DMD_HUMAN
ID DMD_HUMAN Reviewed; 3685 AA.
AC P11532; A1L0U9; E7EQR9; E7EQS5; E7ESB2; E9PDN1; E9PDN5; F5GZY3; F8VX32;
AC Q02295; Q14169; Q14170; Q5JYU0; Q6NSJ9; Q7KZ48; Q8N754; Q9UCW3; Q9UCW4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 254.
DE RecName: Full=Dystrophin;
GN Name=DMD;
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 1), AND VARIANTS GLY-882; LEU-1469 AND
RP GLN-2366.
RC TISSUE=Muscle;
RX PubMed=3282674; DOI=10.1016/0092-8674(88)90383-2;
RA Koenig M., Monaco A.P., Kunkel L.M.;
RT "The complete sequence of dystrophin predicts a rod-shaped cytoskeletal
RT protein.";
RL Cell 53:219-228(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-133; ILE-623;
RP GLY-784; GLY-882; PHE-1197; ASN-1377; HIS-1745 AND SER-1844.
RX PubMed=2668885; DOI=10.1093/nar/17.13.5391;
RA Rosenthal A., Speer A., Billowitz H., Cross G.S., Forrest S.N.,
RA Davies K.E.;
RT "Two human cDNA molecules coding for the Duchenne muscular dystrophy (DMD)
RT locus are highly homologous.";
RL Nucleic Acids Res. 17:5391-5391(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 15), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1319059; DOI=10.1073/pnas.89.12.5346;
RA Lederfein D., Levy Z., Augier N., Mornet D., Morris G., Fuchs O., Yaffe D.,
RA Nudel U.;
RT "A 71-kilodalton protein is a major product of the Duchenne muscular
RT dystrophy gene in brain and other nonmuscle tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5346-5350(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-2937.
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6; 13 AND 14).
RC TISSUE=Brain, Placenta, and Testis;
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 [GENOMIC DNA] OF 1-1411 (ISOFORMS 4 AND 5).
RC TISSUE=Retina;
RA White R.A.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-497 (ISOFORM 1).
RX PubMed=3607877; DOI=10.1016/0092-8674(87)90504-6;
RA Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C.,
RA Kunkel L.M.;
RT "Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and
RT preliminary genomic organization of the DMD gene in normal and affected
RT individuals.";
RL Cell 50:509-517(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-32 (ISOFORM 2), ALTERNATIVE PROMOTER USAGE,
RP AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=2648158; DOI=10.1038/338509a0;
RA Feener C.A., Koenig M., Kunkel L.M.;
RT "Alternative splicing of human dystrophin mRNA generates isoforms at the
RT carboxy terminus.";
RL Nature 338:509-511(1989).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 404-1137, AND VARIANT GLY-882.
RX PubMed=3428261; DOI=10.1002/j.1460-2075.1987.tb02646.x;
RA Cross G.S., Speer A., Rosenthal A., Forrest S.M., Smith T.J., Edwards Y.,
RA Flint T., Hill D., Davies K.E.;
RT "Deletions of fetal and adult muscle cDNA in Duchenne and Becker muscular
RT dystrophy patients.";
RL EMBO J. 6:3277-3283(1987).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 665-722; 2098-2204 AND 2305-2366.
RX PubMed=3205741; DOI=10.1093/nar/16.23.11141;
RA Chamberlain J.S., Gibbs R.A., Ranier J.A., Nguyen P.N., Caskey C.T.;
RT "Deletion screening of the Duchenne muscular dystrophy locus via multiplex
RT DNA amplification.";
RL Nucleic Acids Res. 16:11141-11156(1988).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2147-2204.
RX PubMed=2569720; DOI=10.1093/nar/17.14.5611;
RA Blonden L.A.J., den Dunnen J.T., van Paassen H.M.B., Wapenaar M.C.,
RA Grootscholten P.M., Ginjaar H.B., Bakker E., Pearson P.L.,
RA van Ommen G.J.B.;
RT "High resolution deletion breakpoint mapping in the DMD gene by whole
RT cosmid hybridization.";
RL Nucleic Acids Res. 17:5611-5621(1989).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2305-2364.
RA Huth A., Will K., Speer A., Bauer D.;
RT "Differences in introns flanking exon 48 of the DMD/BMD gene.";
RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3670-3685, AND TISSUE SPECIFICITY.
RC TISSUE=Amnion;
RX PubMed=8541829; DOI=10.1093/hmg/4.9.1475;
RA Austin R.C., Howard P.L., D'Souza V.N., Klamut H.J., Ray P.N.;
RT "Cloning and characterization of alternatively spliced isoforms of Dp71.";
RL Hum. Mol. Genet. 4:1475-1483(1995).
RN [15]
RP ANALYSIS OF THE DOMAIN STRUCTURE.
RX PubMed=2407739; DOI=10.1016/s0021-9258(19)39599-7;
RA Koenig M., Kunkel L.M.;
RT "Detailed analysis of the repeat domain of dystrophin reveals four
RT potential hinge segments that may confer flexibility.";
RL J. Biol. Chem. 265:4560-4566(1990).
RN [16]
RP INTERACTION WITH DAG1.
RX PubMed=7592992; DOI=10.1074/jbc.270.45.27305;
RA Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P.;
RT "Identification and characterization of the dystrophin anchoring site on
RT beta-dystroglycan.";
RL J. Biol. Chem. 270:27305-27310(1995).
RN [17]
RP INTERACTION WITH SNTB1.
RX PubMed=7844150; DOI=10.1083/jcb.128.3.363;
RA Ahn A.H., Kunkel L.M.;
RT "Syntrophin binds to an alternatively spliced exon of dystrophin.";
RL J. Cell Biol. 128:363-371(1995).
RN [18]
RP INTERACTION WITH SNTA1 AND SNTB2.
RX PubMed=8576247; DOI=10.1074/jbc.271.5.2724;
RA Ahn A.H., Feener C.A., Gussoni E., Yoshida M., Ozawa E., Kunkel L.M.;
RT "The three human syntrophin genes are expressed in diverse tissues, have
RT distinct chromosomal locations, and each bind to dystrophin and its
RT relatives.";
RL J. Biol. Chem. 271:2724-2730(1996).
RN [19]
RP ALTERNATIVE SPLICING (ISOFORMS 15 AND 16), AND DEVELOPMENTAL STAGE.
RC TISSUE=Telencephalon;
RX PubMed=9370062; DOI=10.1016/s0165-3806(97)00122-3;
RA Ceccarini M., Rizzo G., Rosa G., Chelucci C., Macioce P., Petrucci T.C.;
RT "A splice variant of Dp71 lacking the syntrophin binding site is expressed
RT in early stages of human neural development.";
RL Brain Res. Dev. Brain Res. 103:77-82(1997).
RN [20]
RP INTERACTION WITH SNTG1 AND SNTG2.
RX PubMed=10747910; DOI=10.1074/jbc.m000439200;
RA Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C., Servidei S.,
RA Puca A.A., Tonali P., Puca G.A., Nigro V.;
RT "Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins
RT localized in neuronal cells.";
RL J. Biol. Chem. 275:15851-15860(2000).
RN [21]
RP ALTERNATIVE SPLICING (ISOFORM 16).
