ITA6_HUMAN
ID ITA6_HUMAN Reviewed; 1130 AA.
AC P23229; B2RMU9; B4DG69; B4DKB8; C4AM96; G5E9H1; Q08443; Q0MRC7; Q14646;
AC Q16508; Q53RX7; Q59HB7; Q86VL6; Q9UCT1; Q9UN03;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 5.
DT 03-AUG-2022, entry version 224.
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 {ECO:0000303|PubMed:11359780};
DE Flags: Precursor;
GN Name=ITGA6;
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 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., Cooper H.M.,
RA Quaranta V.;
RT "Epithelial integrin alpha 6 beta 4: complete primary structure of alpha 6
RT 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 SEQUENCE
RP [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., 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 [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., 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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-6X1A), AND NUCLEOTIDE
RP 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 project:
RT 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 and
RT beta 4 genes.";
RL Eur. J. Biochem. 199:425-433(1991).
RN [9]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-6X1A AND 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 products: a
RT 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; DOI=10.1016/s0021-9258(18)82138-x;
RA Shaw L.M., Lotz M.M., Mercurio A.M.;
RT "Inside-out integrin signaling in macrophages. Analysis of the role of the
RT alpha 6A beta 1 and alpha 6B beta 1 integrin variants in laminin adhesion
RT by cDNA expression in an alpha 6 integrin-deficient 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; DOI=10.1016/s0021-9258(19)74380-4;
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 alpha 7
RT 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; DOI=10.3109/15419069509081283;
RA Delwel G.O., Kuikman I., Sonnenberg A.;
RT "An alternatively spliced exon in the extracellular domain of the human
RT alpha 6 integrin subunit -- functional analysis of the alpha 6 integrin
RT variants.";
RL Cell Adhes. Commun. 3:143-161(1995).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-1130 (ISOFORM 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; DOI=10.1016/s0021-9258(18)83380-4;
RA Hemler M.E., Crouse C., Sonnenberg A.;
RT "Association of the VLA alpha 6 subunit with a novel protein. A possible
RT alternative to the common VLA beta 1 subunit on certain cell lines.";
RL J. Biol. Chem. 264:6529-6535(1989).
RN [16]
RP PROTEIN SEQUENCE OF 24-46.
RX PubMed=2542022; DOI=10.1002/j.1460-2075.1989.tb03425.x;
RA Kajiji S., Tamura R.N., Quaranta V.;
RT "A novel integrin (alpha E beta 4) from human epithelial cells suggests a
RT 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; DOI=10.1042/bj2790419;
RA Catimel B., Parmentier S., Leung L.L., McGregor J.L.;
RT "Separation of important new platelet glycoproteins (GPIa, GPIc, GPIc*,
RT GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal antibodies
RT 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), PHOSPHORYLATION AT
RP SER-1064 (ISOFORM ALPHA-6X1A), AND PHOSPHORYLATION AT SER-1103 (ISOFORM
RP ALPHA-6X1X2A).
RX PubMed=8360143; DOI=10.1016/s0021-9258(17)46641-5;
RA Hogervorst F., Kuikman I., Noteboom E., Sonnenberg A.;
RT "The role of phosphorylation in activation of the alpha 6A beta 1 laminin
RT 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., Daams H.,
RA 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 INVOLVEMENT IN JEB6.
RX PubMed=9185503; DOI=10.1172/jci119474;
RA Ruzzi L., Gagnoux-Palacios L., Pinola M., Belli S., Meneguzzi G.,
RA D'Alessio M., Zambruno G.;
RT "A homozygous mutation in the integrin alpha6 gene in junctional
RT epidermolysis bullosa with pyloric atresia.";
RL J. Clin. Invest. 99:2826-2831(1997).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
RX PubMed=11359780; DOI=10.1074/jbc.m102811200;
RA Davis T.L., Rabinovitz I., Futscher B.W., Schnoelzer M., Burger F., Liu Y.,
RA Kulesz-Martin M., Cress A.E.;
RT "Identification of a novel structural variant of the alpha 6 integrin.";
RL J. Biol. Chem. 276:26099-26106(2001).
RN [23]
RP PROTEOLYTIC PROCESSING, AND TISSUE SPECIFICITY.
RX PubMed=15023541; DOI=10.1016/j.yexcr.2003.11.023;
RA Demetriou M.C., Pennington M.E., Nagle R.B., Cress A.E.;
RT "Extracellular alpha 6 integrin cleavage by urokinase-type plasminogen
RT activator in human prostate cancer.";
RL Exp. Cell Res. 294:550-558(2004).
