ID DYST_HUMAN Reviewed; 7570 AA. AC Q03001; B7Z3H1; E7ERU0; O94833; Q12825; Q13266; Q13267; Q13775; Q5TBT0; AC Q5TBT2; Q5TF23; Q5TF24; Q8N1T8; Q8N8J3; Q8WXK8; Q8WXK9; Q96AK9; Q96DQ5; AC Q96J76; Q96QT5; Q9H555; Q9UGD7; Q9UGD8; Q9UN10; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 4. DT 27-MAR-2024, entry version 239. DE RecName: Full=Dystonin {ECO:0000305}; DE AltName: Full=230 kDa bullous pemphigoid antigen; DE AltName: Full=230/240 kDa bullous pemphigoid antigen; DE AltName: Full=Bullous pemphigoid antigen 1; DE Short=BPA; DE Short=Bullous pemphigoid antigen; DE AltName: Full=Dystonia musculorum protein; DE AltName: Full=Hemidesmosomal plaque protein; GN Name=DST {ECO:0000312|HGNC:HGNC:1090}; GN Synonyms=BP230, BP240, BPAG1, DMH, DT, KIAA0728; 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 3), AND DISEASE. RC TISSUE=Keratinocyte; RX PubMed=1717441; DOI=10.1016/s0021-9258(18)55195-4; RA Sawamura D., Li K., Chu M.-L., Uitto J.; RT "Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced RT from cloned cDNAs predict biologically important peptide segments and RT protein domains."; RL J. Biol. Chem. 266:17784-17790(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Keratinocyte; RX PubMed=8345227; DOI=10.1111/1523-1747.ep12365083; RA Elgart G.W., Stanley J.R.; RT "Cloning of the 5' mRNA for the 230-kD bullous pemphigoid antigen by rapid RT amplification of cDNA ends."; RL J. Invest. Dermatol. 101:244-246(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF RP 1-3386 (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Keratinocyte; RX PubMed=11751855; DOI=10.1074/jbc.m109209200; RA Okumura M., Yamakawa H., Ohara O., Owaribe K.; RT "Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1) RT including the domain structure closely related to MACF (microtubule actin RT cross-linking factor)."; RL J. Biol. Chem. 277:6682-6687(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 4114-6568 (ISOFORM 1), AND VARIANT ALA-5138. RC TISSUE=Brain, Hippocampus, Placenta, and Tongue; 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=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Duodenum; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-461 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [MRNA] OF 1-46 (ISOFORM 6). RC TISSUE=Fetal brain, and Retina; RX PubMed=8575775; DOI=10.1006/geno.1995.9936; RA Brown A., Dalpe G., Mathieu M., Kothary R.; RT "Cloning and characterization of the neural isoforms of human dystonin."; RL Genomics 29:777-780(1995). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-188 (ISOFORM 7), ALTERNATIVE SPLICING RP (ISOFORMS 6 AND 7), FUNCTION OF ISOFORMS 6 AND 7, AND SUBCELLULAR LOCATION RP (ISOFORMS 6 AND 7). RC TISSUE=Fetal brain; RX PubMed=10428034; DOI=10.1016/s0092-8674(00)81017-x; RA Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.; RT "Integrators of the cytoskeleton that stabilize microtubules."; RL Cell 98:229-238(1999). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-308 (ISOFORM 1). RC TISSUE=Pineal gland; RA Geerts D., Sonnenberg A.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 881-7570 (ISOFORM 3). RC TISSUE=Keratinocyte; RX PubMed=1712022; DOI=10.1016/s0021-9258(18)98934-9; RA Tanaka T., Parry D.A.D., Klaus-Kovtun V., Steinert P.M., Stanley J.R.; RT "Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin RT I confirms that they define a new family of cell adhesion junction plaque RT proteins."; RL J. Biol. Chem. 266:12555-12559(1991). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5947-7570 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [12] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [13] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Keratinocyte; RX PubMed=2461961; DOI=10.1172/jci113803; RA Stanley J.R., Tanaka T., Mueller S., Klaus-Kovtun V., Roop D.; RT "Isolation of complementary DNA for bullous pemphigoid antigen by use of RT patients' autoantibodies."; RL J. Clin. Invest. 82:1864-1870(1988). RN [14] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=2090522; DOI=10.1111/j.1432-0436.1990.tb00475.x; RA Owaribe K., Kartenbeck J., Stumpp S., Magin T.M., Krieg T., Diaz L.A., RA Franke W.W.; RT "The hemidesmosomal plaque. I. Characterization of a major constituent RT protein as a differentiation marker for certain forms of epithelia."; RL Differentiation 45:207-220(1990). RN [15] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING RP (ISOFORM 3). RX PubMed=8010969; DOI=10.1042/bj3000851; RA Hopkinson S.B., Jones J.C.; RT "Identification of a second protein product of the gene encoding a human RT epidermal autoantigen."; RL Biochem. J. 300:851-857(1994). RN [16] RP ALTERNATIVE SPLICING (ISOFORMS 3 AND 6), AND TISSUE SPECIFICITY. RX PubMed=8752219; DOI=10.1016/s0092-8674(00)80138-5; RA Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.; RT "An essential cytoskeletal linker protein connecting actin microfilaments RT to intermediate filaments."; RL Cell 86:655-665(1996). RN [17] RP ALTERNATIVE SPLICING (ISOFORM 3), AND INTERACTION WITH COL17A1 AND ITGB4. RX PubMed=10637308; DOI=10.1091/mbc.11.1.277; RA Hopkinson S.B., Jones J.C.; RT "The N terminus of the transmembrane protein BP180 interacts with the N- RT terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage RT to the cell surface at the site of the hemidesmosome."; RL Mol. Biol. Cell 11:277-286(2000). RN [18] RP DOMAINS. RX PubMed=8621649; DOI=10.1074/jbc.271.16.9716; RA Tang H.-Y., Chaffotte A.