RC TISSUE=Brain;
RX PubMed=10734266; DOI=10.1016/s0960-8966(99)00105-4;
RA Austin R.C., Morris G.E., Howard P.L., Klamut H.J., Ray P.N.;
RT "Expression and synthesis of alternatively spliced variants of Dp71 in
RT adult human brain.";
RL Neuromuscul. Disord. 10:187-193(2000).
RN [22]
RP INTERACTION WITH DAG1.
RX PubMed=11495720; DOI=10.1016/s0898-6568(01)00188-7;
RA Ilsley J.L., Sudol M., Winder S.J.;
RT "The interaction of dystrophin with beta-dystroglycan is regulated by
RT tyrosine phosphorylation.";
RL Cell. Signal. 13:625-632(2001).
RN [23]
RP REVIEW ON ALTERNATIVE PROMOTER USAGE.
RX PubMed=14636778; DOI=10.1016/s1474-4422(03)00585-4;
RA Muntoni F., Torelli S., Ferlini A.;
RT "Dystrophin and mutations: one gene, several proteins, multiple
RT phenotypes.";
RL Lancet Neurol. 2:731-740(2003).
RN [24]
RP INTERACTION WITH KRT19, AND TISSUE SPECIFICITY.
RX PubMed=16000376; DOI=10.1091/mbc.e05-02-0112;
RA Stone M.R., O'Neill A., Catino D., Bloch R.J.;
RT "Specific interaction of the actin-binding domain of dystrophin with
RT intermediate filaments containing keratin 19.";
RL Mol. Biol. Cell 16:4280-4293(2005).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [26]
RP FUNCTION IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
RX PubMed=16710609; DOI=10.1007/s00018-005-5461-0;
RA Haenggi T., Fritschy J.M.;
RT "Role of dystrophin and utrophin for assembly and function of the
RT dystrophin glycoprotein complex in non-muscle tissue.";
RL Cell. Mol. Life Sci. 63:1614-1631(2006).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3483; SER-3613; SER-3617;
RP SER-3623 AND SER-3666, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340;
RP SER-344 AND SER-348 (ISOFORMS 13 AND 15), AND IDENTIFICATION BY MASS
RP 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 [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3613 AND SER-3623,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3612; SER-3623 AND SER-3624,
RP AND IDENTIFICATION BY MASS 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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3490; SER-3500; SER-3623;
RP SER-3624 AND SER-3666, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-616
RP (ISOFORM 15), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-629 (ISOFORM
RP 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519 (ISOFORM 16), AND
RP IDENTIFICATION BY MASS 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 [33]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3046-3306 IN COMPLEX WITH DAG1,
RP AND INTERACTION WITH DAG1.
RX PubMed=10932245; DOI=10.1038/77923;
RA Huang X., Poy F., Zhang R., Joachimiak A., Sudol M., Eck M.J.;
RT "Structure of a WW domain containing fragment of dystrophin in complex with
RT beta-dystroglycan.";
RL Nat. Struct. Biol. 7:634-638(2000).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-246.
RX PubMed=10801490; DOI=10.1016/s0969-2126(00)00132-5;
RA Norwood F.L.M., Sutherland-Smith A.J., Keep N.H., Kendrick-Jones J.;
RT "The structure of the N-terminal actin-binding domain of human dystrophin
RT and how mutations in this domain may cause Duchenne or Becker muscular
RT dystrophy.";
RL Structure 8:481-491(2000).
RN [35]
RP REVIEW ON DMD VARIANTS.
RX PubMed=7951253; DOI=10.1002/humu.1380040102;
RA Roberts R.G., Gardner R.J., Bobrow M.;
RT "Searching for the 1 in 2,400,000: a review of dystrophin gene point
RT mutations.";
RL Hum. Mutat. 4:1-11(1994).
RN [36]
RP REVIEW ON VARIANTS.
RX PubMed=8045556; DOI=10.1007/bf00202854;
RA Rininsland F., Reiss J.;
RT "Microlesions and polymorphisms in the Duchenne/Becker muscular dystrophy
RT gene.";
RL Hum. Genet. 94:111-116(1994).
RN [37]
RP VARIANT DMD ARG-54.
RX PubMed=8401582; DOI=10.1038/ng0893-357;
RA Prior T.W., Papp A.C., Snyder P.J., Burghes A.H.M., Bartolo C., Sedra M.S.,
RA Western L.M., Mendell J.R.;
RT "A missense mutation in the dystrophin gene in a Duchenne muscular
RT dystrophy patient.";
RL Nat. Genet. 4:357-360(1993).
RN [38]
RP VARIANT DMD GLY-645.
RX PubMed=7981690; DOI=10.1093/hmg/3.7.1173;
RA Prior T.W., Bartolo C., Papp A.C., Snyder P.J., Sedra M.S., Burghes A.H.,
RA Mendell J.R.;
RT "Identification of a missense mutation, single base deletion and a
RT polymorphism in the dystrophin exon 16.";
RL Hum. Mol. Genet. 3:1173-1174(1994).
RN [39]
RP VARIANTS HIS-365; TRP-2191 AND ARG-2937.
RX PubMed=7849724; DOI=10.1093/hmg/3.10.1907;
RA Nigro V., Nigro G., Esposito M.G., Comi L.I., Molinari A.M., Puca G.A.,
RA Politano L.;
RT "Novel small mutations along the DMD/BMD gene associated with different
RT phenotypes.";
RL Hum. Mol. Genet. 3:1907-1908(1994).
RN [40]
RP VARIANT DMD TYR-3340.
RX PubMed=8817332; DOI=10.1093/hmg/5.7.973;
RA Lenk U., Oexle K., Voit T., Ancker U., Hellner K.A., Speer A., Hubner C.;
RT "A cysteine 3340 substitution in the dystroglycan-binding domain of
RT dystrophin associated with Duchenne muscular dystrophy, mental retardation
RT and absence of the ERG b-wave.";
RL Hum. Mol. Genet. 5:973-975(1996).
RN [41]
RP VARIANT CMD3B ALA-279.
RX PubMed=9170407; DOI=10.1161/01.cir.95.10.2434;
RA Ortiz-Lopez R., Li H., Su J., Goytia V., Towbin J.A.;
RT "Evidence for a dystrophin missense mutation as a cause of X-linked dilated
RT cardiomyopathy.";
RL Circulation 95:2434-2440(1997).
RN [42]
RP VARIANT DMD HIS-3335.
RX PubMed=9851445; DOI=10.1002/ana.410440619;
RA Goldberg L.R., Hausmanowa-Petrusewicz I., Fidzianska A., Duggan D.J.,
RA Steinberg L.S., Hoffman E.P.;
RT "A dystrophin missense mutation showing persistence of dystrophin and
RT dystrophin-associated proteins yet a severe phenotype.";
RL Ann. Neurol. 44:971-976(1998).
RN [43]
RP VARIANT BMD PRO-171.
RX PubMed=10573008; DOI=10.1038/sj.ejhg.5200370;
RA Eraslan S., Kayserili H., Apak M.Y., Kirdar B.;
RT "Identification of point mutations in Turkish DMD/BMD families using
RT multiplex-single stranded conformation analysis (SSCA).";
RL Eur. J. Hum. Genet. 7:765-770(1999).
RN [44]
RP VARIANT LYS-1672.