RN [24]
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 [25]
RP INTERACTION WITH MDK.
RX PubMed=15466886; DOI=10.1242/jcs.01423;
RA Muramatsu H., Zou P., Suzuki H., Oda Y., Chen G.Y., Sakaguchi N.,
RA Sakuma S., Maeda N., Noda M., Takada Y., Muramatsu T.;
RT "alpha4beta1- and alpha6beta1-integrins are functional receptors for
RT midkine, a heparin-binding growth factor.";
RL J. Cell Sci. 117:5405-5415(2004).
RN [26]
RP INTERACTION WITH RAB21.
RX PubMed=16754960; DOI=10.1083/jcb.200509019;
RA Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M.,
RA Ivaska J.;
RT "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic
RT of beta1-integrins.";
RL J. Cell Biol. 173:767-780(2006).
RN [27]
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 [28]
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 multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [29]
RP PROTEOLYTIC PROCESSING.
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 [30]
RP FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1 AND
RP ERBB3.
RX PubMed=20682778; DOI=10.1074/jbc.m110.113878;
RA Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
RA Wang B., Takada Y.K., Takada Y.;
RT "Direct binding of the EGF-like domain of neuregulin-1 to integrins
RT ({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
RT signaling.";
RL J. Biol. Chem. 285:31388-31398(2010).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
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).
RN [33]
RP FUNCTION, BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH IGF1 AND
RP IGF1R.
RX PubMed=22351760; DOI=10.1074/jbc.m111.304170;
RA Fujita M., Ieguchi K., Davari P., Yamaji S., Taniguchi Y., Sekiguchi K.,
RA Takada Y.K., Takada Y.;
RT "Cross-talk between integrin alpha6beta4 and insulin-like growth factor-1
RT receptor (IGF1R) through direct alpha6beta4 binding to IGF1 and subsequent
RT alpha6beta4-IGF1-IGF1R ternary complex formation in anchorage-independent
RT conditions.";
RL J. Biol. Chem. 287:12491-12500(2012).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [35]
RP INVOLVEMENT IN JEB6.
RX PubMed=27607025; DOI=10.1111/1346-8138.13575;
RA Masunaga T., Ogawa J., Akiyama M., Nishikawa T., Shimizu H., Ishiko A.;
RT "Compound heterozygosity for novel splice site mutations of ITGA6 in lethal
RT junctional epidermolysis bullosa with pyloric atresia.";
RL J. Dermatol. 44:160-166(2017).
RN [36]
RP FUNCTION, AND INTERACTION WITH IGF2.
RX PubMed=28873464; DOI=10.1371/journal.pone.0184285;
RA Cedano Prieto D.M., Cheng Y., Chang C.C., Yu J., Takada Y.K., Takada Y.;
RT "Direct integrin binding to insulin-like growth factor-2 through the C-
RT domain is required for insulin-like growth factor receptor type 1 (IGF1R)
RT signaling.";
RL PLoS ONE 12:E0184285-E0184285(2017).
CC -!- FUNCTION: Integrin alpha-6/beta-1 (ITGA6:ITGB1) is a receptor for
CC laminin on platelets (By similarity). Integrin alpha-6/beta-1
CC (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion
CC (By similarity). Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor
CC for laminin in epithelial cells and it plays a critical structural role
CC in the hemidesmosome (By similarity). ITGA6:ITGB4 binds to NRG1 (via
CC EGF domain) and this binding is essential for NRG1-ERBB signaling
CC (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is
CC essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to
CC IGF2 and this binding is essential for IGF2 signaling
CC (PubMed:28873464). {ECO:0000250|UniProtKB:Q61739,
CC ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760,
CC ECO:0000269|PubMed:28873464}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chain linked by a disulfide bond (By
CC similarity). Alpha-6 associates with either beta-1 (ITGB1) or beta-4
CC (ITGB4) to form ITGA6:ITGB1 and ITGA6:ITGB4, respectively (By
CC similarity). ITGA6:ITGB1 is found in a complex with CD9; interaction
CC takes place in oocytes and is involved in sperm-egg fusion (By
CC similarity). ITGA6:ITGB4 is found in a ternary complex with NRG1 and
CC ERBB3 (PubMed:20682778). ITGA6:ITGB4 is found in a ternary complex with
CC IGF1 and IGF1R (PubMed:22351760). ITGA6:ITGB4 interacts with IGF2
CC (PubMed:28873464). Interacts with ADAM9 (By similarity). Interacts with
CC RAB21 (PubMed:16754960). Interacts with MDK (PubMed:15466886).