-F., Thacher S.M.; RT "Structural analysis of the predicted coiled-coil rod domain of the RT cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of RT the N-terminal globular domain-rod boundary."; RL J. Biol. Chem. 271:9716-9722(1996). RN [19] RP INTERACTION WITH ITGB4 AND ERBIN. RX PubMed=11375975; DOI=10.1074/jbc.m011005200; RA Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H., RA Sonnenberg A., Borradori L.; RT "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin RT beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative RT splice variants of ERBIN and analysis of their tissue expression."; RL J. Biol. Chem. 276:32427-32436(2001). RN [20] RP ALTERNATIVE SPLICING (ISOFORM 9). RX PubMed=14581450; DOI=10.1083/jcb.200306075; RA Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C., RA Mobley W., Fuchs E., Yang Y.; RT "BPAG1n4 is essential for retrograde axonal transport in sensory neurons."; RL J. Cell Biol. 163:223-229(2003). RN [21] RP ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, INTERACTION WITH RP COL17A1 AND ITGB4, AND SUBCELLULAR LOCATION (ISOFORM 3). RX PubMed=12482924; DOI=10.1242/jcs.00241; RA Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.; RT "Analysis of the interactions between BP180, BP230, plectin and the RT integrin alpha6beta4 important for hemidesmosome assembly."; RL J. Cell Sci. 116:387-399(2003). RN [22] RP ALTERNATIVE SPLICING (ISOFORM 3), ASSOCIATION WITH KERATIN FILAMENTS, AND RP SUBCELLULAR LOCATION (ISOFORM 3). RX PubMed=12802069; DOI=10.1091/mbc.e02-08-0548; RA Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., RA Green K.J., Sonnenberg A., Borradori L.; RT "Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin RT with intermediate filaments is mediated by distinct sequences within their RT COOH terminus."; RL Mol. Biol. Cell 14:1978-1992(2003). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7432, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION OF ISOFORM 3, AND SUBCELLULAR RP LOCATION (ISOFORM 3). RX PubMed=19403692; DOI=10.1091/mbc.e09-01-0051; RA Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.; RT "BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated RT modulation of Rac1 and cofilin activities."; RL Mol. Biol. Cell 20:2954-2962(2009). RN [25] RP ALTERNATIVE SPLICING (ISOFORM 1), HOMODIMERIZATION, INTERACTION WITH ACTN2 RP AND PLEC, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010; RA Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., RA Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., RA Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.; RT "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle RT and association with plectin and alpha-actinin."; RL Exp. Cell Res. 316:297-313(2010). RN [26] RP INVOLVEMENT IN EBS3. RX PubMed=20164846; DOI=10.1038/jid.2010.19; RA Groves R.W., Liu L., Dopping-Hepenstal P.J., Markus H.S., Lovell P.A., RA Ozoemena L., Lai-Cheong J.E., Gawler J., Owaribe K., Hashimoto T., RA Mellerio J.E., Mee J.B., McGrath J.A.; RT "A homozygous nonsense mutation within the dystonin gene coding for the RT coiled-coil domain of the epithelial isoform of BPAG1 underlies a new RT subtype of autosomal recessive epidermolysis bullosa simplex."; RL J. Invest. Dermatol. 130:1551-1557(2010). RN [27] 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 [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2919, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [29] RP INVOLVEMENT IN HSAN6. RX PubMed=22522446; DOI=10.1002/ana.23524; RA Edvardson S., Cinnamon Y., Jalas C., Shaag A., Maayan C., Axelrod F.B., RA Elpeleg O.; RT "Hereditary sensory autonomic neuropathy caused by a mutation in RT dystonin."; RL Ann. Neurol. 71:569-572(2012). RN [30] RP INVOLVEMENT IN EBS3. RX PubMed=22113475; DOI=10.1038/jid.2011.379; RA Liu L., Dopping-Hepenstal P.J., Lovell P.A., Michael M., Horn H., Fong K., RA Lai-Cheong J.E., Mellerio J.E., Parsons M., McGrath J.A.; RT "Autosomal recessive epidermolysis bullosa simplex due to loss of BPAG1-e RT expression."; RL J. Invest. Dermatol. 132:742-744(2012). RN [31] RP INTERACTION WITH TMIGD2. RX PubMed=22419821; DOI=10.1091/mbc.e11-11-0934; RA Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.; RT "Identification of IGPR-1 as a novel adhesion molecule involved in RT angiogenesis."; RL Mol. Biol. Cell 23:1646-1656(2012). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3968, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-135 (ISOFORM 6), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3968, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-184 (ISOFORM 8), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [34] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 7541-7570 IN COMPLEX WITH MAPRE1, RP DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, AND MUTAGENESIS OF LYS-7548; RP SER-7550; ILE-7552; PRO-7553 AND 7557-ARG-LYS-7558. RX PubMed=19632184; DOI=10.1016/j.cell.2009.04.065; RA Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., RA Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., RA Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.; RT "An EB1-binding motif acts as a microtubule tip localization signal."; RL Cell 138:366-376(2009). CC -!- FUNCTION: Cytoskeletal linker protein. Acts as an integrator of CC intermediate filaments, actin and microtubule cytoskeleton networks. CC Required for anchoring either intermediate filaments to the actin CC cytoskeleton in neural and muscle cells or keratin-containing CC intermediate filaments to hemidesmosomes in epithelial cells. The CC proteins may self-aggregate to form filaments or a two-dimensional CC mesh. Regulates the organization and stability of the microtubule CC network of sensory neurons to allow axonal transport. Mediates docking CC of the dynein/dynactin motor complex to vesicle cargos for retrograde CC axonal transport through its interaction with TMEM108 and DCTN1 (By CC similarity). {ECO:0000250|UniProtKB:Q91ZU6}. CC -!- FUNCTION: [Isoform 3]: Plays a structural role in the assembly of CC hemidesmosomes of epithelial cells; anchors keratin-containing CC intermediate filaments to the inner plaque of hemidesmosomes. Required CC for the regulation of keratinocyte polarity and motility; mediates CC integrin ITGB4 regulation of RAC1 activity. CC -!- FUNCTION: [Isoform 6]: Required for bundling actin filaments around the CC nucleus. {ECO:0000250, ECO:0000269|PubMed:10428034, CC ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692}. CC -!- FUNCTION: [Isoform 7]: Regulates the organization and stability of the CC microtubule network of sensory neurons to allow axonal transport. CC -!