DMD_MOUSE
ID DMD_MOUSE Reviewed; 3678 AA.
AC P11531; A2A9Z0; O35653; Q60703;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Dystrophin;
GN Name=Dmd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RX PubMed=1579466; DOI=10.1093/nar/20.7.1725;
RA Bies R.D., Phelps S.F., Cortez M.D., Roberts R., Caskey C.T.,
RA Chamberlain J.S.;
RT "Human and murine dystrophin mRNA transcripts are differentially expressed
RT during skeletal muscle, heart, and brain development.";
RL Nucleic Acids Res. 20:1725-1731(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-201.
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-176.
RC STRAIN=129/J;
RX PubMed=1543903; DOI=10.1007/bf00570441;
RA Maconochie M.K., Brown S.D.M., Greenfield A.J.;
RT "Sequence analysis of two exons from the murine dystrophin locus.";
RL Mamm. Genome 2:64-68(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 300-1390.
RX PubMed=3659917; DOI=10.1126/science.3659917;
RA Hoffman E.P., Monaco A.P., Feener C.C., Kunkel L.M.;
RT "Conservation of the Duchenne muscular dystrophy gene in mice and humans.";
RL Science 238:347-350(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 986-1056.
RC STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RX PubMed=8111539; DOI=10.1007/978-94-011-1528-5_7;
RA Chamberlain J.S., Phelps S.F., Cox G.A., Maichele A.J., Greenwood A.D.;
RT "PCR analysis of muscular dystrophy in mdx mice.";
RL Mol. Cell Biol. Hum. Dis. Ser. 3:167-189(1993).
RN [7]
RP PROTEIN SEQUENCE OF 1129-1134, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3069-3181.
RX PubMed=1377655; DOI=10.1111/j.1432-0436.1992.tb00666.x;
RA Rapaport D., Lederfein D., den Dunnen J.T., Grootscholten P.M.,
RA van Ommen G.J.B., Fuchs O., Nudel U., Yaffe D.;
RT "Characterization and cell type distribution of a novel, major transcript
RT of the Duchenne muscular dystrophy gene.";
RL Differentiation 49:187-193(1992).
RN [9]
RP INTERACTION WITH SNTA1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
RX PubMed=7547961; DOI=10.1021/bi00038a014;
RA Madhavan R., Jarrett H.W.;
RT "Interactions between dystrophin glycoprotein complex proteins.";
RL Biochemistry 34:12204-12209(1995).
RN [10]
RP ALTERNATIVE SPLICING, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/10; TISSUE=Retina;
RX PubMed=7633443; DOI=10.1093/hmg/4.5.837;
RA D'Souza V.N., Nguyen T.M., Morris G.E., Karges W., Pillers D.-A.M.,
RA Ray P.N.;
RT "A novel dystrophin isoform is required for normal retinal
RT electrophysiology.";
RL Hum. Mol. Genet. 4:837-842(1995).
RN [11]
RP INTERACTION WITH PGM5.
RX PubMed=7890770; DOI=10.1074/jbc.270.11.6328;
RA Belkin A.M., Burridge K.;
RT "Association of aciculin with dystrophin and utrophin.";
RL J. Biol. Chem. 270:6328-6337(1995).
RN [12]
RP INTERACTION WITH SNTB1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
RX PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA Peters M.F., Adams M.E., Froehner S.C.;
RT "Differential association of syntrophin pairs with the dystrophin
RT complex.";
RL J. Cell Biol. 138:81-93(1997).
RN [13]
RP INTERACTION WITH DTNB.
RX PubMed=10893187; DOI=10.1242/jcs.113.15.2715;
RA Loh N.Y., Newey S.E., Davies K.E., Blake D.J.;
RT "Assembly of multiple dystrobrevin-containing complexes in the kidney.";
RL J. Cell Sci. 113:2715-2724(2000).
RN [14]
RP INTERACTION WITH DAG1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN COMPLEX.
RX PubMed=11520903; DOI=10.1046/j.1471-4159.2001.00466.x;
RA Moukhles H., Carbonetto S.;
RT "Dystroglycan contributes to the formation of multiple dystrophin-like
RT complexes in brain.";
RL J. Neurochem. 78:824-834(2001).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH DRP2; PRX; DAG1 AND UTRN, AND TISSUE
RP SPECIFICITY.
RX PubMed=11430802; DOI=10.1016/s0896-6273(01)00327-0;
RA Sherman D.L., Fabrizi C., Gillespie C.S., Brophy P.J.;
RT "Specific disruption of a Schwann cell dystrophin-related protein complex
RT in a demyelinating neuropathy.";
RL Neuron 30:677-687(2001).
RN [16]
RP INTERACTION WITH SYNM.
RX PubMed=16777071; DOI=10.1016/j.bbrc.2006.05.192;
RA Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.;
RT "Interactions of intermediate filament protein synemin with dystrophin and
RT utrophin.";
RL Biochem. Biophys. Res. Commun. 346:768-777(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3616 AND SER-3617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [18]
RP INTERACTION WITH ANK2 AND ANK3, AND SUBCELLULAR LOCATION.