RX PubMed=12354438; DOI=10.1016/s0735-1097(02)02126-5;
RA Feng J., Yan J.Y., Buzin C.H., Sommer S.S., Towbin J.A.;
RT "Comprehensive mutation scanning of the dystrophin gene in patients with
RT nonsyndromic X-linked dilated cardiomyopathy.";
RL J. Am. Coll. Cardiol. 40:1120-1124(2002).
RN [45]
RP VARIANTS CMD3B ASN-18 AND LEU-3228, AND VARIANTS TRP-2155; THR-2299;
RP GLN-2366; VAL-2910; ASP-2912 AND ARG-2937.
RX PubMed=12359139; DOI=10.1016/s1096-7192(02)00153-1;
RA Feng J., Yan J., Buzin C.H., Towbin J.A., Sommer S.S.;
RT "Mutations in the dystrophin gene are associated with sporadic dilated
RT cardiomyopathy.";
RL Mol. Genet. Metab. 77:119-126(2002).
RN [46]
RP VARIANT DMD PHE-3313, AND VARIANT VAL-165.
RX PubMed=12632325; DOI=10.1086/374176;
RA Flanigan K.M., von Niederhausern A., Dunn D.M., Alder J., Mendell J.R.,
RA Weiss R.B.;
RT "Rapid direct sequence analysis of the dystrophin gene.";
RL Am. J. Hum. Genet. 72:931-939(2003).
RN [47]
RP VARIANTS [LARGE SCALE ANALYSIS] PHE-334; GLN-1219; HIS-1470 AND VAL-2164.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [48]
RP VARIANT ARG-118.
RX PubMed=21396098; DOI=10.1186/1471-2350-12-37;
RA Magri F., Del Bo R., D'Angelo M.G., Govoni A., Ghezzi S., Gandossini S.,
RA Sciacco M., Ciscato P., Bordoni A., Tedeschi S., Fortunato F., Lucchini V.,
RA Cereda M., Corti S., Moggio M., Bresolin N., Comi G.P.;
RT "Clinical and molecular characterization of a cohort of patients with novel
RT nucleotide alterations of the Dystrophin gene detected by direct
RT sequencing.";
RL BMC Med. Genet. 12:37-37(2011).
RN [49]
RP CHARACTERIZATION OF VARIANTS DMD PHE-3313; HIS-3335 AND TYR-3340.
RX PubMed=24302611; DOI=10.1002/humu.22479;
RA Vulin A., Wein N., Strandjord D.M., Johnson E.K., Findlay A.R., Maiti B.,
RA Howard M.T., Kaminoh Y.J., Taylor L.E., Simmons T.R., Ray W.C.,
RA Montanaro F., Ervasti J.M., Flanigan K.M.;
RT "The ZZ domain of dystrophin in DMD: making sense of missense mutations.";
RL Hum. Mutat. 35:257-264(2014).
RN [50]
RP CHARACTERIZATION OF VARIANT CMD3B ASN-18.
RX PubMed=25340340; DOI=10.1371/journal.pone.0110439;
RA Singh S.M., Bandi S., Shah D.D., Armstrong G., Mallela K.M.;
RT "Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated
RT cardiomyopathy decreases protein stability, increases protein unfolding,
RT and perturbs protein structure, but does not affect protein function.";
RL PLoS ONE 9:E110439-E110439(2014).
CC -!- FUNCTION: Anchors the extracellular matrix to the cytoskeleton via F-
CC actin. Ligand for dystroglycan. Component of the dystrophin-associated
CC glycoprotein complex which accumulates at the neuromuscular junction
CC (NMJ) and at a variety of synapses in the peripheral and central
CC nervous systems and has a structural function in stabilizing the
CC sarcolemma. Also implicated in signaling events and synaptic
CC transmission. {ECO:0000250|UniProtKB:P11531,
CC ECO:0000269|PubMed:16710609}.
CC -!- SUBUNIT: Interacts with SYNM (By similarity). Interacts with the
CC syntrophins SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2 (PubMed:7844150,
CC PubMed:8576247). Interacts with KRT19 (PubMed:16000376). Component of
CC the dystrophin-associated glycoprotein complex which is composed of
CC three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN),
CC DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and
CC SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-
CC sarcospan complex. Interacts with DAG1 (betaDAG1) with DMD; the
CC interaction is inhibited by phosphorylation on the PPXY motif of DAG1
CC (PubMed:7592992, PubMed:11495720, PubMed:10932245). Interacts with
CC CMYA5 (By similarity). Directly interacts with ANK2 and ANK3; these
CC interactions do not interfere with betaDAG1-binding and are necessary
CC for proper localization in muscle cells (By similarity). Identified in
CC a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and
CC DAG1 (By similarity). Interacts with DTNB (By similarity). Interacts
CC with PGM5; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P11530, ECO:0000250|UniProtKB:P11531,
CC ECO:0000269|PubMed:10932245, ECO:0000269|PubMed:11495720,
CC ECO:0000269|PubMed:16000376, ECO:0000269|PubMed:7592992,
CC ECO:0000269|PubMed:7844150, ECO:0000269|PubMed:8576247}.
CC -!- INTERACTION:
CC P11532; Q9UBT7: CTNNAL1; NbExp=8; IntAct=EBI-295827, EBI-514206;
CC P11532; O60941: DTNB; NbExp=4; IntAct=EBI-295827, EBI-740402;
CC P11532; O60941-5: DTNB; NbExp=3; IntAct=EBI-295827, EBI-11984733;
CC P11532; Q96CS2: HAUS1; NbExp=4; IntAct=EBI-295827, EBI-2514791;
CC P11532; P41235-3: HNF4A; NbExp=3; IntAct=EBI-295827, EBI-12690684;
CC P11532; P08727: KRT19; NbExp=2; IntAct=EBI-295827, EBI-742756;
CC P11532; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-295827, EBI-79165;
CC P11532; Q13884: SNTB1; NbExp=4; IntAct=EBI-295827, EBI-295843;
CC P11532; Q13425: SNTB2; NbExp=2; IntAct=EBI-295827, EBI-80411;
CC P11532-5; Q01484: ANK2; NbExp=2; IntAct=EBI-1018651, EBI-941975;
CC P11532-5; Q3T1J5: Ank3; Xeno; NbExp=2; IntAct=EBI-1018651, EBI-2133962;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P11531}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P11531}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P11531}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P11531}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P11531}. Note=In muscle cells, sarcolemma
CC localization requires the presence of ANK2, while localization to
CC costameres requires the presence of ANK3. Localizes to neuromuscular
CC junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2
CC presence, but not in newborn animals. {ECO:0000250|UniProtKB:P11531}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=17;
CC Name=1; Synonyms=Dystrophin-4, Dp427m;
CC IsoId=P11532-1; Sequence=Displayed;
CC Name=2; Synonyms=Dystrophin-3, Dp427c;
CC IsoId=P11532-4; Sequence=VSP_006809;
CC Name=3; Synonyms=Dp427p;
CC IsoId=P11532-11; Sequence=VSP_060274;
CC Name=4; Synonyms=Dystrophin-1, Dp260-1;
CC IsoId=P11532-2; Sequence=VSP_006806, VSP_006807;
CC Name=5; Synonyms=Dystrophin-2, Dp260-2;
CC IsoId=P11532-3; Sequence=VSP_006808, VSP_006807;
CC Name=6; Synonyms=Dp140;
CC IsoId=P11532-12; Sequence=VSP_060275;
CC Name=7; Synonyms=Dp140c;
CC IsoId=P11532-13; Sequence=VSP_060275, VSP_046319;
CC Name=8; Synonyms=Dp140b;
CC IsoId=P11532-14; Sequence=VSP_060275, VSP_017493;
CC Name=9; Synonyms=Dp140ab;
CC IsoId=P11532-15; Sequence=VSP_060275, VSP_017492, VSP_017493;
CC Name=10; Synonyms=Dp140bc;
CC IsoId=P11532-16; Sequence=VSP_060275, VSP_046319, VSP_017493;
CC Name=11; Synonyms=Dp116;
CC IsoId=P11532-17; Sequence=VSP_060276, VSP_060277;
CC Name=12; Synonyms=Dp71;
CC IsoId=P11532-7; Sequence=VSP_017490, VSP_017491;
CC Name=13; Synonyms=Dp71a;
CC IsoId=P11532-8; Sequence=VSP_017490, VSP_017491, VSP_017492;
CC Name=14; Synonyms=Dp71b;
CC IsoId=P11532-6; Sequence=VSP_017490, VSP_017491, VSP_017493;
CC Name=15; Synonyms=Dp71ab;
CC IsoId=P11532-5; Sequence=VSP_017490, VSP_017491, VSP_017492,
CC VSP_017493;
CC Name=16; Synonyms=Dp60, Dp71delta110;
CC IsoId=P11532-9; Sequence=VSP_017490, VSP_017491, VSP_046319,
CC VSP_017493;
CC Name=17; Synonyms=Dp40;
CC IsoId=P11532-18; Sequence=VSP_017490, VSP_017491, VSP_060278;
CC -!- TISSUE SPECIFICITY: Expressed in muscle fibers accumulating in the
CC costameres of myoplasm at the sarcolemma. Expressed in brain, muscle,
CC kidney, lung and testis. Most tissues contain transcripts of multiple
CC isoforms. Isoform 15: Only isoform to be detected in heart and liver
CC and is also expressed in brain, testis and hepatoma cells.
