou M.C., Nagle R.B., Bowden G.T., Cress A.E.;
"Integrin alpha6 cleavage: a novel modification to modulate cell
migration.";
Exp. Cell Res. 313:1080-1089(2007).
[26]
FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1
AND ERBB3.
PubMed=20682778; DOI=10.1074/jbc.M110.113878;
Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
Wang B., Takada Y.K., Takada Y.;
"Direct binding of the EGF-like domain of neuregulin-1 to integrins
({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
signaling.";
J. Biol. Chem. 285:31388-31398(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
PALMITOYLATION AT CYS-1078 BY DHHC3, AND SUBCELLULAR LOCATION.
PubMed=22314500; DOI=10.1007/s00018-012-0924-6;
Sharma C., Rabinovitz I., Hemler M.E.;
"Palmitoylation by DHHC3 is critical for the function, expression, and
stability of integrin alpha6beta4.";
Cell. Mol. Life Sci. 69:2233-2244(2012).
[29]
FUNCTION, BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH IGF1
AND IGF1R.
PubMed=22351760; DOI=10.1074/jbc.M111.304170;
Fujita M., Ieguchi K., Davari P., Yamaji S., Taniguchi Y.,
Sekiguchi K., Takada Y.K., Takada Y.;
"Cross-talk between integrin alpha6beta4 and insulin-like growth
factor-1 receptor (IGF1R) through direct alpha6beta4 binding to IGF1
and subsequent alpha6beta4-IGF1-IGF1R ternary complex formation in
anchorage-independent conditions.";
J. Biol. Chem. 287:12491-12500(2012).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Integrin alpha-6/beta-1 is a receptor for laminin on
platelets. Integrin alpha-6/beta-4 is a receptor for laminin in
epithelial cells and it plays a critical structural role in the
hemidesmosome (By similarity). ITGA6:ITGB4 binds to NRG1 (via EGF
domain) and this binding is essential for NRG1-ERBB signaling
(PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is
essential for IGF1 signaling (PubMed:22351760).
{ECO:0000250|UniProtKB:Q61739, ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:22351760}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit is composed of a heavy and a light chain linked by a
disulfide bond. Alpha-6 associates with either beta-1 or beta-4.
Interacts with HPS5. Interacts with RAB21. ITGA6:ITGB4 is found in
a ternary complex with NRG1 and ERBB3 (PubMed:20682778).
ITGA6:ITGB4 is found in a ternary complex with IGF1 and IGF1R
(PubMed:22351760). Interacts with ADAM9 (By similarity).
{ECO:0000250|UniProtKB:Q61739, ECO:0000269|PubMed:16754960,
ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760}.
-!- INTERACTION:
P16144:ITGB4; NbExp=3; IntAct=EBI-2436548, EBI-948678;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22314500};
Single-pass type I membrane protein {ECO:0000255}. Cell membrane
{ECO:0000269|PubMed:22314500}; Lipid-anchor
{ECO:0000269|PubMed:22314500}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist. There is a
combination of at least four alternatively spliced domains, two
extracellular (X1 and X2) and two cytoplasmic (A and B). So far
detected are isoform Alpha-6X1A, isoform Alpha-6X1B and isoform
Alpha-6X1X2A (minor). Experimental confirmation may be lacking
for some isoforms.;
Name=Alpha-6X1X2B;
IsoId=P23229-1; Sequence=Displayed;
Name=Alpha-6X1A;
IsoId=P23229-2; Sequence=VSP_002724, VSP_002725;
Note=Contains a phosphoserine at position 1064.
{ECO:0000269|PubMed:8360143};
Name=Alpha-6X1B;
IsoId=P23229-3; Sequence=VSP_002724;
Name=Alpha-6X2A;
IsoId=P23229-4; Sequence=VSP_002723, VSP_002725;
Note=Contains a phosphoserine at position 1059.