CC ITGA6:ITGB1 interacts with MDK; this interaction mediates MDK-induced
CC neurite outgrowth (PubMed:15466886). {ECO:0000250|UniProtKB:Q61739,
CC ECO:0000269|PubMed:15466886, ECO:0000269|PubMed:16754960,
CC ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760,
CC ECO:0000269|PubMed:28873464}.
CC -!- INTERACTION:
CC P23229; P16144: ITGB4; NbExp=3; IntAct=EBI-2436548, EBI-948678;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22314500};
CC Single-pass type I membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:22314500}; Lipid-anchor
CC {ECO:0000269|PubMed:22314500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist. There is a combination of
CC at least four alternatively spliced domains, two extracellular (X1
CC and X2) and two cytoplasmic (A and B). So far detected are isoform
CC Alpha-6X1A, isoform Alpha-6X1B and isoform Alpha-6X1X2A (minor).
CC Experimental confirmation may be lacking 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 Name=Alpha-6X1B;
CC IsoId=P23229-3; Sequence=VSP_002724;
CC Name=Alpha-6X2A;
CC IsoId=P23229-4; Sequence=VSP_002723, VSP_002725;
CC Name=Alpha-6X2B;
CC IsoId=P23229-5; Sequence=VSP_002723;
CC Name=Alpha-6X1X2A;
CC IsoId=P23229-6; Sequence=VSP_002725;
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 expressed
CC by epithelia. Isoforms containing segment X1 are ubiquitously
CC expressed. Isoforms containing segment X1X2 are expressed in heart,
CC kidney, placenta, colon, duodenum, myoblasts and myotubes, and in a
CC limited number of cell lines; they are always coexpressed with the
CC ubiquitous isoform containing segment X1. In some tissues (e.g.
CC Salivary gland), isoforms containing cytoplasmic segment A and isoforms
CC containing segment B are detected while in others, only isoforms
CC containing one cytoplasmic segment are found (segment A in epidermis
CC and segment B in kidney). Processed integrin alpha-6: Expressed at low
CC levels in normal prostate tissue with elevated levels in prostate
CC cancer tissue (at protein level) (PubMed:15023541).
CC {ECO:0000269|PubMed:15023541, ECO:0000269|PubMed:7681434}.
CC -!- PTM: Isoforms containing segment A, but not segment B, are the major
CC targets for PMA-induced phosphorylation. Phosphorylation occurs on
CC 'Ser-1103' of isoform alpha-6X1X2A. Phosphorylation is not required for
CC the induction of integrin alpha-6A/beta-1 high affinity but may reduce
CC the affinity for ligand.
CC -!- PTM: Undergoes PLAU-mediated cleavage at residues Arg-634-635-Arg in a
CC time-dependent manner to produce processed integrin alpha-6 (alpha6p)
CC (PubMed:11359780, PubMed:15023541, PubMed:17303120). Production of
CC alpha6p enhances prostate cancer cell invasion and migration
CC (PubMed:17303120). {ECO:0000269|PubMed:11359780,
CC ECO:0000269|PubMed:15023541, ECO:0000269|PubMed:17303120}.
CC -!- PTM: Palmitoylation by DHHC3 enhances stability and cell surface
CC expression. {ECO:0000269|PubMed:15611341, ECO:0000269|PubMed:22314500}.
CC -!- DISEASE: Epidermolysis bullosa, junctional 6, with pyloric atresia
CC (JEB6) [MIM:619817]: A form of epidermolysis bullosa, a genodermatosis
CC characterized by recurrent blistering, fragility of the skin and
CC mucosal epithelia, and erosions caused by minor mechanical trauma. JEB6
CC is an autosomal recessive form in which blistering lesions occur
CC between the epidermis and the dermis at the lamina lucida level of the
CC basement membrane zone. Clinical manifestations include severe
CC blistering, atrophic scarring, nail dystrophy, and pyloric atresia.
CC Congenital absence of skin (aplasia cutis congenita) is common, and ear
CC anomalies are also relatively common. Disease course is usually severe
CC and often lethal in the neonatal period. {ECO:0000269|PubMed:27607025,
CC ECO:0000269|PubMed:9185503}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG57680.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS82534.1; -. [P23229-7]
DR PIR; A41543; A41543.