CC {ECO:0000269|PubMed:1319059, ECO:0000269|PubMed:16000376,
CC ECO:0000269|PubMed:8541829}.
CC -!- DEVELOPMENTAL STAGE: Isoform 15: Expressed in embryonic neural tissue
CC from the sixth week of development. Isoform 16: Detected in all
CC embryonic tissues examined. {ECO:0000269|PubMed:9370062}.
CC -!- DISEASE: Duchenne muscular dystrophy (DMD) [MIM:310200]: Most common
CC form of muscular dystrophy; a sex-linked recessive disorder. It
CC typically presents in boys aged 3 to 7 year as proximal muscle weakness
CC causing waddling gait, toe-walking, lordosis, frequent falls, and
CC difficulty in standing up and climbing up stairs. The pelvic girdle is
CC affected first, then the shoulder girdle. Progression is steady and
CC most patients are confined to a wheelchair by age of 10 or 12. Flexion
CC contractures and scoliosis ultimately occur. About 50% of patients have
CC a lower IQ than their genetic expectations would suggest. There is no
CC treatment. {ECO:0000269|PubMed:12632325, ECO:0000269|PubMed:24302611,
CC ECO:0000269|PubMed:7981690, ECO:0000269|PubMed:8401582,
CC ECO:0000269|PubMed:8817332, ECO:0000269|PubMed:9851445}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Becker muscular dystrophy (BMD) [MIM:300376]: A neuromuscular
CC disorder characterized by dystrophin deficiency. It appears between the
CC age of 5 and 15 years with a proximal motor deficiency of variable
CC progression. Heart involvement can be the initial sign. Becker muscular
CC dystrophy has a more benign course than Duchenne muscular dystrophy.
CC {ECO:0000269|PubMed:10573008}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated, X-linked 3B (CMD3B) [MIM:302045]: A
CC disorder characterized by ventricular dilation and impaired systolic
CC function, resulting in congestive heart failure and arrhythmia.
CC Patients are at risk of premature death. {ECO:0000269|PubMed:12359139,
CC ECO:0000269|PubMed:25340340, ECO:0000269|PubMed:9170407}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The DMD gene is the largest known gene in humans. It is
CC 2.4 million base-pairs in size, comprises 79 exons and takes over 16
CC hours to be transcribed and cotranscriptionally spliced.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
CC 4. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing of isoform
CC 6. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing of isoform
CC 6. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing of isoform
CC 6. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 10]: Produced by alternative splicing of
CC isoform 6. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 11]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 12]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 13]: Produced by alternative splicing of
CC isoform 12. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 14]: Produced by alternative splicing of
CC isoform 12. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 15]: Produced by alternative splicing of
CC isoform 12. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 16]: Produced by alternative splicing of
CC isoform 12. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 17]: Produced by alternative splicing of
CC isoform 12. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=DMD; Note=Dystrophin Mutation Database;
CC URL="https://www.dmd.nl/database.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Dystrophin entry;
CC URL="https://en.wikipedia.org/wiki/Dystrophin";
CC ---------------------------------------------------------------------------
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DR EMBL; M18533; AAA53189.1; -; mRNA.
DR EMBL; X14298; CAA32479.1; -; mRNA.
DR EMBL; M92650; AAA52316.1; -; mRNA.
DR EMBL; AC078957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031542; CAI42229.1; -; Genomic_DNA.
DR EMBL; AC004468; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC006061; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC078958; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC079143; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC079175; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC079177; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC079864; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC090632; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC093167; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC093193; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AC096506; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AL031643; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AL096699; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AL109609; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AL139278; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AL451144; CAI42229.1; JOINED; Genomic_DNA.
DR EMBL; AL031643; CAI43058.1; -; Genomic_DNA.
DR EMBL; AC004468; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC006061; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC078958; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC079143; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC079175; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC079177; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC079864; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC090632; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC093167; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC093193; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AC096506; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AL031542; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AL096699; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AL109609; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AL139278; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AL451144; CAI43058.1; JOINED; Genomic_DNA.
DR EMBL; AL049643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096699; CAI42225.1; -; Genomic_DNA.
DR EMBL; AC004468; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC006061; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC078958; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC079143; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC079175; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC079177; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC079864; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC090632; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC093167; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC093193; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AC096506; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AL031542; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AL031643; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AL109609; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AL139278; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AL451144; CAI42225.1; JOINED; Genomic_DNA.
DR EMBL; AL109609; CAI42950.1; -; Genomic_DNA.
DR EMBL; AC004468; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC006061; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC078958; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC079143; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC079175; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC079177; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC079864; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC090632; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC093167; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC093193; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AC096506; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AL031542; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AL031643; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AL096699; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AL139278; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AL451144; CAI42950.1; JOINED; Genomic_DNA.
DR EMBL; AL121880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139278; CAI42991.1; -; Genomic_DNA.
DR EMBL; AC004468; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC006061; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC078958; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC079143; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC079175; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC079177; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC079864; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC090632; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC093167; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC093193; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AC096506; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AL031542; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AL031643; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AL096699; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AL109609; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AL451144; CAI42991.1; JOINED; Genomic_DNA.
DR EMBL; AL139401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451144; CAI39566.1; -; Genomic_DNA.