RX PubMed=19109891; DOI=10.1016/j.cell.2008.10.018;
RA Ayalon G., Davis J.Q., Scotland P.B., Bennett V.;
RT "An ankyrin-based mechanism for functional organization of dystrophin and
RT dystroglycan.";
RL Cell 135:1189-1200(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3610; SER-3616 AND SER-3617,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [20]
RP INTERACTION WITH CMYA5.
RX PubMed=20634290; DOI=10.1074/jbc.m110.108720;
RA Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A.,
RA Hackman P., Ehler E., Richard I., Udd B.;
RT "Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to
RT tibial and limb-girdle muscular dystrophies.";
RL J. Biol. Chem. 285:30304-30315(2010).
RN [21]
RP DISRUPTION PHENOTYPE.
RX PubMed=28498977; DOI=10.1093/hmg/ddx189;
RA Saha M., Mitsuhashi S., Jones M.D., Manko K., Reddy H.M., Bruels C.,
RA Cho K.A., Pacak C.A., Draper I., Kang P.B.;
RT "Consequences of MEGF10 deficiency on myoblast function and Notch1
RT interactions.";
RL Hum. Mol. Genet. 26:2984-3000(2017).
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:0000269|PubMed:7633443}.
CC -!- SUBUNIT: Interacts with SYNM (PubMed:16777071). Interacts with the
CC syntrophins SNTG1 and SNTG2. Interacts with KRT19. Component of the
CC dystrophin-associated glycoprotein complex which is composed of three
CC subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA
CC and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the
CC transmembrane dystroglycan complex, and the sarcoglycan-sarcospan
CC complex. Interacts with DAG1 (betaDAG1) with DMD; the interaction is
CC inhibited by phosphorylation on the PPXY motif of DAG1 (By similarity).
CC Interacts with SYNM; SNTA1 and SNTB1. Interacts with CMYA5
CC (PubMed:20634290). 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 (PubMed:19109891). Identified
CC in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD
CC and DAG1 (PubMed:11430802). Interacts with DTNB (PubMed:10893187).
CC Interacts with PGM5; the interaction is direct (PubMed:7890770).
CC {ECO:0000250|UniProtKB:P11532, ECO:0000269|PubMed:10893187,
CC ECO:0000269|PubMed:11430802, ECO:0000269|PubMed:11520903,
CC ECO:0000269|PubMed:16777071, ECO:0000269|PubMed:19109891,
CC ECO:0000269|PubMed:20634290, ECO:0000269|PubMed:7547961,
CC ECO:0000269|PubMed:7890770, ECO:0000269|PubMed:9214383}.
CC -!- INTERACTION:
CC P11531; Q9CZA6-1: Nde1; NbExp=2; IntAct=EBI-295928, EBI-15949673;
CC P11531; Q61234: Snta1; NbExp=4; IntAct=EBI-295928, EBI-295952;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:19109891}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19109891}; Cytoplasmic side
CC {ECO:0000269|PubMed:19109891}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19109891}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:19109891}. 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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=At least 11 isoforms are produced.;
CC Name=1;
CC IsoId=P11531-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Detected in quadriceps muscle and in sciatic nerve
CC (at protein level) (PubMed:11430802). Differentially expressed during
CC skeletal muscle, heart, and brain development. Also expressed in retina
CC (PubMed:7633443). {ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:7633443}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show reduced contractile force
CC compared to wild-types, at least for soleus muscle. They have decreased
CC motor activity levels after exercise, increased muscle permeability and
CC fibrosis with impaired regeneration (PubMed:28498977). MEGF10 and DMD
CC double knockout animals have pronounced fiber size variability and
CC intracellular inclusions in the quadriceps femoris with extensive
CC endomysial connective tissue infiltration. Mice develop muscle
CC weakness, kyphosis and a waddling gait. At 2 months of age, they have
CC reduced contractile force compared to wild-type mice. They display
CC reduced motor activity after exercise and they walk shorter distances
CC than wild-type. They have a delayed regeneration after muscle injury
CC and an aberrant muscle fiber typing and cross-sectional areas
CC (PubMed:28498977). {ECO:0000269|PubMed:28498977}.
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DR EMBL; M68859; AAB02797.1; -; mRNA.
DR EMBL; AL645477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL806516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL808024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL833800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX000479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX294443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR352330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR382328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X58153; CAA41157.1; -; Genomic_DNA.
DR EMBL; M18025; AAA37530.1; -; mRNA.
DR EMBL; U56724; AAB01216.1; -; Genomic_DNA.
DR EMBL; U15218; AAA87068.1; -; mRNA.
DR CCDS; CCDS41047.1; -. [P11531-1]
DR PIR; S28916; S28916.
DR RefSeq; NP_031894.1; NM_007868.6. [P11531-1]
DR SMR; P11531; -.
DR BioGRID; 199245; 47.
DR CORUM; P11531; -.
DR DIP; DIP-32899N; -.
DR IntAct; P11531; 48.
DR MINT; P11531; -.
DR STRING; 10090.ENSMUSP00000109633; -.
DR iPTMnet; P11531; -.
DR PhosphoSitePlus; P11531; -.
DR EPD; P11531; -.
