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 27-MAR-2024, entry version 233. 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=5; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS92897.1; -. [P23229-1] 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 EMDB; EMD-30342; -. DR SMR; P23229; -. DR BioGRID; 109864; 177. DR ComplexPortal; CPX-1803; Integrin alpha6-beta1 complex. DR ComplexPortal; CPX-1822; Integrin alpha6-beta4 complex. DR CORUM; P23229; -. DR IntAct; P23229; 45. 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 GlyCosmos; P23229; 9 sites, 20 glycans. DR GlyGen; P23229; 14 sites, 20 N-linked glycans (4 sites), 1 O-linked glycan (1 site). 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; 9606-ENSP00000386896; -. DR PeptideAtlas; 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 Pumba; P23229; -. DR ABCD; P23229; 3 sequenced antibodies. DR Antibodypedia; 1485; 1433 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 AGR; HGNC:6142; -. 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; HYINRTV; -. DR OrthoDB; 3816176at2759; -. 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; 23 hits in 1163 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 220 other cell types or tissues. DR ExpressionAtlas; P23229; baseline and differential. DR GO; GO:0005912; C:adherens junction; IEA:Ensembl. 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:0030175; C:filopodium; IEA:Ensembl. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0034676; C:integrin alpha6-beta4 complex; IEA:Ensembl. 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:0043236; F:laminin binding; IEA:Ensembl. 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:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl. 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:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl. 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; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1. DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR048286; Integrin_alpha_Ig-like_3. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF9; INTEGRIN ALPHA-6; 1. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF20806; Integrin_A_Ig_3; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. DR Genevisible; P23229; HS. 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 FT Alpha-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; FT AAI36456/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 //