DR EMBL; AC004468; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC006061; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC078958; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC079143; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC079175; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC079177; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC079864; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC090632; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC093167; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC093193; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AC096506; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AL031542; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AL031643; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AL096699; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AL109609; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AL139278; CAI39566.1; JOINED; Genomic_DNA.
DR EMBL; AL596023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW99065.1; -; Genomic_DNA.
DR EMBL; BC028720; AAH28720.1; -; mRNA.
DR EMBL; BC070078; AAH70078.1; -; mRNA.
DR EMBL; BC094758; AAH94758.1; -; mRNA.
DR EMBL; BC127103; AAI27104.2; -; mRNA.
DR EMBL; U27203; AAA86115.1; -; Genomic_DNA.
DR EMBL; U27203; AAA86116.1; -; Genomic_DNA.
DR EMBL; X15148; CAA33245.1; -; mRNA.
DR EMBL; X06178; CAA29544.1; -; mRNA.
DR EMBL; X06179; CAA29545.1; -; mRNA.
DR EMBL; X13045; CAA31451.1; -; Genomic_DNA.
DR EMBL; X13046; CAA31452.1; -; Genomic_DNA.
DR EMBL; X13047; CAA31453.1; -; Genomic_DNA.
DR EMBL; X13048; CAA31454.1; -; Genomic_DNA.
DR EMBL; X15495; CAA33518.1; -; Genomic_DNA.
DR EMBL; X54820; CAA38589.1; -; Genomic_DNA.
DR CCDS; CCDS14231.1; -. [P11532-6]
DR CCDS; CCDS14232.1; -. [P11532-5]
DR CCDS; CCDS14233.1; -. [P11532-1]
DR CCDS; CCDS14234.1; -. [P11532-7]
DR CCDS; CCDS48091.1; -. [P11532-12]
DR CCDS; CCDS55394.1; -. [P11532-13]
DR CCDS; CCDS55395.1; -. [P11532-11]
DR CCDS; CCDS75965.1; -. [P11532-17]
DR PIR; A45255; A45255.
DR RefSeq; NP_000100.2; NM_000109.3.
DR RefSeq; NP_003997.1; NM_004006.2.
DR RefSeq; NP_004000.1; NM_004009.3.
DR RefSeq; NP_004001.1; NM_004010.3.
DR RefSeq; NP_004002.2; NM_004011.3.
DR RefSeq; NP_004003.1; NM_004012.3.
DR RefSeq; NP_004004.1; NM_004013.2. [P11532-12]
DR RefSeq; NP_004005.1; NM_004014.2. [P11532-17]
DR RefSeq; NP_004006.1; NM_004015.2. [P11532-7]
DR RefSeq; NP_004007.1; NM_004016.2. [P11532-6]
DR RefSeq; NP_004008.1; NM_004017.2. [P11532-8]
DR RefSeq; NP_004009.1; NM_004018.2. [P11532-5]
DR RefSeq; NP_004010.1; NM_004019.2. [P11532-18]
DR RefSeq; NP_004011.2; NM_004020.3. [P11532-13]
DR RefSeq; NP_004012.1; NM_004021.2.
DR RefSeq; NP_004013.1; NM_004022.2. [P11532-15]
DR RefSeq; NP_004014.1; NM_004023.2.
DR PDB; 1DXX; X-ray; 2.60 A; A/B/C/D=1-246.
DR PDB; 1EG3; X-ray; 2.00 A; A=3046-3306.
DR PDB; 1EG4; X-ray; 2.00 A; A=3046-3306.
DR PDB; 3UUN; X-ray; 2.30 A; A/B=338-456.
DR PDBsum; 1DXX; -.
DR PDBsum; 1EG3; -.
DR PDBsum; 1EG4; -.
DR PDBsum; 3UUN; -.
DR SASBDB; P11532; -.
DR SMR; P11532; -.
DR BioGRID; 108096; 92.
DR DIP; DIP-32593N; -.
DR IntAct; P11532; 63.
DR MINT; P11532; -.
DR STRING; 9606.ENSP00000354923; -.
DR DrugBank; DB15593; Golodirsen.
DR DrugCentral; P11532; -.
DR TCDB; 8.A.66.1.2; the dystrophin (dystrophin) family.
DR CarbonylDB; P11532; -.
DR GlyGen; P11532; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11532; -.
DR PhosphoSitePlus; P11532; -.
DR SwissPalm; P11532; -.
DR BioMuta; DMD; -.
DR DMDM; 313104240; -.
DR EPD; P11532; -.
DR jPOST; P11532; -.
DR MassIVE; P11532; -.
DR MaxQB; P11532; -.
DR PaxDb; P11532; -.
DR PeptideAtlas; P11532; -.
DR PRIDE; P11532; -.
DR ProteomicsDB; 17631; -.
DR ProteomicsDB; 17635; -.
DR ProteomicsDB; 17951; -.
DR ProteomicsDB; 19709; -.
DR ProteomicsDB; 19712; -.
DR ProteomicsDB; 25166; -.
DR ProteomicsDB; 29059; -.
DR ProteomicsDB; 52788; -. [P11532-1]
DR ProteomicsDB; 52789; -. [P11532-2]
DR ProteomicsDB; 52790; -. [P11532-3]
DR ProteomicsDB; 52791; -. [P11532-4]
DR ProteomicsDB; 52792; -. [P11532-5]
DR ProteomicsDB; 52793; -. [P11532-6]
DR Antibodypedia; 476; 643 antibodies from 38 providers.
DR DNASU; 1756; -.
DR Ensembl; ENST00000361471.8; ENSP00000354464.4; ENSG00000198947.18. [P11532-5]
DR Ensembl; ENST00000378680.6; ENSP00000367951.2; ENSG00000198947.18. [P11532-9]
DR Ensembl; ENST00000378702.8; ENSP00000367974.4; ENSG00000198947.18. [P11532-7]
DR Ensembl; ENST00000378723.7; ENSP00000367997.3; ENSG00000198947.18. [P11532-6]
DR Ensembl; ENST00000682600.1; ENSP00000507640.1; ENSG00000198947.18. [P11532-8]
DR GeneID; 1756; -.
DR KEGG; hsa:1756; -.
DR UCSC; uc004dcm.2; human. [P11532-1]
DR UCSC; uc004dcq.1; human.
DR UCSC; uc004dcr.1; human.
DR UCSC; uc004dct.1; human.
DR UCSC; uc004dcu.2; human.
DR UCSC; uc004dcv.1; human.
DR UCSC; uc004dcy.2; human.
DR CTD; 1756; -.
DR DisGeNET; 1756; -.
DR GeneCards; DMD; -.
DR GeneReviews; DMD; -.
DR HGNC; HGNC:2928; DMD.
DR HPA; ENSG00000198947; Low tissue specificity.
DR MalaCards; DMD; -.
DR MIM; 300376; phenotype.
DR MIM; 300377; gene.
DR MIM; 302045; phenotype.
DR MIM; 310200; phenotype.
DR neXtProt; NX_P11532; -.
DR OpenTargets; ENSG00000198947; -.
DR Orphanet; 98895; Becker muscular dystrophy.
DR Orphanet; 98896; Duchenne muscular dystrophy.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 206546; Symptomatic form of muscular dystrophy of Duchenne and Becker in female carriers.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA27378; -.