DR PIR; B36429; B36429.
DR RefSeq; NP_000201.2; NM_000210.3. [P23229-2]
DR RefSeq; NP_001073286.1; NM_001079818.2. [P23229-3]
DR RefSeq; NP_001303235.1; NM_001316306.1. [P23229-7]
DR PDB; 7CEB; X-ray; 2.89 A; A=24-680.
DR PDB; 7CEC; EM; 3.90 A; A=24-680.
DR PDBsum; 7CEB; -.
DR PDBsum; 7CEC; -.
DR AlphaFoldDB; P23229; -.
DR SMR; P23229; -.
DR BioGRID; 109864; 161.
DR ComplexPortal; CPX-1803; Integrin alpha6-beta1 complex.
DR ComplexPortal; CPX-1822; Integrin alpha6-beta4 complex.
DR CORUM; P23229; -.
DR IntAct; P23229; 42.
DR MINT; P23229; -.
DR STRING; 9606.ENSP00000386896; -.
DR ChEMBL; CHEMBL3716; -.
DR TCDB; 8.A.54.1.2; the integrin (integrin) family.
DR CarbonylDB; P23229; -.
DR GlyConnect; 1408; 20 N-Linked glycans (4 sites).
DR GlyGen; P23229; 13 sites, 20 N-linked glycans (4 sites).
DR iPTMnet; P23229; -.
DR PhosphoSitePlus; P23229; -.
DR SwissPalm; P23229; -.
DR BioMuta; ITGA6; -.
DR DMDM; 519668687; -.
DR OGP; P23229; -.
DR CPTAC; CPTAC-528; -.
DR CPTAC; CPTAC-529; -.
DR EPD; P23229; -.
DR jPOST; P23229; -.
DR MassIVE; P23229; -.
DR MaxQB; P23229; -.
DR PaxDb; P23229; -.
DR PeptideAtlas; P23229; -.
DR PRIDE; P23229; -.
DR ProteomicsDB; 33937; -.
DR ProteomicsDB; 54065; -. [P23229-1]
DR ProteomicsDB; 54066; -. [P23229-2]
DR ProteomicsDB; 54067; -. [P23229-3]
DR ProteomicsDB; 54068; -. [P23229-4]
DR ProteomicsDB; 54069; -. [P23229-5]
DR ProteomicsDB; 54070; -. [P23229-6]
DR ProteomicsDB; 54071; -. [P23229-7]
DR ProteomicsDB; 54072; -. [P23229-9]
DR ABCD; P23229; 3 sequenced antibodies.
DR Antibodypedia; 1485; 1351 antibodies from 47 providers.
DR DNASU; 3655; -.
DR Ensembl; ENST00000409080.6; ENSP00000386896.1; ENSG00000091409.16. [P23229-3]
DR Ensembl; ENST00000409532.5; ENSP00000386614.1; ENSG00000091409.16. [P23229-7]
DR Ensembl; ENST00000442250.6; ENSP00000406694.1; ENSG00000091409.16. [P23229-1]
DR Ensembl; ENST00000458358.5; ENSP00000394169.1; ENSG00000091409.16. [P23229-5]
DR Ensembl; ENST00000684293.1; ENSP00000508249.1; ENSG00000091409.16. [P23229-2]
DR GeneID; 3655; -.
DR KEGG; hsa:3655; -.
DR MANE-Select; ENST00000684293.1; ENSP00000508249.1; NM_000210.4; NP_000201.2. [P23229-2]
DR UCSC; uc002uho.2; human. [P23229-1]
DR CTD; 3655; -.
DR DisGeNET; 3655; -.
DR GeneCards; ITGA6; -.
DR GeneReviews; ITGA6; -.
DR HGNC; HGNC:6142; ITGA6.
DR HPA; ENSG00000091409; Low tissue specificity.
DR MalaCards; ITGA6; -.
DR MIM; 147556; gene.
DR MIM; 619817; phenotype.
DR neXtProt; NX_P23229; -.
DR OpenTargets; ENSG00000091409; -.
DR Orphanet; 79403; Junctional epidermolysis bullosa with pyloric atresia.
DR PharmGKB; PA29942; -.
DR VEuPathDB; HostDB:ENSG00000091409; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000155353; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; P23229; -.
DR OMA; SGATRYG; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; P23229; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; P23229; -.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR SignaLink; P23229; -.
DR SIGNOR; P23229; -.