{ECO:0000269|PubMed:8360143};
Name=Alpha-6X2B;
IsoId=P23229-5; Sequence=VSP_002723;
Name=Alpha-6X1X2A;
IsoId=P23229-6; Sequence=VSP_002725;
Note=Contains a phosphoserine at position 1103.
{ECO:0000269|PubMed:8360143};
Name=7;
IsoId=P23229-7; Sequence=VSP_036406, VSP_002723, VSP_002725;
Name=9;
IsoId=P23229-9; Sequence=VSP_036407, VSP_002725;
-!- TISSUE SPECIFICITY: Integrin alpha-6/beta-4 is predominantly
expressed by epithelia. Isoforms containing segment X1 are
ubiquitously expressed. Isoforms containing segment X1X2 are
expressed in heart, kidney, placenta, colon, duodenum, myoblasts
and myotubes, and in a limited number of cell lines; they are
always coexpressed with the ubiquitous isoform containing segment
X1. In some tissues (e.g. Salivary gland), isoforms containing
cytoplasmic segment A and isoforms containing segment B are
detected while in others, only isoforms containing one cytoplasmic
segment are found (segment A in epidermis and segment B in
kidney). {ECO:0000269|PubMed:7681434}.
-!- PTM: Isoforms containing segment A, but not segment B, are the
major targets for PMA-induced phosphorylation. Phosphorylation
occurs on 'Ser-1103' of isoform alpha-6X1X2A. Phosphorylation is
not required for the induction of integrin alpha-6A/beta-1 high
affinity but may reduce the affinity for ligand.
-!- PTM: In invasive prostate cancer ITGA6 undergoes PLAU-mediated
cleavage at residues Arg-634-635-Arg in a time-dependent manner
enhancing cell invasion and migration in vitro.
{ECO:0000269|PubMed:17303120}.
-!- PTM: Palmitoylation by DHHC3 enhances stability and cell surface
expression. {ECO:0000269|PubMed:15611341,
ECO:0000269|PubMed:22314500}.
-!- DISEASE: Epidermolysis bullosa letalis, with pyloric atresia (EB-
PA) [MIM:226730]: An autosomal recessive, frequently lethal,
epidermolysis bullosa with variable involvement of skin, nails,
mucosa, and with variable effects on the digestive system. It is
characterized by mucocutaneous fragility, aplasia cutis congenita,
and gastrointestinal atresia, which most commonly affects the
pylorus. Pyloric atresia is a primary manifestation rather than a
scarring process secondary to epidermolysis bullosa. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG57680.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X53586; CAA37655.1; -; mRNA.
EMBL; AF166343; AAD48469.1; -; Genomic_DNA.
EMBL; AF166335; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AF166336; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AF166337; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AF166338; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AF166339; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AF166340; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AF166341; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AF166342; AAD48469.1; JOINED; Genomic_DNA.
EMBL; AK294436; BAG57680.1; ALT_INIT; mRNA.
EMBL; AK296496; BAG59130.1; -; mRNA.
EMBL; AC078883; AAX93133.1; -; Genomic_DNA.
EMBL; CH471058; EAX11176.1; -; Genomic_DNA.
EMBL; CH471058; EAX11177.1; -; Genomic_DNA.
EMBL; BC050585; AAH50585.1; -; mRNA.
EMBL; BC136455; AAI36456.1; -; mRNA.
EMBL; BC136456; AAI36457.1; -; mRNA.
EMBL; X59512; CAA42099.1; -; mRNA.
EMBL; S66213; AAB20355.1; -; mRNA.
EMBL; S66196; AAB20354.1; -; mRNA.
EMBL; S52135; AAB24829.1; -; Genomic_DNA.
EMBL; L40385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB208842; BAD92079.1; -; mRNA.
EMBL; DQ858220; ABH11650.1; -; mRNA.