- SUBUNIT: Homodimer. Isoform 1 interacts (via N-terminus) with PLEC (via CC N-terminus). Interacts with the neuronal intermediate filament protein, CC PRPH. Interacts with DES. Interacts with SYNE3 (By similarity). Isoform CC 1 and isoform 6 can homodimerize (via N-terminus). Isoform 1 interacts CC (via N-terminus) with ACTN2. Isoform 1 interacts (via N-terminus) with CC PLEC (via N-terminus). Isoform 3 interacts (via N-terminus) with CC COL17A1 (via cytoplasmic region). Isoform 3 interacts (via N-terminus) CC with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 3 CC interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 3 CC associates (via C-terminal) with KRT5-KRT14 (via rod region) CC intermediate filaments of keratins. Interacts with MAPRE1; probably CC required for targeting to the growing microtubule plus ends. Interacts CC with TMIGD2. Isoform 9 interacts with TMEM108 (By similarity). CC {ECO:0000250|UniProtKB:Q91ZU6, ECO:0000269|PubMed:10637308, CC ECO:0000269|PubMed:11375975, ECO:0000269|PubMed:12482924, CC ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:19932097, CC ECO:0000269|PubMed:22419821}. CC -!- INTERACTION: CC Q03001; Q9UKG1: APPL1; NbExp=3; IntAct=EBI-310758, EBI-741243; CC Q03001; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-310758, EBI-529989; CC Q03001; Q15691: MAPRE1; NbExp=4; IntAct=EBI-310758, EBI-1004115; CC Q03001; Q61166: Mapre1; Xeno; NbExp=4; IntAct=EBI-310758, EBI-2027055; CC Q03001; PRO_0000037946 [P29991]; Xeno; NbExp=4; IntAct=EBI-310758, EBI-8826488; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:11751855, ECO:0000269|PubMed:19932097}. Cytoplasm, CC cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q91ZU6}. Cell CC projection, axon {ECO:0000250|UniProtKB:Q91ZU6}. Note=Associates with CC intermediate filaments, actin and microtubule cytoskeletons. Localizes CC to actin stress fibers and to actin-rich ruffling at the cortex of CC cells (By similarity). Associated at the growing distal tip of CC microtubules. {ECO:0000250|UniProtKB:Q91ZU6}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton CC {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, CC myofibril, sarcomere, H zone {ECO:0000250}. Note=Localizes to CC microtubules and actin microfilaments throughout the cytoplasm and at CC focal contact attachments at the plasma membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton CC {ECO:0000250}. Note=Colocalizes both cortical and cytoplasmic actin CC filaments. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton. Cell CC junction, hemidesmosome. Note=Localizes to actin and intermediate CC filaments cytoskeletons (By similarity). Colocalizes with the epidermal CC KRT5-KRT14 intermediate filaments network of keratins. Colocalizes with CC ITGB4 at the leading edge of migrating keratinocytes. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus CC {ECO:0000250|UniProtKB:Q91ZU6}. Nucleus envelope CC {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}; CC Single-pass membrane protein {ECO:0000269|PubMed:10428034}. Endoplasmic CC reticulum membrane {ECO:0000250|UniProtKB:Q91ZU6}; Single-pass membrane CC protein {ECO:0000250|UniProtKB:Q91ZU6}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10428034}. Cytoplasm, cytoskeleton, stress fiber CC {ECO:0000250|UniProtKB:Q91ZU6}. Note=Localizes to actin and CC intermediate filaments cytoskeletons. Localizes to central actin stress CC fibers around the nucleus and is excluded form focal contact sites in CC myoblast cells. Translocates to the nucleus (By similarity). Associates CC with actin cytoskeleton in sensory neurons. CC {ECO:0000250|UniProtKB:Q91ZU6}. CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10428034}. Cell projection, axon CC {ECO:0000269|PubMed:10428034}. Membrane {ECO:0000269|PubMed:10428034}. CC Note=Associates with axonal microtubules and intermediate filaments, CC but not with actin cytoskeleton, in sensory neurons. CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm, cytoskeleton CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell membrane CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=BPAG1-b; CC IsoId=Q03001-7; Sequence=Displayed; CC Name=2; Synonyms=BPAG1eA, Dystonin-1, eA; CC IsoId=Q03001-8; Sequence=VSP_041525, VSP_041535, VSP_041539, CC VSP_041540; CC Name=3; Synonyms=BPAG1e, eBPAG1; CC IsoId=Q03001-3; Sequence=VSP_041525, VSP_041533, VSP_041534; CC Name=4; Synonyms=BPAG1eA, eB; CC IsoId=Q03001-9; Sequence=VSP_041525, VSP_041536; CC Name=5; CC IsoId=Q03001-10; Sequence=VSP_041524, VSP_041537, VSP_041538; CC Name=6; Synonyms=BPAG1n1, BPAG1n2, Dystonin-2; CC IsoId=Q03001-11; Sequence=VSP_041528, VSP_041529; CC Name=7; Synonyms=BPAG1n3; CC IsoId=Q03001-12; Sequence=VSP_041526, VSP_041530; CC Name=8; CC IsoId=Q03001-13; Sequence=VSP_041527, VSP_041531, VSP_041532; CC Name=9; Synonyms=BPAG1-a {ECO:0000303|PubMed:14581450}, BAPG1n4 CC {ECO:0000303|PubMed:14581450}; CC IsoId=Q03001-14; Sequence=VSP_058835, VSP_058836; CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in myoblasts (at protein CC level). Isoform 3 is expressed in the skin. Isoform 6 is expressed in CC the brain. Highly expressed in skeletal muscle and cultured CC keratinocytes. {ECO:0000269|PubMed:11751855, CC ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:8752219}. CC -!- DOMAIN: Its association with epidermal and simple keratins is dependent CC on the tertiary structure induced by heterodimerization of these CC intermediate filaments proteins and most likely involves recognition CC sites located in the rod domain of these keratins. CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates CC interaction with MAPRE1 and targeting to the growing microtubule plus CC ends. CC -!