DR VEuPathDB; HostDB:ENSG00000198947; -.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000154342; -.
DR HOGENOM; CLU_001187_1_2_1; -.
DR InParanoid; P11532; -.
DR OrthoDB; 72477at2759; -.
DR PhylomeDB; P11532; -.
DR TreeFam; TF320178; -.
DR PathwayCommons; P11532; -.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P11532; -.
DR SIGNOR; P11532; -.
DR BioGRID-ORCS; 1756; 10 hits in 711 CRISPR screens.
DR ChiTaRS; DMD; human.
DR EvolutionaryTrace; P11532; -.
DR GeneWiki; Dystrophin; -.
DR GenomeRNAi; 1756; -.
DR Pharos; P11532; Tclin.
DR PRO; PR:P11532; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P11532; protein.
DR Bgee; ENSG00000198947; Expressed in trigeminal ganglion and 201 other tissues.
DR ExpressionAtlas; P11532; baseline and differential.
DR Genevisible; P11532; HS.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030055; C:cell-substrate junction; ISS:BHF-UCL.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
DR GO; GO:0031527; C:filopodium membrane; IDA:BHF-UCL.
DR GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
DR GO; GO:0044306; C:neuron projection terminus; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR GO; GO:0016013; C:syntrophin complex; TAS:BHF-UCL.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
DR GO; GO:0017022; F:myosin binding; IDA:BHF-UCL.
DR GO; GO:0050998; F:nitric-oxide synthase binding; ISS:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0008307; F:structural constituent of muscle; IDA:UniProtKB.
DR GO; GO:0017166; F:vinculin binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0086001; P:cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0044458; P:motile cilium assembly; TAS:BHF-UCL.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:BHF-UCL.
DR GO; GO:0055001; P:muscle cell development; ISS:BHF-UCL.
DR GO; GO:0007517; P:muscle organ development; NAS:ProtInc.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:BHF-UCL.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0043043; P:peptide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IMP:BHF-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
DR GO; GO:0090287; P:regulation of cellular response to growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0090257; P:regulation of muscle system process; IBA:GO_Central.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS:BHF-UCL.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL.
DR GO; GO:0014819; P:regulation of skeletal muscle contraction; ISS:BHF-UCL.
DR GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; ISS:BHF-UCL.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISS:BHF-UCL.
DR GO; GO:0035994; P:response to muscle stretch; ISS:BHF-UCL.
DR GO; GO:0007519; P:skeletal muscle tissue development; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 11.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
DR IDEAL; IID00267; -.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035436; Dystrophin/utrophin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 17.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 22.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative promoter usage;
KW Alternative splicing; Calcium; Cardiomyopathy; Cell membrane; Cytoplasm;
KW Cytoskeleton; Disease variant; Membrane; Metal-binding; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Zinc;
KW Zinc-finger.
FT CHAIN 1..3685
FT /note="Dystrophin"
FT /id="PRO_0000076075"
FT DOMAIN 15..119
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 134..240
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 339..447
FT /note="Spectrin 1"
FT REPEAT 448..556
FT /note="Spectrin 2"
FT REPEAT 559..667
FT /note="Spectrin 3"
FT REPEAT 719..828
FT /note="Spectrin 4"
FT REPEAT 830..934
FT /note="Spectrin 5"
FT REPEAT 943..1045
FT /note="Spectrin 6"
FT REPEAT 1048..1154
FT /note="Spectrin 7"
FT REPEAT 1157..1263
FT /note="Spectrin 8"
FT REPEAT 1266..1367
FT /note="Spectrin 9"
FT REPEAT 1368..1463
FT /note="Spectrin 10"
FT REPEAT 1468..1568
FT /note="Spectrin 11"
FT REPEAT 1571..1676
FT /note="Spectrin 12"
FT REPEAT 1679..1778
FT /note="Spectrin 13"
FT REPEAT 1779..1874
FT /note="Spectrin 14"
FT REPEAT 1877..1979
FT /note="Spectrin 15"
FT REPEAT 1992..2101
FT /note="Spectrin 16"
FT REPEAT 2104..2208
FT /note="Spectrin 17"
FT REPEAT 2211..2318
FT /note="Spectrin 18"
FT REPEAT 2319..2423
FT /note="Spectrin 19"
FT REPEAT 2475..2577
FT /note="Spectrin 20"
FT REPEAT 2580..2686
FT /note="Spectrin 21"
FT REPEAT 2689..2802
FT /note="Spectrin 22"
FT REPEAT 2808..2930
FT /note="Spectrin 23"
FT REPEAT 2935..3040
FT /note="Spectrin 24"
FT DOMAIN 3055..3088
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 3308..3364
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..240
FT /note="Actin-binding"
FT REGION 63..72
FT /note="ANK2- and ANK-3 binding"
FT /evidence="ECO:0000250"
FT REGION 1415..1913
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250"
FT REGION 3058..3408
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000250"
FT REGION 3466..3518
FT /note="Binds to SNTB1"
FT REGION 3528..3554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3603..3685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3603..3673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 3483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 3490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 3500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 3612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 3617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 3623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 3624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 3666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..3068
FT /note="Missing (in isoform 12, isoform 13, isoform 14,
FT isoform 15, isoform 16 and isoform 17)"
FT /evidence="ECO:0000303|PubMed:1319059,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829"
FT /id="VSP_017490"
FT VAR_SEQ 1..2729
FT /note="Missing (in isoform 11)"
FT /id="VSP_060276"
FT VAR_SEQ 1..2460
FT /note="Missing (in isoform 6, isoform 7, isoform 8, isoform
FT 9 and isoform 10)"
FT /id="VSP_060275"
FT VAR_SEQ 1..11
FT /note="MLWWEEVEDCY -> MED (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2648158"
FT /id="VSP_006809"
FT VAR_SEQ 1..11
FT /note="MLWWEEVEDCY -> MSEVSSD (in isoform 3)"
FT /id="VSP_060274"
FT VAR_SEQ 1
FT /note="M -> MTEIILLIFFPAYFLN (in isoform 4)"
FT /id="VSP_006806"
FT VAR_SEQ 1
FT /note="M -> MSARKLRNLSYKK (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_006808"
FT VAR_SEQ 2..1357
FT /note="Missing (in isoform 4 and isoform 5)"
FT /id="VSP_006807"
FT VAR_SEQ 2730..2739
FT /note="GVKELMKQWQ -> MLHRKTYHVK (in isoform 11)"
FT /id="VSP_060277"
FT VAR_SEQ 3069..3075
FT /note="KVPYYIN -> MREQLKG (in isoform 12, isoform 13,
FT isoform 14, isoform 15, isoform 16 and isoform 17)"