CCDS; CCDS2249.1; -. [P23229-2]
CCDS; CCDS46451.1; -. [P23229-3]
CCDS; CCDS82534.1; -. [P23229-7]
PIR; A41543; A41543.
PIR; B36429; B36429.
RefSeq; NP_000201.2; NM_000210.3. [P23229-2]
RefSeq; NP_001073286.1; NM_001079818.2. [P23229-3]
RefSeq; NP_001303235.1; NM_001316306.1. [P23229-7]
UniGene; Hs.133397; -.
ProteinModelPortal; P23229; -.
BioGrid; 109864; 45.
CORUM; P23229; -.
IntAct; P23229; 6.
MINT; MINT-5002506; -.
STRING; 9606.ENSP00000386896; -.
ChEMBL; CHEMBL3716; -.
TCDB; 8.A.54.1.2; the integrin (integrin) family.
iPTMnet; P23229; -.
PhosphoSitePlus; P23229; -.
SwissPalm; P23229; -.
BioMuta; ITGA6; -.
DMDM; 519668687; -.
OGP; P23229; -.
EPD; P23229; -.
MaxQB; P23229; -.
PaxDb; P23229; -.
PeptideAtlas; P23229; -.
PRIDE; P23229; -.
Ensembl; ENST00000264107; ENSP00000264107; ENSG00000091409. [P23229-2]
Ensembl; ENST00000409080; ENSP00000386896; ENSG00000091409. [P23229-3]
Ensembl; ENST00000409532; ENSP00000386614; ENSG00000091409. [P23229-7]
Ensembl; ENST00000442250; ENSP00000406694; ENSG00000091409. [P23229-1]
Ensembl; ENST00000458358; ENSP00000394169; ENSG00000091409. [P23229-5]
GeneID; 3655; -.
KEGG; hsa:3655; -.
UCSC; uc002uho.2; human. [P23229-1]
CTD; 3655; -.
DisGeNET; 3655; -.
EuPathDB; HostDB:ENSG00000091409.14; -.
GeneCards; ITGA6; -.
GeneReviews; ITGA6; -.
H-InvDB; HIX0023932; -.
HGNC; HGNC:6142; ITGA6.
HPA; CAB009009; -.
HPA; HPA012696; -.
HPA; HPA027582; -.
MalaCards; ITGA6; -.
MIM; 147556; gene.
MIM; 226730; phenotype.
neXtProt; NX_P23229; -.
OpenTargets; ENSG00000091409; -.
Orphanet; 79403; Junctional epidermolysis bullosa - pyloric atresia.
PharmGKB; PA29942; -.
eggNOG; ENOG410IPBB; Eukaryota.
eggNOG; ENOG410XVGZ; LUCA.
GeneTree; ENSGT00760000118782; -.
HOVERGEN; HBG108011; -.
InParanoid; P23229; -.
KO; K06485; -.
OMA; YVYINQQ; -.
OrthoDB; EOG091G012D; -.
PhylomeDB; P23229; -.
TreeFam; TF105391; -.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-446107; Type I hemidesmosome assembly.
SignaLink; P23229; -.
SIGNOR; P23229; -.
ChiTaRS; ITGA6; human.
GeneWiki; ITGA6; -.
GenomeRNAi; 3655; -.
PMAP-CutDB; Q53RX7; -.
PRO; PR:P23229; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000091409; -.
CleanEx; HS_ITGA6; -.
ExpressionAtlas; P23229; baseline and differential.
Genevisible; P23229; HS.
GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030056; C:hemidesmosome; IEA:Ensembl.
GO; GO:0034676; C:integrin alpha6-beta4 complex; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0043236; F:laminin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0038132; F:neuregulin binding; IDA:UniProtKB.
GO; GO:0097186; P:amelogenesis; IMP:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0007044; P:cell-substrate junction assembly; TAS:ProtInc.
GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
GO; GO:0010668; P:ectodermal cell differentiation; IEP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
GO; GO:0031581; P:hemidesmosome assembly; TAS:Reactome.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0035878; P:nail development; IMP:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:Ensembl.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0072001; P:renal system development; IMP:UniProtKB.
GO; GO:0043588; P:skin development; IMP:UniProtKB.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR032695; Integrin_dom_sf.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell adhesion; Cell membrane;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Epidermolysis bullosa;
Glycoprotein; Integrin; Lipoprotein; Membrane; Metal-binding;
Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000269|PubMed:1953640,
ECO:0000269|PubMed:2542022,
ECO:0000269|PubMed:2649503}.
CHAIN 24 1130 Integrin alpha-6.
/FTId=PRO_0000016258.
CHAIN 24 938 Integrin alpha-6 heavy chain.
{ECO:0000255}.
/FTId=PRO_0000016259.
CHAIN 636 1130 Processed integrin alpha-6.
/FTId=PRO_0000425742.
CHAIN 942 1130 Integrin alpha-6 light chain.
{ECO:0000255}.
/FTId=PRO_0000016260.
TOPO_DOM 24 1050 Extracellular. {ECO:0000255}.
TRANSMEM 1051 1076 Helical. {ECO:0000255}.
TOPO_DOM 1077 1130 Cytoplasmic. {ECO:0000255}.
REPEAT 30 95 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 101 166 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 176 229 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 283 339 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 340 402 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 403 458 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 459 518 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 363 371 {ECO:0000255}.
CA_BIND 425 433 {ECO:0000255}.
CA_BIND 480 488 {ECO:0000255}.
REGION 1077 1083 Interaction with HPS5.
MOTIF 1079 1083 GFFKR motif.
SITE 634 635 Cleavage; by PLAU in invasive prostate
cancer. {ECO:0000269|PubMed:17303120}.
LIPID 1078 1078 S-palmitoyl cysteine; by DHHC3.
{ECO:0000269|PubMed:15611341,
ECO:0000269|PubMed:22314500}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 770 770 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 787 787 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 930 930 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 966 966 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 997 997 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 86 94 {ECO:0000250}.
DISULFID 131 154 {ECO:0000250}.
DISULFID 175 188 {ECO:0000250}.
DISULFID 528 535 {ECO:0000250}.
DISULFID 541 601 {ECO:0000250}.
DISULFID 665 671 {ECO:0000250}.
DISULFID 765 776 {ECO:0000250}.
DISULFID 920 967 Interchain (between heavy and light
chains). {ECO:0000250}.
DISULFID 973 978 {ECO:0000250}.
VAR_SEQ 1 114 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036406.
VAR_SEQ 215 258 Missing (in isoform Alpha-6X2A, isoform
Alpha-6X2B and isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_002723.
VAR_SEQ 259 297 Missing (in isoform Alpha-6X1A and
isoform Alpha-6X1B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1976638}.
/FTId=VSP_002724.
VAR_SEQ 918 932 Missing (in isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036407.
VAR_SEQ 1084 1130 SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWN
ENESYS -> NKKDHYDATYHKAEIHAQPSDKERLTSDA
(in isoform Alpha-6X1A, isoform Alpha-
6X2A, isoform Alpha-6X1X2A, isoform 7 and
isoform 9). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1976638}.
/FTId=VSP_002725.
CONFLICT 69 69 A -> G (in Ref. 1; CAA37655 and 8;
CAA42099). {ECO:0000305}.
CONFLICT 419 419 A -> T (in Ref. 4; BAG59130 and 7;
AAI36456/AAI36457). {ECO:0000305}.
CONFLICT 501 501 F -> L (in Ref. 8; CAA42099).
{ECO:0000305}.
CONFLICT 805 805 D -> Y (in Ref. 1; CAA37655 and 3;
AAD48469). {ECO:0000305}.
CONFLICT 1125 1125 E -> R (in Ref. 1; AAB20355).
{ECO:0000305}.
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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