- DISEASE: Neuropathy, hereditary sensory and autonomic, 6 (HSAN6) CC [MIM:614653]: A form of hereditary sensory and autonomic neuropathy, a CC genetically and clinically heterogeneous group of disorders CC characterized by degeneration of dorsal root and autonomic ganglion CC cells, and by sensory and/or autonomic abnormalities. HSAN6 is a severe CC autosomal recessive disorder characterized by neonatal hypotonia, CC respiratory and feeding difficulties, lack of psychomotor development, CC and autonomic abnormalities including labile cardiovascular function, CC lack of corneal reflexes leading to corneal scarring, areflexia, and CC absent axonal flare response after intradermal histamine injection. CC {ECO:0000269|PubMed:22522446}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa simplex 3, localized or generalized CC intermediate, with BP230 deficiency (EBS3) [MIM:615425]: A form of CC epidermolysis bullosa, a genodermatosis characterized by recurrent CC blistering, fragility of the skin and mucosal epithelia, and erosions CC caused by minor mechanical trauma. EBS3 is an autosomal recessive CC disorder characterized by skin blistering mainly occurring on the feet CC and ankles. Ultrastructural analysis of skin biopsy shows abnormal CC hemidesmosomes with poorly formed inner plaques. CC {ECO:0000269|PubMed:20164846, ECO:0000269|PubMed:22113475}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform 4]: Incomplete sequence. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Incomplete sequence. Transmembrane protein CC (helical transmembrane domain from amino acid 18 to 38). {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Incomplete sequence. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 8]: Probably myristoylated on Gly-2. Probably CC S-palmitoylated on Cys-5 and Cys-7. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA35538.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305}; CC Sequence=AAA57185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAH16991.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB70870.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC04449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC04848.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAC50244.1; Type=Frameshift; 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; M69225; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; L11690; AAA52288.1; -; mRNA. DR EMBL; AF400226; AAL62061.1; -; mRNA. DR EMBL; AF400227; AAL62062.1; -; mRNA. DR EMBL; AK055189; BAB70870.1; ALT_INIT; mRNA. DR EMBL; AK094883; BAC04449.1; ALT_INIT; mRNA. DR EMBL; AK096713; BAC04848.1; ALT_INIT; mRNA. DR EMBL; AK295864; BAH12207.1; -; mRNA. DR EMBL; AL049215; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL096710; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590005; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137008; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL512422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL512448; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590037; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF458172; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016991; AAH16991.1; ALT_INIT; mRNA. DR EMBL; U31850; AAC50243.1; -; mRNA. DR EMBL; U31851; AAC50244.1; ALT_FRAME; mRNA. DR EMBL; AF165191; AAD49334.1; -; mRNA. DR EMBL; AY032900; AAK63130.1; -; mRNA. DR EMBL; AY032901; AAK63131.1; -; mRNA. DR EMBL; M63618; AAA35606.1; -; mRNA. DR EMBL; AB018271; BAA34448.2; -; mRNA. DR EMBL; M22942; AAA35538.1; ALT_SEQ; mRNA. DR EMBL; X58677; CAA41528.1; -; mRNA. DR EMBL; U04850; AAA57184.1; -; Genomic_DNA. DR EMBL; U04850; AAA57185.1; ALT_SEQ; Genomic_DNA. DR CCDS; CCDS47443.1; -. [Q03001-8] DR CCDS; CCDS4959.1; -. [Q03001-3] DR CCDS; CCDS93934.1; -. [Q03001-14] DR PIR; I56317; A40937. DR RefSeq; NP_001138241.1; NM_001144769.2. DR RefSeq; NP_001138242.1; NM_001144770.1. DR RefSeq; NP_001714.1; NM_001723.5. [Q03001-3] DR RefSeq; NP_056363.2; NM_015548.4. [Q03001-8] DR RefSeq; NP_899236.1; NM_183380.3. DR RefSeq; XP_016866713.1; XM_017011224.1. DR PDB; 3GJO; X-ray; 2.50 A; E/F/G/H=7541-7570. DR PDB; 7OLG; NMR; -; C/D=7548-7558. DR PDBsum; 3GJO; -. DR PDBsum; 7OLG; -. DR SMR; Q03001; -. DR BioGRID; 107135; 243. DR DIP; DIP-33131N; -. DR ELM; Q03001; -. DR IntAct; Q03001; 118. DR MINT; Q03001; -. DR STRING; 9606.ENSP00000307959; -. DR GlyCosmos; Q03001; 6 sites, 1 glycan. DR GlyGen; Q03001; 11 sites, 1 O-linked glycan (11 sites). DR iPTMnet; Q03001; -. DR MetOSite; Q03001; -. DR PhosphoSitePlus; Q03001; -. DR SwissPalm; Q03001; -. DR BioMuta; DST; -. DR DMDM; 294862529; -. DR EPD; Q03001; -. DR jPOST; Q03001; -. DR MassIVE; Q03001; -. DR MaxQB; Q03001; -. DR PaxDb; 9606-ENSP00000307959; -. DR PeptideAtlas; Q03001; -. DR ProteomicsDB; 17852; -. DR ProteomicsDB; 58151; -. [Q03001-7] DR ProteomicsDB; 58152; -. [Q03001-10] DR ProteomicsDB; 58153; -. [Q03001-11] DR ProteomicsDB; 58154; -. [Q03001-12] DR ProteomicsDB; 58155; -. [Q03001-13] DR ProteomicsDB; 58156; -. [Q03001-3] DR ProteomicsDB; 58157; -. [Q03001-8] DR ProteomicsDB; 58158; -. [Q03001-9] DR Pumba; Q03001; -. DR ABCD; Q03001; 3 sequenced antibodies. DR Antibodypedia; 31066; 193 antibodies from 23 providers. DR DNASU; 667; -. DR Ensembl; ENST00000244364.10; ENSP00000244364.6; ENSG00000151914.22. [Q03001-8] DR Ensembl; ENST00000370765.11; ENSP00000359801.6; ENSG00000151914.22. [Q03001-3] DR Ensembl; ENST00000370788.6; ENSP00000359824.2; ENSG00000151914.22. [Q03001-14] DR Ensembl; ENST00000439203.5; ENSP00000404924.1; ENSG00000151914.22. [Q03001-9] DR GeneID; 667; -. DR KEGG; hsa:667; -. DR UCSC; uc003pcy.5; human. [Q03001-7] DR AGR; HGNC:1090; -. DR CTD; 667; -. DR DisGeNET; 667; -. DR GeneCards; DST; -. DR GeneReviews; DST; -. DR HGNC; HGNC:1090; DST. DR HPA; ENSG00000151914; Low tissue specificity. DR MalaCards; DST; -. DR MIM; 113810; gene. DR MIM; 614653; phenotype. DR MIM; 615425; phenotype. DR neXtProt; NX_Q03001; -. DR OpenTargets; ENSG00000151914; -. DR Orphanet; 412181; Epidermolysis bullosa simplex due to BP230 deficiency. DR Orphanet; 314381; Hereditary sensory and autonomic neuropathy type 6. DR PharmGKB; PA25399; -. DR VEuPathDB; HostDB:ENSG00000151914; -. DR eggNOG; KOG0516; Eukaryota. DR eggNOG; KOG0517; Eukaryota. DR GeneTree; ENSGT00940000155008; -. DR HOGENOM; CLU_000015_3_0_1; -. DR InParanoid; Q03001; -. DR OrthoDB; 5489926at2759; -. DR PhylomeDB; Q03001; -. DR TreeFam; TF335163; -. DR PathwayCommons; Q03001; -. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. [Q03001-3] DR Reactome; R-HSA-446107; Type I hemidesmosome assembly. DR Reactome; R-HSA-9013420; RHOU GTPase cycle. DR Reactome; R-HSA-9013424; RHOV GTPase cycle. DR Reactome; R-HSA-9696264; RND3 GTPase cycle. DR Reactome; R-HSA-9696270; RND2 GTPase cycle. DR Reactome; R-HSA-9696273; RND1 GTPase cycle. DR SignaLink; Q03001; -. DR SIGNOR; Q03001; -. DR BioGRID-ORCS; 667; 16 hits in 1162 CRISPR screens. DR ChiTaRS; DST; human. DR EvolutionaryTrace; Q03001; -. DR GeneWiki; Dystonin; -. DR GenomeRNAi; 667; -. DR Pharos; Q03001; Tbio. DR PRO; PR:Q03001; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q03001; Protein. DR Bgee; ENSG00000151914; Expressed in corpus callosum and 207 other cell types or tissues. DR ExpressionAtlas; Q03001; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0009925; C:basal plasma membrane; NAS:UniProtKB. DR GO; GO:0005604; C:basement membrane; TAS:ProtInc. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0031673; C:H zone; IEA:UniProtKB-SubCell. DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB. DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB. DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell. DR GO; GO:0030018; C:Z disc; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0048870; P:cell motility; IMP:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEP:UniProtKB. DR GO; GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB. DR GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB. DR GO; GO:0042060; P:wound healing; IBA:GO_Central. DR CDD; cd21236; CH_DYST_rpt1; 1. DR CDD; cd21239; CH_DYST_rpt2; 1. DR CDD; cd00051; EFh; 1. DR CDD; cd00176; SPEC; 17. DR Gene3D; 1.20.58.1060; -; 1. DR Gene3D; 1.20.58.60; -; 31. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.30.920.20; Gas2-like domain; 1. DR Gene3D; 3.90.1290.10; Plakin repeat; 3. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR041615; Desmoplakin_SH3. DR InterPro; IPR041573; Desmoplakin_Spectrin-like. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR003108; GAR_dom. DR InterPro; IPR036534; GAR_dom_sf. DR InterPro; IPR049538; PCN-like_spectrin-like_rpt. DR InterPro; IPR043197; Plakin. DR InterPro; IPR035915; Plakin_repeat_sf. DR InterPro; IPR001101; Plectin_repeat. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR23169; ENVOPLAKIN; 1. DR PANTHER; PTHR23169:SF21; EPIPLAKIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF02187; GAS2; 1. DR Pfam; PF00681; Plectin; 2. DR Pfam; PF17902; SH3_10; 1. DR Pfam; PF00435; Spectrin; 20. DR Pfam; PF18373; Spectrin_2; 1. DR Pfam; PF21019; Spectrin_3; 1. DR Pfam; PF21020; Spectrin_4; 1. DR Pfam; PF21097; SR_plectin_7; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00054; EFh; 2. DR SMART; SM00243; GAS2; 1. DR SMART; SM00250; PLEC; 8. DR SMART; SM00150; SPEC; 32. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF143575; GAS2 domain-like; 1. DR SUPFAM; SSF75399; Plakin repeat; 2. DR SUPFAM; SSF46966; Spectrin repeat; 29. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS51460; GAR; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q03001; HS. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative promoter usage; KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane; KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; KW Endoplasmic reticulum; Epidermolysis bullosa; Intermediate filament; KW Isopeptide bond; Lipoprotein; Membrane; Metal-binding; Microtubule; KW Muscle protein; Neurodegeneration; Neuropathy; Nucleus; Palmitate; KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Transmembrane; KW Ubl conjugation. FT CHAIN 1..7570 FT /note="Dystonin" FT /id="PRO_0000078138" FT DOMAIN 35..138 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 151..255 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 602..699 FT /note="Spectrin 1" FT REPEAT 701..802 FT /note="Spectrin 2" FT DOMAIN 887..944 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REPEAT 1293..1422 FT /note="Spectrin 3" FT REPEAT 1440..1540 FT /note="Spectrin 4" FT REPEAT 1584..1626 FT /note="Plectin 1" FT REPEAT 1660..1703 FT /note="Plectin 2" FT REPEAT 1774..1817 FT /note="Plectin 3" FT REPEAT 1818..1855 FT /note="Plectin 4" FT REPEAT 1856..1891 FT /note="Plectin 5" FT REPEAT 3395..3501 FT /note="Spectrin 5" FT REPEAT 3643..3752 FT /note="Spectrin 6" FT REPEAT 3926..4040 FT /note="Spectrin 7" FT REPEAT 4047..4153 FT /note="Spectrin 8" FT REPEAT 4160..4259 FT /note="Spectrin 9" FT REPEAT 4269..4368 FT /note="Spectrin 10" FT REPEAT 4516..4621 FT /note="Spectrin 11" FT REPEAT 4628..4732 FT /note="Spectrin 12" FT REPEAT 4742..4842 FT /note="Spectrin 13" FT REPEAT 4849..4951 FT /note="Spectrin 14" FT REPEAT 4958..5058 FT /note="Spectrin 15" FT REPEAT 5068..5167 FT /note="Spectrin 16" FT REPEAT 5174..5277 FT /note="Spectrin 17" FT REPEAT 5284..5388 FT /note="Spectrin 18" FT REPEAT 5395..5497 FT /note="Spectrin 19" FT REPEAT 5504..5715 FT /note="Spectrin 20" FT REPEAT 5831..5933 FT /note="Spectrin 21" FT REPEAT 5941..6041 FT /note="Spectrin 22" FT REPEAT 6048..6154 FT /note="Spectrin 23" FT REPEAT 6161..6263 FT /note="Spectrin 24" FT REPEAT 6270..6373 FT /note="Spectrin 25" FT REPEAT 6380..6482 FT /note="Spectrin 26" FT REPEAT 6489..6591 FT /note="Spectrin 27" FT REPEAT 6598..6700 FT /note="Spectrin 28" FT REPEAT 6707..6810 FT /note="Spectrin 29" FT REPEAT 6817..6918 FT /note="Spectrin 30" FT REPEAT 6925..7027 FT /note="Spectrin 31" FT REPEAT 7037..7167 FT /note="Spectrin 32" FT DOMAIN 7197..7232 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 7233..7268 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 7273..7351 FT /note="GAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792" FT REGION 35..252 FT /note="Actin-binding" FT REGION 2317..2346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2383..2441 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2585..2616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3190..3221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7358..7379 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7395..7452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7481..7570 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1383..1389 FT /note="Nuclear localization signal; in isoform 6" FT /evidence="ECO:0000250" FT MOTIF 7550..7553 FT /note="Microtubule tip localization signal" FT COMPBIAS 2408..2431 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2587..2605 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3190..3214 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7361..7378 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7411..7446 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7515..7561 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 7210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7212 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7214 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7246 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7250 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7252 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7257 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 236 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT MOD_RES 237 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT MOD_RES 1382 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT MOD_RES 2229 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT MOD_RES 2919 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 3968 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 4749 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT MOD_RES 7432 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 7510 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT MOD_RES 7513 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT MOD_RES 7525 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91ZU6" FT CROSSLNK 5470 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT VAR_SEQ 1..3896 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041524" FT VAR_SEQ 1..381 FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV FT NIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGYAG FT IRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLD FT PEDVDVSSPDEKSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIR FT HHVTTMSERTFPNNPVELKALYNQYLQFKETEIPPKETEKSKIKRLYKLLEIWIEFGRI FT KLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVE -> MHSSSYSYRSSDSVFSNTTST FT RTSLDSNENLLLVHCGPTLINSCISFGSESFDGH (in isoform 2, isoform 3 FT and isoform 4)" FT /evidence="ECO:0000303|PubMed:11751855, FT ECO:0000303|PubMed:1712022, ECO:0000303|PubMed:1717441, FT ECO:0000303|PubMed:8345227, ECO:0000303|PubMed:9872452" FT /id="VSP_041525" FT VAR_SEQ 1..138 FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV FT NIRNDDITDGNPKLTLGLIWTIILHFQ -> MQHSIFSLKKKRCHSLYTSMSSVSKDTD FT GNE (in isoform 7)" FT /evidence="ECO:0000303|PubMed:10428034" FT /id="VSP_041526" FT VAR_SEQ 1..138 FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV FT NIRNDDITDGNPKLTLGLIWTIILHFQ -> MGNVCGCVRAEKEEQYVDPAKTPLNPEK FT YSPGRKYFRRKPIKKTGGDKESVGANNENEGKKKSSSQPSKEQPAPLSRGLVQQESVTL FT NSALGDGIQQKKTEVVADSVKQKLLPSAVSSWSDCVNTSPAKDSETEVKVSELDERISE FT KDSTPYCAKRKKHLDDVNTSEITFQEKTDVFSFRKAASLSSIPSGIERSLEKGGFPEDP FT PKSYSSIQEKQNTERFCPHATQHFQFKKKRCHSLYTSMSSVSKDTDGNE (in FT isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041527" FT VAR_SEQ 1..30 FT /note="MAGYLSPAAYLYVEEQEYLQAYEDVLERYK -> MIAAAFLVLLRPYSIQCA FT LFLLLLLLGTIATIVFFCCWHRKLQKGRHPMKSVFSGRSRSRDAVLRSHHFRSEGFRAS FT PRHLRRRVAAAAAARLEEVKPVVEVHHQSEQETSVRKRRIKKSSRVQPEFYHSVQGASI FT RRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASPAPGDTLPWNLPKHERSKRKIQGGS FT VLDPAERAVLRIA (in isoform 6)" FT /evidence="ECO:0000303|PubMed:8575775" FT /id="VSP_041528" FT VAR_SEQ 47..7570 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:8575775" FT /id="VSP_041529" FT VAR_SEQ 189..7570 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:10428034" FT /id="VSP_041530" FT VAR_SEQ 778..789 FT /note="AYRAAMQTQWSW -> VKLESVMVLVEY (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041531" FT VAR_SEQ 790..7570 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041532" FT VAR_SEQ 1433 FT /note="K -> IKRCKETSEHGAYSDLLQRQKATVLENSKLTGKISELERMVAELKKQ FT KSRVEEELPKVREAAENELRKQQRNVEDISLQKIRAESEAKQYRRELETIVREKEAAER FT ELERVRQLTIEAEAKRAAVEENLLNFRNQLEENTFTRRTLEDHLKRKDLSLNDLEQQKN FT KLMEELRRKRDNEEELLKLIKQMEKDLAFQKQVAEKQLKEKQKIELEARRKITEIQYTC FT RENALPVCPITQATSCRAVTGLQQEHDKQKAEELKQQVDELTAANRKAEQDMRELTYEL FT NALQLEKTSSEEKARLLKDKLDETNNTLRCLKLELERKDQAEKGYSQQLRELGRQLNQT FT TGKAEEAMQEASDLKKIKRNYQLELESLNHEKGKLQREVDRITRAHAVAEKNIQHLNSQ FT IHSFRDEKELERLQICQRKSDHLKEQFEKSHEQLLQNIKAEKENNDKIQRLNEELEKSN FT ECAEMLKQKVEELTRQNNETKLMMQRIQAESENIVLEKQTIQQRCEALKIQADGFKDQL FT RSTNEHLHKQTKTEQDFQRKIKCLEEDLAKSQNLVSEFKQKCDQQNIIIQNTKKEVRNL FT NAELNASKEEKRRGEQKVQLQQAQVQELNNRLKKVQDELHLKTIEEQMTHRKMVLFQEE FT SGKFKQSAEEFRKKMEKLMESKVITENDISGIRLDFVSLQQENSRAQENAKLCETNIKE FT LERQLQQYREQMQQGQHMEANHYQKCQKLEDELIAQKREVENLKQKMDQQIKEHEHQLV FT LLQCEIQKKSTAKDCTFKPDFEMTVKECQHSGELSSRNTGHLHPTPRSPLLRWTQEPQP FT LEEKWQHRVVEQIPKEVQFQPPGAPLEKEKSQQCYSEYFSQTSTELQITFDETNPITRL FT SEIEKIRDQALNNSRPPVRYQDNACEMELVKVLTPLEIAKNKQYDMHTEVTTLKQEKNP FT VPSAEEWMLEGCRASGGLKKGDFLKKGLEPETFQNFDGDHACSVRDDEFKFQGLRHTVT FT ARQLVEAKLLDMRTIEQLRLGLKTVEEVQKTLNKFLTKATSIAGLYLESTKEKISFASA FT AERIIIDKMVALAFLEAQAATGFIIDPISGQTYSVEDAVLKGVVDPEFRIRLLEAEKAA FT VGYSYSSKTLSVFQAMENRMLDRQKGKHILEAQIASGGVIDPVRGIRVPPEIALQQGLL FT NNAILQFLHEPSSNTRVFPNPNNKQALYYSELLRMCVFDVESQCFLFPFGERNISNLNV FT KKTHRISVVDTKTGSELTVYEAFQRNLIEKSIYLELSGQQYQWKEAMFFESYGHSSHML FT TDTKTGLHFNINEAIEQGTIDKALVKKYQEGLITLTELADSLLSRLVPKKDLHSPVAGY FT WLTASGERISVLKASRRNLVDRITALRCLEAQVSTGGIIDPLTGKKYRVAEALHRGLVD FT EGFAQQLRQCELVITGIGHPITNKMMSVVEAVNANIINKEMGIRCLEFQYLTGGLIEPQ FT VHSRLSIEEALQVGIIDVLIATKLKDQKSYVRNIICPQTKRKLTYKEALEKADFDFHTG FT LKLLEVSEPLMTGISSLYYSS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:1712022, FT ECO:0000303|PubMed:1717441, ECO:0000303|PubMed:8345227" FT /id="VSP_041533" FT VAR_SEQ 1434..7570 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:1712022, FT ECO:0000303|PubMed:1717441, ECO:0000303|PubMed:8345227" FT /id="VSP_041534" FT VAR_SEQ 1550..3635 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11751855, FT ECO:0000303|PubMed:9872452" FT /id="VSP_041535" FT VAR_SEQ 1551..3636 FT /note="Missing (in isoform 9)" FT /id="VSP_058835" FT VAR_SEQ 3387..7570 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11751855" FT /id="VSP_041536" FT VAR_SEQ 4184..4200 FT /note="GQVPLNSTALQDIISKN -> DVGTGYCRSSEQYKCHE (in isoform FT 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041537" FT VAR_SEQ 4201..7570 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041538" FT VAR_SEQ 5546..5654 FT /note="Missing (in isoform 9)" FT /id="VSP_058836" FT VAR_SEQ 7352..7375 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11751855, FT ECO:0000303|PubMed:9872452" FT /id="VSP_041539" FT VAR_SEQ 7442 FT /note="K -> KILHPLTRNYGKPWLTNSKMSTPCKAAECSDFPVPSAE (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:11751855, FT ECO:0000303|PubMed:9872452" FT /id="VSP_041540" FT VARIANT 1319 FT /note="N -> K (in dbSNP:rs35014998)" FT /id="VAR_063045" FT VARIANT 2332 FT /note="Q -> R (in dbSNP:rs16888053)" FT /id="VAR_063046" FT VARIANT 3720 FT /note="Q -> R (in dbSNP:rs4712138)" FT /id="VAR_063047" FT VARIANT 5138 FT /note="T -> A (in dbSNP:rs4715631)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_063048" FT MUTAGEN 7548 FT /note="K->Q: Loss of interaction with MAPRE1 and FT association with microtubule growing ends." FT /evidence="ECO:0000269|PubMed:19632184" FT MUTAGEN 7550 FT /note="S->A,N: Loss of association with microtubule growing FT ends." FT /evidence="ECO:0000269|PubMed:19632184" FT MUTAGEN 7552 FT /note="I->N: Loss of interaction with MAPRE1 and FT association with the growing microtubule plus ends; when FT associated with N-7553." FT /evidence="ECO:0000269|PubMed:19632184" FT MUTAGEN 7553 FT /note="P->N: Loss of interaction with MAPRE1 and FT association with the growing microtubule plus ends; when FT associated with N-7552." FT /evidence="ECO:0000269|PubMed:19632184" FT MUTAGEN 7557 FT /note="R->N: Loss of interaction with MAPRE1 and FT association with the growing microtubule plus ends." FT MUTAGEN 7558 FT /note="K->N: Loss of interaction with MAPRE1 and FT association with the growing microtubule plus ends." FT CONFLICT 573 FT /note="P -> A (in Ref. 4; BAH12207)" FT /evidence="ECO:0000305" FT CONFLICT 1177 FT /note="V -> G (in Ref. 1; M69225 and 3; AAL62061/AAL62062)" FT /evidence="ECO:0000305" FT CONFLICT 1363 FT /note="K -> E (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 4703 FT /note="R -> H (in Ref. 4; BAC04449)" FT /evidence="ECO:0000305" FT CONFLICT 4935 FT /note="N -> S (in Ref. 4; BAC04449)" FT /evidence="ECO:0000305" FT CONFLICT 5030 FT /note="E -> G (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 5177 FT /note="Q -> R (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 5225 FT /note="M -> I (in Ref. 4; BAB70870)" FT /evidence="ECO:0000305" FT CONFLICT 5299 FT /note="K -> R (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 5823 FT /note="I -> V (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 5882 FT /note="K -> R (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 5986 FT /note="L -> S (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 6080 FT /note="K -> E (in Ref. 4; BAC04848)" FT /evidence="ECO:0000305" FT CONFLICT 6186 FT /note="D -> G (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT CONFLICT 6440 FT /note="A -> G (in Ref. 3; AAL62061)" FT /evidence="ECO:0000305" FT MOD_RES Q03001-3:1565 FT /note="Phosphoserine" FT /evidence="ECO:0000305" FT CONFLICT Q03001-3:1644 FT /note="R -> T (in Ref. 1; M69225)" FT /evidence="ECO:0000305" FT CONFLICT Q03001-3:1943 FT /note="G -> R (in Ref. 13; CAA41528)" FT /evidence="ECO:0000305" FT CONFLICT Q03001-3:2364 FT /note="S -> T (in Ref. 1; M69225)" FT /evidence="ECO:0000305" FT CONFLICT Q03001-3:2495 FT /note="G -> V (in Ref. 1; M69225)" FT /evidence="ECO:0000305" FT CONFLICT Q03001-3:2543 FT /note="N -> K (in Ref. 1; M69225)" FT /evidence="ECO:0000305" FT CONFLICT Q03001-3:2621 FT /note="A -> P (in Ref. 1; M69225)" FT /evidence="ECO:0000305" FT MOD_RES Q03001-11:135 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CONFLICT Q03001-11:48 FT /note="P -> L (in Ref. 7; AAC50244)" FT /evidence="ECO:0000305" FT MOD_RES Q03001-13:184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" SQ SEQUENCE 7570 AA; 860662 MW; 1EA992E53D1C243E CRC64; MAGYLSPAAY LYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG IRCENFTTCW RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VTTMSERTFP NNPVELKALY NQYLQFKETE IPPKETEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLEMLQQIA NRVQRDSVIC EDKLILAGNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRIL TTEQTKLMIS GITQSLNSGF AQTLHPSLTS GLTQSLTPSL TSSSMTSGLS SGMTSRLTPS VTPAYTPGFP SGLVPNFSSG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE EEINMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI SEIQMTAPLK LTYAEKLHRL ESQYAKLLNT SRNQERHLDT LHNFVSRATN ELIWLNEKEE EEVAYDWSER NTNIARKKDY HAELMRELDQ KEENIKSVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH IKENTAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES MEEKEELLQY KSTIANLMGK AKTIIQLKPR NSDCPLKTSI PIKAICDYRQ IEITIYKDDE CVLANNSHRA KWKVISPTGN EAMVPSVCFT VPPPNKEAVD LANRIEQQYQ NVLTLWHESH INMKSVVSWH YLINEIDRIR ASNVASIKTM LPGEHQQVLS NLQSRFEDFL EDSQESQVFS GSDITQLEKE VNVCKQYYQE LLKSAEREEQ EESVYNLYIS EVRNIRLRLE NCEDRLIRQI RTPLERDDLH ESVFRITEQE KLKKELERLK DDLGTITNKC EEFFSQAAAS SSVPTLRSEL NVVLQNMNQV YSMSSTYIDK LKTVNLVLKN TQAAEALVKL YETKLCEEEA VIADKNNIEN LISTLKQWRS EVDEKRQVFH ALEDELQKAK AISDEMFKTY KERDLDFDWH KEKADQLVER WQNVHVQIDN RLRDLEGIGK SLKYYRDTYH PLDDWIQQVE TTQRKIQENQ PENSKTLATQ LNQQKMLVSE IEMKQSKMDE CQKYAEQYSA TVKDYELQTM TYRAMVDSQQ KSPVKRRRMQ SSADLIIQEF MDLRTRYTAL VTLMTQYIKF AGDSLKRLEE EEKSLEEEKK EHVEKAKELQ KWVSNISKTL KDAEKAGKPP FSKQKISSEE ISTKKEQLSE ALQTIQLFLA KHGDKMTDEE RNELEKQVKT LQESYNLLFS ESLKQLQESQ TSGDVKVEEK LDKVIAGTID QTTGEVLSVF QAVLRGLIDY DTGIRLLETQ LMISGLISPE LRKCFDLKDA KSHGLIDEQI LCQLKELSKA KEIISAASPT TIPVLDALAQ SMITESMAIK VLEILLSTGS LVIPATGEQL TLQKAFQQNL VSSALFSKVL ERQNMCKDLI DPCTSEKVSL IDMVQRSTLQ ENTGMWLLPV RPQEGGRITL KCGRNISILR AAHEGLIDRE TMFRLLSAQL LSGGLINSNS GQRMTVEEAV REGVIDRDTA SSILTYQVQT GGIIQSNPAK RLTVDEAVQC DLITSSSALL VLEAQRGYVG LIWPHSGEIF PTSSSLQQEL ITNELAYKIL NGRQKIAALY IPESSQVIGL DAAKQLGIID NNTASILKNI TLPDKMPDLG DLEACKNARR WLSFCKFQPS TVHDYRQEED VFDGEEPVTT QTSEETKKLF LSYLMINSYM DANTGQRLLL