DR BioGRID-ORCS; 3655; 22 hits in 1083 CRISPR screens.
DR ChiTaRS; ITGA6; human.
DR GeneWiki; ITGA6; -.
DR GenomeRNAi; 3655; -.
DR Pharos; P23229; Tbio.
DR PRO; PR:P23229; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P23229; protein.
DR Bgee; ENSG00000091409; Expressed in tibial nerve and 218 other tissues.
DR ExpressionAtlas; P23229; baseline and differential.
DR Genevisible; P23229; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038132; F:neuregulin binding; IDA:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0007044; P:cell-substrate junction assembly; TAS:ProtInc.
DR GO; GO:0010668; P:ectodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; IBA:GO_Central.
DR GO; GO:0035878; P:nail development; IMP:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
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 InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Epidermolysis bullosa; Glycoprotein; Integrin; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1953640,
FT ECO:0000269|PubMed:2542022, ECO:0000269|PubMed:2649503"
FT CHAIN 24..1130
FT /note="Integrin alpha-6"
FT /id="PRO_0000016258"
FT CHAIN 24..938
FT /note="Integrin alpha-6 heavy chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016259"
FT CHAIN 636..1130
FT /note="Processed integrin alpha-6"
FT /evidence="ECO:0000269|PubMed:17303120"
FT /id="PRO_0000425742"
FT CHAIN 942..1130
FT /note="Integrin alpha-6 light chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016260"
FT TOPO_DOM 24..1050
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1051..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1077..1130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 30..95
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 101..166
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 176..229
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 283..339
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 340..402
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 403..458
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 459..518
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1077..1083
FT /note="Interaction with HPS5"
FT MOTIF 1079..1083
FT /note="GFFKR motif"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 367
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 480
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 488
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT SITE 634..635
FT /note="Cleavage; by PLAU in invasive prostate cancer"
FT /evidence="ECO:0000269|PubMed:17303120"
FT LIPID 1078
FT /note="S-palmitoyl cysteine; by DHHC3"
FT /evidence="ECO:0000269|PubMed:15611341,
FT ECO:0000269|PubMed:22314500"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 997
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 86..94
FT /evidence="ECO:0000250"
FT DISULFID 131..154
FT /evidence="ECO:0000250"
FT DISULFID 175..188
FT /evidence="ECO:0000250"
FT DISULFID 528..535
FT /evidence="ECO:0000250"
FT DISULFID 541..601
FT /evidence="ECO:0000250"
FT DISULFID 665..671
FT /evidence="ECO:0000250"
FT DISULFID 765..776
FT /evidence="ECO:0000250"
FT DISULFID 920..967
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 973..978
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036406"
FT VAR_SEQ 215..258
FT /note="Missing (in isoform Alpha-6X2A, isoform Alpha-6X2B
FT and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_002723"
FT VAR_SEQ 259..297
FT /note="Missing (in isoform Alpha-6X1A and isoform Alpha-
FT 6X1B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1976638"
FT /id="VSP_002724"
FT VAR_SEQ 918..932
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036407"
FT VAR_SEQ 1084..1130
FT /note="SRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS -> N
FT KKDHYDATYHKAEIHAQPSDKERLTSDA (in isoform Alpha-6X1A,
FT isoform Alpha-6X2A, isoform Alpha-6X1X2A, isoform 7 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1976638"
FT /id="VSP_002725"
FT CONFLICT 69
FT /note="A -> G (in Ref. 1; CAA37655 and 8; CAA42099)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="A -> T (in Ref. 4; BAG59130 and 7; AAI36456/
FT AAI36457)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="F -> L (in Ref. 8; CAA42099)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="D -> Y (in Ref. 1; CAA37655 and 3; AAD48469)"
FT /evidence="ECO:0000305"
FT CONFLICT 1125
FT /note="E -> R (in Ref. 1; AAB20355)"
FT /evidence="ECO:0000305"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:7CEB"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:7CEB"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:7CEB"
FT TURN 182..187
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:7CEB"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 299..319
FT /evidence="ECO:0007829|PDB:7CEB"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 335..347
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 445..452
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 455..465
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 467..479
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 488..501
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 506..517
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 535..550
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 557..563
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 600..607
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:7CEB"
FT STRAND 652..660
FT /evidence="ECO:0007829|PDB:7CEB"
FT MOD_RES P23229-2:1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8360143"
FT MOD_RES P23229-4:1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8360143"
FT MOD_RES P23229-6:1103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8360143"
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