FT /evidence="ECO:0000303|PubMed:1319059,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829"
FT /id="VSP_017491"
FT VAR_SEQ 3409..3685
FT /note="Missing (in isoform 17)"
FT /id="VSP_060278"
FT VAR_SEQ 3409..3518
FT /note="Missing (in isoform 7, isoform 10 and isoform 16)"
FT /id="VSP_046319"
FT VAR_SEQ 3409..3421
FT /note="Missing (in isoform 9, isoform 13 and isoform 15)"
FT /evidence="ECO:0000303|PubMed:1319059,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829"
FT /id="VSP_017492"
FT VAR_SEQ 3673..3685
FT /note="RNTPGKPMREDTM -> HNVGSLFHMADDLGRAMESLVSVMTDEEGAE (in
FT isoform 8, isoform 9, isoform 10, isoform 14, isoform 15
FT and isoform 16)"
FT /evidence="ECO:0000303|PubMed:1319059,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8541829"
FT /id="VSP_017493"
FT VARIANT 18
FT /note="K -> N (in CMD3B; decreased thermodynamic stability;
FT accelerated unfolding, perturbed protein structure; no
FT effect on anchoring function)"
FT /evidence="ECO:0000269|PubMed:12359139,
FT ECO:0000269|PubMed:25340340"
FT /id="VAR_023537"
FT VARIANT 32..62
FT /note="Missing (in BMD)"
FT /id="VAR_005146"
FT VARIANT 54
FT /note="L -> R (in DMD)"
FT /evidence="ECO:0000269|PubMed:8401582"
FT /id="VAR_005147"
FT VARIANT 118
FT /note="W -> R (in a patient with Becker muscular
FT dystrophy)"
FT /evidence="ECO:0000269|PubMed:21396098"
FT /id="VAR_065764"
FT VARIANT 133
FT /note="Q -> P (in dbSNP:rs1800256)"
FT /evidence="ECO:0000269|PubMed:2668885"
FT /id="VAR_005148"
FT VARIANT 165
FT /note="D -> V (in one patient with Becker muscular
FT dystrophy)"
FT /evidence="ECO:0000269|PubMed:12632325"
FT /id="VAR_023538"
FT VARIANT 168
FT /note="A -> D (in BMD)"
FT /id="VAR_005149"
FT VARIANT 171
FT /note="A -> P (in BMD)"
FT /evidence="ECO:0000269|PubMed:10573008"
FT /id="VAR_023539"
FT VARIANT 231
FT /note="Y -> N (in BMD)"
FT /id="VAR_005150"
FT VARIANT 279
FT /note="T -> A (in CMD3B)"
FT /evidence="ECO:0000269|PubMed:9170407"
FT /id="VAR_023540"
FT VARIANT 334
FT /note="L -> F (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036353"
FT VARIANT 365
FT /note="Q -> H (in dbSNP:rs1800266)"
FT /evidence="ECO:0000269|PubMed:7849724"
FT /id="VAR_005151"
FT VARIANT 409
FT /note="T -> S (in dbSNP:rs34155804)"
FT /id="VAR_057642"
FT VARIANT 495..534
FT /note="Missing (in BMD)"
FT /id="VAR_005152"
FT VARIANT 573
FT /note="A -> V (in dbSNP:rs5972599)"
FT /id="VAR_057643"
FT VARIANT 623
FT /note="L -> I (in dbSNP:rs1800259)"
FT /evidence="ECO:0000269|PubMed:2668885"
FT /id="VAR_005153"
FT VARIANT 645
FT /note="D -> G (in DMD)"
FT /evidence="ECO:0000269|PubMed:7981690"
FT /id="VAR_023541"
FT VARIANT 666
FT /note="S -> L (in dbSNP:rs34563188)"
FT /id="VAR_062110"
FT VARIANT 715
FT /note="T -> S (in dbSNP:rs16998350)"
FT /id="VAR_057644"
FT VARIANT 773
FT /note="K -> E (in DMD)"
FT /id="VAR_005154"
FT VARIANT 784
FT /note="A -> G (in dbSNP:rs1800260)"
FT /evidence="ECO:0000269|PubMed:2668885"
FT /id="VAR_005155"
FT VARIANT 882
FT /note="D -> G (in dbSNP:rs228406)"
FT /evidence="ECO:0000269|PubMed:2668885,
FT ECO:0000269|PubMed:3282674, ECO:0000269|PubMed:3428261"
FT /id="VAR_005156"
FT VARIANT 1136
FT /note="T -> S (in dbSNP:rs3827462)"
FT /id="VAR_057645"
FT VARIANT 1197
FT /note="V -> F (in dbSNP:rs1800262)"
FT /evidence="ECO:0000269|PubMed:2668885"
FT /id="VAR_005157"
FT VARIANT 1219
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036354"
FT VARIANT 1245
FT /note="T -> I (in dbSNP:rs1800269)"
FT /id="VAR_005158"
FT VARIANT 1278
FT /note="A -> P (in dbSNP:rs1800270)"
FT /id="VAR_005159"
FT VARIANT 1377
FT /note="K -> N (in dbSNP:rs1800263)"
FT /evidence="ECO:0000269|PubMed:2668885"
FT /id="VAR_005160"
FT VARIANT 1388
FT /note="F -> V (in dbSNP:rs28715870)"
FT /id="VAR_057646"
FT VARIANT 1469
FT /note="Q -> L (in dbSNP:rs1057872)"
FT /evidence="ECO:0000269|PubMed:3282674"
FT /id="VAR_005161"
FT VARIANT 1470
FT /note="R -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036355"
FT VARIANT 1672
FT /note="N -> K (in dbSNP:rs16990264)"
FT /evidence="ECO:0000269|PubMed:12354438"
FT /id="VAR_023542"
FT VARIANT 1745
FT /note="R -> H (in dbSNP:rs1801187)"
FT /evidence="ECO:0000269|PubMed:2668885"
FT /id="VAR_005162"
FT VARIANT 1844
FT /note="R -> S (in dbSNP:rs1801186)"
FT /evidence="ECO:0000269|PubMed:2668885"
FT /id="VAR_005163"
FT VARIANT 2108
FT /note="R -> C (in dbSNP:rs16990169)"
FT /id="VAR_057647"
FT VARIANT 2155
FT /note="R -> W (in dbSNP:rs1800273)"
FT /evidence="ECO:0000269|PubMed:12359139"
FT /id="VAR_005164"
FT VARIANT 2164
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036356"
FT VARIANT 2191
FT /note="R -> W"
FT /evidence="ECO:0000269|PubMed:7849724"
FT /id="VAR_005165"
FT VARIANT 2299
FT /note="N -> T"
FT /evidence="ECO:0000269|PubMed:12359139"
FT /id="VAR_023543"
FT VARIANT 2305..2366
FT /note="Missing (in DMD)"
FT /id="VAR_005166"
FT VARIANT 2366
FT /note="K -> Q (in dbSNP:rs1800275)"
FT /evidence="ECO:0000269|PubMed:12359139,
FT ECO:0000269|PubMed:3282674"
FT /id="VAR_005167"
FT VARIANT 2910
FT /note="E -> V (in dbSNP:rs41305353)"
FT /evidence="ECO:0000269|PubMed:12359139"
FT /id="VAR_005168"
FT VARIANT 2912
FT /note="N -> D (in dbSNP:rs1800278)"
FT /evidence="ECO:0000269|PubMed:12359139"
FT /id="VAR_005169"
FT VARIANT 2921
FT /note="H -> R (in BMD; dbSNP:rs1800279)"
FT /id="VAR_005170"
FT VARIANT 2937
FT /note="Q -> R (in dbSNP:rs1800280)"
FT /evidence="ECO:0000269|PubMed:12359139,
FT ECO:0000269|PubMed:15772651, ECO:0000269|PubMed:7849724"
FT /id="VAR_005171"
FT VARIANT 3228
FT /note="F -> L (in CMD3B)"
FT /evidence="ECO:0000269|PubMed:12359139"
FT /id="VAR_023544"
FT VARIANT 3313
FT /note="C -> F (in DMD; results in highly reduced protein
FT levels and expression at the sarcolemma)"
FT /evidence="ECO:0000269|PubMed:12632325,
FT ECO:0000269|PubMed:24302611"
FT /id="VAR_023545"
FT VARIANT 3335
FT /note="D -> H (in DMD; does not affect protein stability;
FT does not affect protein expression at the sarcolemma;
FT interaction with DAG1 is reduced)"
FT /evidence="ECO:0000269|PubMed:24302611,
FT ECO:0000269|PubMed:9851445"
FT /id="VAR_023546"
FT VARIANT 3340
FT /note="C -> Y (in DMD; results in highly reduced protein
FT levels and expression at the sarcolemma)"
FT /evidence="ECO:0000269|PubMed:24302611,
FT ECO:0000269|PubMed:8817332"
FT /id="VAR_023547"
FT VARIANT 3421
FT /note="A -> V (in BMD)"
FT /id="VAR_005172"
FT CONFLICT 664
FT /note="Q -> QM (in Ref. 10; CAA29544)"
FT /evidence="ECO:0000305"
FT CONFLICT 2361
FT /note="G -> E (in Ref. 13; CAA38589)"
FT /evidence="ECO:0000305"
FT CONFLICT 3542
FT /note="P -> T (in Ref. 6; AAH70078)"
FT /evidence="ECO:0000305"
FT CONFLICT 3546
FT /note="M -> V (in Ref. 6; AAH70078)"
FT /evidence="ECO:0000305"
FT HELIX 14..31
FT /evidence="ECO:0007829|PDB:1DXX"
FT TURN 40..46