YDGDLDEAVG MLLEGCHAEF DGNTAIKECL DVLSSSGVFL NNASGREKDE CTATPSSFNK CHCGEPEHEE TPENRKCAID EEFNEMRNTV INSEFSQSGK LASTISIDPK VNSSPSVCVP SLISYLTQTE LADISMLRSD SENILTNYEN QSRVETNERA NECSHSKNIQ NFPSDLIENP IMKSKMSKFC GVNETENEDN TNRDSPIFDY SPRLSALLSH DKLMHSQGSF NDTHTPESNG NKCEAPALSF SDKTMLSGQR IGEKFQDQFL GIAAINISLP GEQYGQKSLN MISSNPQVQY HNDKYISNTS GEDEKTHPGF QQMPEDKEDE SEIEEYSCAV TPGGDTDNAI VSLTCATPLL DETISASDYE TSLLNDQQNN TGTDTDSDDD FYDTPLFEDD DHDSLLLDGD DRDCLHPEDY DTLQEENDET ASPADVFYDV SKENENSMVP QGAPVGSLSV KNKAHCLQDF LMDVEKDELD SGEKIHLNPV GSDKVNGQSL ETGSERECTN ILEGDESDSL TDYDIVGGKE SFTASLKFDD SGSWRGRKEE YVTGQEFHSD TDHLDSMQSE ESYGDYIYDS NDQDDDDDDG IDEEGGGIRD ENGKPRCQNV AEDMDIQLCA SILNENSDEN ENINTMILLD KMHSCSSLEK QQRVNVVQLA SPSENNLVTE KSNLPEYTTE IAGKSKENLL NHEMVLKDVL PPIIKDTESE KTFGPASISH DNNNISSTSE LGTDLANTKV KLIQGSELPE LTDSVKGKDE YFKNMTPKVD SSLDHIICTE PDLIGKPAEE SHLSLIASVT DKDPQGNGSD LIKGRDGKSD ILIEDETSIQ KMYLGEGEVL VEGLVEEENR HLKLLPGKNT RDSFKLINSQ FPFPQITNNE ELNQKGSLKK ATVTLKDEPN NLQIIVSKSP VQFENLEEIF DTSVSKEISD DITSDITSWE GNTHFEESFT DGPEKELDLF TYLKHCAKNI KAKDVAKPNE DVPSHVLITA PPMKEHLQLG VNNTKEKSTS TQKDSPLNDM IQSNDLCSKE SISGGGTEIS QFTPESIEAT LSILSRKHVE DVGKNDFLQS ERCANGLGND NSSNTLNTDY SFLEINNKKE RIEQQLPKEQ ALSPRSQEKE VQIPELSQVF VEDVKDILKS RLKEGHMNPQ EVEEPSACAD TKILIQNLIK RITTSQLVNE ASTVPSDSQM SDSSGVSPMT NSSELKPESR DDPFCIGNLK SELLLNILKQ DQHSQKITGV FELMRELTHM EYDLEKRGIT SKVLPLQLEN IFYKLLADGY SEKIEHVGDF NQKACSTSEM MEEKPHILGD IKSKEGNYYS PNLETVKEIG LESSTVWAST LPRDEKLKDL CNDFPSHLEC TSGSKEMASG DSSTEQFSSE LQQCLQHTEK MHEYLTLLQD MKPPLDNQES LDNNLEALKN QLRQLETFEL GLAPIAVILR KDMKLAEEFL KSLPSDFPRG HVEELSISHQ SLKTAFSSLS NVSSERTKQI MLAIDSEMSK LAVSHEEFLH KLKSFSDWVS EKSKSVKDIE IVNVQDSEYV KKRLEFLKNV LKDLGHTKMQ LETTAFDVQF FISEYAQDLS PNQSKQLLRL LNTTQKCFLD VQESVTTQVE RLETQLHLEQ DLDDQKIVAE RQQEYKEKLQ GICDLLTQTE NRLIGHQEAF MIGDGTVELK KYQSKQEELQ KDMQGSAQAL AEVVKNTENF LKENGEKLSQ EDKALIEQKL NEAKIKCEQL NLKAEQSKKE LDKVVTTAIK EETEKVAAVK QLEESKTKIE NLLDWLSNVD KDSERAGTKH KQVIEQNGTH FQEGDGKSAI GEEDEVNGNL LETDVDGQVG TTQENLNQQY QKVKAQHEKI ISQHQAVIIA TQSAQVLLEK QGQYLSPEEK EKLQKNMKEL KVHYETALAE SEKKMKLTHS LQEELEKFDA DYTEFEHWLQ QSEQELENLE AGADDINGLM TKLKRQKSFS EDVISHKGDL RYITISGNRV LEAAKSCSKR DGGKVDTSAT HREVQRKLDH ATDRFRSLYS KCNVLGNNLK DLVDKYQHYE DASCGLLAGL QACEATASKH LSEPIAVDPK NLQRQLEETK ALQGQISSQQ VAVEKLKKTA EVLLDARGSL LPAKNDIQKT LDDIVGRYED LSKSVNERNE KLQITLTRSL SVQDGLDEML DWMGNVESSL KEQGQVPLNS TALQDIISKN IMLEQDIAGR QSSINAMNEK VKKFMETTDP STASSLQAKM KDLSARFSEA SHKHKETLAK MEELKTKVEL FENLSEKLQT FLETKTQALT EVDVPGKDVT ELSQYMQEST SEFLEHKKHL EVLHSLLKEI SSHGLPSDKA LVLEKTNNLS KKFKEMEDTI KEKKEAVTSC QEQLDAFQVL VKSLKSWIKE TTKKVPIVQP SFGAEDLGKS LEDTKKLQEK WSLKTPEIQK VNNSGISLCN LISAVTTPAK AIAAVKSGGA VLNGEGTATN TEEFWANKGL TSIKKDMTDI SHGYEDLGLL LKDKIAELNT KLSKLQKAQE ESSAMMQWLQ KMNKTATKWQ QTPAPTDTEA VKTQVEQNKS FEAELKQNVN KVQELKDKLT ELLEENPDTP EAPRWKQMLT EIDSKWQELN QLTIDRQQKL EESSNNLTQF QTVEAQLKQW LVEKELMVSV LGPLSIDPNM LNTQRQQVQI LLQEFATRKP QYEQLTAAGQ GILSRPGEDP SLRGIVKEQL AAVTQKWDSL TGQLSDRCDW IDQAIVKSTQ YQSLLRSLSD KLSDLDNKLS SSLAVSTHPD AMNQQLETAQ KMKQEIQQEK KQIKVAQALC EDLSALVKEE YLKAELSRQL EGILKSFKDV EQKAENHVQH LQSACASSHQ FQQMSRDFQA WLDTKKEEQN KSHPISAKLD VLESLIKDHK DFSKTLTAQS HMYEKTIAEG ENLLLKTQGS EKAALQLQLN TIKTNWDTFN KQVKERENKL KESLEKALKY KEQVETLWPW IDKCQNNLEE IKFCLDPAEG ENSIAKLKSL QKEMDQHFGM VELLNNTANS LLSVCEIDKE VVTDENKSLI QKVDMVTEQL HSKKFCLENM TQKFKEFQEV SKESKRQLQC AKEQLDIHDS LGSQAYSNKY LTMLQTQQKS LQALKHQVDL AKRLAQDLVV EASDSKGTSD VLLQVETIAQ EHSTLSQQVD EKCSFLETKL QGIGHFQNTI REMFSQFAEF DDELDSMAPV GRDAETLQKQ KETIKAFLKK LEALMASNDN ANKTCKMMLA TEETSPDLVG IKRDLEALSK QCNKLLDRAQ AREEQVEGTI KRLEEFYSKL KEFSILLQKA EEHEESQGPV GMETETINQQ LNMFKVFQKE EIEPLQGKQQ DVNWLGQGLI QSAAKSTSTQ GLEHDLDDVN ARWKTLNKKV AQRAAQLQEA LLHCGRFQDA LESLLSWMVD TEELVANQKP PSAEFKVVKA QIQEQKLLQR LLDDRKSTVE VIKREGEKIA TTAEPADKVK ILKQLSLLDS RWEALLNKAE TRNRQLEGIS VVAQQFHETL EPLNEWLTTI EKRLVNCEPI GTQASKLEEQ IAQHKALEDD IINHNKHLHQ AVSIGQSLKV LSSREDKDMV QSKLDFSQVW YIEIQEKSHS RSELLQQALC NAKIFGEDEV ELMNWLNEVH DKLSKLSVQD YSTEGLWKQQ SELRVLQEDI LLRKQNVDQA LLNGLELLKQ TTGDEVLIIQ DKLEAIKARY KDITKLSTDV AKTLEQALQL ARRLHSTHEE LCTWLDKVEV ELLSYETQVL KGEEASQAQM RPKELKKEAK NNKALLDSLN EVSSALLELV PWRAREGLEK MVAEDNERYR LVSDTITQKV EEIDAAILRS QQFDQAADAE LSWITETEKK LMSLGDIRLE QDQTSAQLQV QKTFTMEILR HKDIIDDLVK SGHKIMTACS EEEKQSMKKK LDKVLKNYDT ICQINSERYL QLERAQSLVN QFWETYEELW PWLTETQSII SQLPAPALEY ETLRQQQEEH RQLRELIAEH KPHIDKMNKT GPQLLELSPG EGFSIQEKYV AADTLYSQIK EDVKKRAVAL DEAISQSTQF HDKIDQILES LERIVERLRQ PPSISAEVEK IKEQISENKN VSVDMEKLQP LYETLKQRGE EMIARSGGTD KDISAKAVQD KLDQMVFIWE NIHTLVEERE AKLLDVMELA EKFWCDHMSL IVTIKDTQDF IRDLEDPGID PSVVKQQQEA AETIREEIDG LQEELDIVIN LGSELIAACG EPDKPIVKKS IDELNSAWDS LNKAWKDRID KLEEAMQAAV QYQDGLQAVF DWVDIAGGKL ASMSPIGTDL ETVKQQIEEL KQFKSEAYQQ QIEMERLNHQ AELLLKKVTE ESDKHTVQDP LMELKLIWDS LEERIINRQH KLEGALLALG QFQHALDELL AWLTHTEGLL SEQKPVGGDP KAIEIELAKH HVLQNDVLAH QSTVEAVNKA GNDLIESSAG EEASNLQNKL EVLNQRWQNV LEKTEQRKQQ LDGALRQAKG FHGEIEDLQQ WLTDTERHLL ASKPLGGLPE TAKEQLNVHM EVCAAFEAKE ETYKSLMQKG QQMLARCPKS AETNIDQDIN NLKEKWESVE TKLNERKTKL EEALNLAMEF HNSLQDFINW LTQAEQTLNV ASRPSLILDT VLFQIDEHKV FANEVNSHRE QIIELDKTGT HLKYFSQKQD VVLIKNLLIS VQSRWEKVVQ RLVERGRSLD DARKRAKQFH EAWSKLMEWL EESEKSLDSE LEIANDPDKI KTQLAQHKEF QKSLGAKHSV YDTTNRTGRS LKEKTSLADD NLKLDDMLSE LRDKWDTICG KSVERQNKLE EALLFSGQFT DALQALIDWL YRVEPQLAED QPVHGDIDLV MNLIDNHKAF QKELGKRTSS VQALKRSARE LIEGSRDDSS WVKVQMQELS TRWETVCALS ISKQTRLEAA LRQAEEFHSV VHALLEWLAE AEQTLRFHGV LPDDEDALRT LIDQHKEFMK KLEEKRAELN KATTMGDTVL AICHPDSITT IKHWITIIRA RFEEVLAWAK QHQQRLASAL AGLIAKQELL EALLAWLQWA ETTLTDKDKE VIPQEIEEVK ALIAEHQTFM EEMTRKQPDV DKVTKTYKRR AADPSSLQSH IPVLDKGRAG RKRFPASSLY PSGSQTQIET KNPRVNLLVS KWQQVWLLAL ERRRKLNDAL DRLEELREFA NFDFDIWRKK YMRWMNHKKS RVMDFFRRID KDQDGKITRQ EFIDGILSSK FPTSRLEMSA VADIFDRDGD GYIDYYEFVA ALHPNKDAYK PITDADKIED EVTRQVAKCK CAKRFQVEQI GDNKYRFFLG NQFGDSQQLR LVRILRSTVM VRVGGGWMAL DEFLVKNDPC RVHHHGSKML RSESNSSITT TQPTIAKGRT NMELREKFIL ADGASQGMAA FRPRGRRSRP SSRGASPNRS TSVSSQAAQA ASPQVPATTT PKGTPIQGSK LRLPGYLSGK GFHSGEDSGL ITTAAARVRT QFADSKKTPS RPGSRAGSKA GSRASSRRGS DASDFDISEI QSVCSDVETV PQTHRPTPRA GSRPSTAKPS KIPTPQRKSP ASKLDKSSKR //