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:1DXX"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:1DXX"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:1DXX"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:1DXX"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1DXX"
FT HELIX 339..365
FT /evidence="ECO:0007829|PDB:3UUN"
FT HELIX 372..409
FT /evidence="ECO:0007829|PDB:3UUN"
FT HELIX 414..452
FT /evidence="ECO:0007829|PDB:3UUN"
FT HELIX 3050..3054
FT /evidence="ECO:0007829|PDB:1EG3"
FT STRAND 3061..3065
FT /evidence="ECO:0007829|PDB:1EG3"
FT STRAND 3071..3075
FT /evidence="ECO:0007829|PDB:1EG3"
FT TURN 3076..3079
FT /evidence="ECO:0007829|PDB:1EG3"
FT STRAND 3080..3084
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3086..3094
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3095..3098
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3104..3118
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3121..3123
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3126..3135
FT /evidence="ECO:0007829|PDB:1EG3"
FT STRAND 3143..3146
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3147..3164
FT /evidence="ECO:0007829|PDB:1EG3"
FT STRAND 3165..3168
FT /evidence="ECO:0007829|PDB:1EG4"
FT HELIX 3171..3186
FT /evidence="ECO:0007829|PDB:1EG3"
FT STRAND 3192..3195
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3196..3205
FT /evidence="ECO:0007829|PDB:1EG3"
FT STRAND 3207..3209
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3211..3222
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3231..3247
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3251..3254
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3260..3269
FT /evidence="ECO:0007829|PDB:1EG3"
FT TURN 3270..3272
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3278..3286
FT /evidence="ECO:0007829|PDB:1EG3"
FT TURN 3290..3293
FT /evidence="ECO:0007829|PDB:1EG3"
FT HELIX 3294..3304
FT /evidence="ECO:0007829|PDB:1EG3"
FT MOD_RES P11532-5:340
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P11532-5:344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P11532-5:348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P11532-5:616
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES P11532-6:629
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES P11532-8:340
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P11532-8:344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P11532-8:348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES P11532-9:519
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 3685 AA; 426750 MW; 24FF7E83F1E6BF8D CRC64;
MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ
KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV
KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL
FDWNSVVCQQ SATQRLEHAF NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP
QQVSIEAIQE VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA
YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE VLSWLLSAED
TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL QLGSKLIGTG KLSEDEETEV
QEQMNLLNSR WECLRVASME KQSNLHRVLM DLQNQKLKEL NDWLTKTEER TRKMEEEPLG
PDLEDLKRQV QQHKVLQEDL EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW
ANICRWTEDR WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL
QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC WDNLVQKLEK
STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ EELPPPPPQK KRQITVDSEI
RKRLDVDITE LHSWITRSEA VLQSPEFAIF RKEGNFSDLK EKVNAIEREK AEKFRKLQDA
SRSAQALVEQ MVNEGVNADS IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ
QLEQMTTTAE NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SDLQPQIERL KIQSIALKEK
GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA IRTWVQQSET
KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS TTVKEMSKKA PSEISRKYQS
EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL RKIQNHIQTL KKWMAEVDVF LKEEWPALGD
SEILKKQLKQ CRLLVSDIQT IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH
MCQQVYARKE ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM
KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL CTRLNGKCKT
LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE EISEVLDSLE NLMRHSEDNP
NQIRILAQTL TDGGVMDELI NEELETFNSR WRELHEEAVR RQKLLEQSIQ SAQETEKSLH
LIQESLTFID KQLAAYIADK VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV
LSQIDVAQKK LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS
QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL HYNELGAKVT
ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV EGMPSNLDSE VAWGKATQKE
IEKQKVHLKS ITEVGEALKT VLGKKETLVE DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH
METFDQNVDH ITKWIIQADT LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN
LMANRGDHCR KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE
IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK QQLLQTKHNA
LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL ASLPEPRDER KIKEIDRELQ
KKKEELNAVR RQAEGLSEDG AAMAVEPTQI QLSKRWREIE SKFAQFRRLN FAQIHTVREE
TMMVMTEDMP LEISYVPSTY LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN
IKDSLQQSSG RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD
RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD GIGQRQTVVR
TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS DRKKRLEEQK NILSEFQRDL
NEFVLWLEEA DNIASIPLEP GKEQQLKEKL EQVKLLVEEL PLRQGILKQL NETGGPVLVS
APISPEEQDK LENKLKQTNL QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL
LLWLSPIRNQ LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK
RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV TKETAISKLE
MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV GDLEDINEMI IKQKATMQDL
EQRRPQLEEL ITAAQNLKNK TSNQEARTII TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK
DSTQWLEAKE EAEQVLGQAR AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA
NDLALKLLRD YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK
FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD VYHNLDENSQ
KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL EASSDQWKRL HLSLQELLVW
LQLKDDELSR QAPIGGDFPA VQKQNDVHRA FKRELKTKEP VIMSTLETVR IFLTEQPLEG
LEKLYQEPRE LPPEERAQNV TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ
EATDELDLKL RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR
QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ HFLSTSVQGP
WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC
LDLLSLSAAC DALDQHNLKQ NDQPMDILQI INCLTTIYDR LEQEHNNLVN VPLCVDMCLN
WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD
SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR
VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC
TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV TLINFWPVDS
APASSPQLSH DDTHSRIEHY ASRLAEMENS NGSYLNDSIS PNESIDDEHL LIQHYCQSLN
QDSPLSQPRS PAQILISLES EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP
SPPEMMPTSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP
QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ DTSTGLEEVM
EQLNNSFPSS RGRNTPGKPM REDTM