DR jPOST; P11531; -.
DR MaxQB; P11531; -.
DR PaxDb; P11531; -.
DR PeptideAtlas; P11531; -.
DR PRIDE; P11531; -.
DR ProteomicsDB; 277346; -. [P11531-1]
DR Antibodypedia; 476; 643 antibodies from 38 providers.
DR DNASU; 13405; -.
DR Ensembl; ENSMUST00000114000; ENSMUSP00000109633; ENSMUSG00000045103. [P11531-1]
DR GeneID; 13405; -.
DR KEGG; mmu:13405; -.
DR UCSC; uc009tri.2; mouse. [P11531-1]
DR CTD; 1756; -.
DR MGI; MGI:94909; Dmd.
DR VEuPathDB; HostDB:ENSMUSG00000045103; -.
DR eggNOG; KOG4286; Eukaryota.
DR GeneTree; ENSGT00940000154342; -.
DR HOGENOM; CLU_000246_1_0_1; -.
DR InParanoid; P11531; -.
DR OMA; LQHPEDN; -.
DR OrthoDB; 72477at2759; -.
DR PhylomeDB; P11531; -.
DR TreeFam; TF320178; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 13405; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Dmd; mouse.
DR PRO; PR:P11531; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P11531; protein.
DR Bgee; ENSMUSG00000045103; Expressed in ascending aorta and 275 other tissues.
DR ExpressionAtlas; P11531; baseline and differential.
DR Genevisible; P11531; MM.
DR GO; GO:0097449; C:astrocyte projection; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030055; C:cell-substrate junction; IDA:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; ISO:MGI.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0099617; C:matrix side of mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0030016; C:myofibril; ISO:MGI.
DR GO; GO:0005883; C:neurofilament; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0005521; F:lamin binding; ISO:MGI.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0008307; F:structural constituent of muscle; ISO:MGI.
DR GO; GO:0017166; F:vinculin binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0086001; P:cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0008065; P:establishment of blood-nerve barrier; IMP:MGI.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR GO; GO:0055001; P:muscle cell development; IGI:MGI.
DR GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR GO; GO:0014904; P:myotube cell development; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IMP:BHF-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0045213; P:neurotransmitter receptor metabolic process; IMP:MGI.
DR GO; GO:0051647; P:nucleus localization; IMP:MGI.
DR GO; GO:0021629; P:olfactory nerve structural organization; IMP:MGI.
DR GO; GO:0043043; P:peptide biosynthetic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:BHF-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IMP:BHF-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IMP:BHF-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0090287; P:regulation of cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
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; IMP:BHF-UCL.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:BHF-UCL.
DR GO; GO:0014819; P:regulation of skeletal muscle contraction; IMP:BHF-UCL.
DR GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IMP:BHF-UCL.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IMP:MGI.
DR GO; GO:0009414; P:response to water deprivation; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
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 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; 16.
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 Actin-binding; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Membrane; Metal-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Zinc; Zinc-finger.
FT CHAIN 1..3678
FT /note="Dystrophin"
FT /id="PRO_0000076076"
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 341..449
FT /note="Spectrin 1"
FT REPEAT 450..558
FT /note="Spectrin 2"
FT REPEAT 561..669
FT /note="Spectrin 3"
FT REPEAT 721..830
FT /note="Spectrin 4"
FT REPEAT 832..936
FT /note="Spectrin 5"
FT REPEAT 945..1047
FT /note="Spectrin 6"
FT REPEAT 1050..1156
FT /note="Spectrin 7"
FT REPEAT 1159..1265
FT /note="Spectrin 8"
FT REPEAT 1268..1369
FT /note="Spectrin 9"
FT REPEAT 1370..1465
FT /note="Spectrin 10"
FT REPEAT 1470..1570
FT /note="Spectrin 11"
FT REPEAT 1573..1678
FT /note="Spectrin 12"
FT REPEAT 1681..1780
FT /note="Spectrin 13"
FT REPEAT 1781..1876
FT /note="Spectrin 14"
FT REPEAT 1879..1981
FT /note="Spectrin 15"
FT REPEAT 1994..2103
FT /note="Spectrin 16"
FT REPEAT 2106..2210
FT /note="Spectrin 17"
FT REPEAT 2213..2318
FT /note="Spectrin 18"
FT REPEAT 2319..2416
FT /note="Spectrin 19"
FT REPEAT 2468..2570
FT /note="Spectrin 20"
FT REPEAT 2573..2679
FT /note="Spectrin 21"
FT REPEAT 2682..2795
FT /note="Spectrin 22"
FT REPEAT 2801..2923
FT /note="Spectrin 23"
FT REPEAT 2928..3033
FT /note="Spectrin 24"
FT DOMAIN 3048..3081
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 3301..3357
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 REGION 313..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1915
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000269|PubMed:16777071"
FT REGION 3051..3401
FT /note="Interaction with SYNM"
FT /evidence="ECO:0000269|PubMed:16777071"
FT REGION 3459..3511
FT /note="Binds to SNTB1"
FT /evidence="ECO:0000250"
FT REGION 3521..3547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3596..3678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3596..3665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 3333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 3476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT MOD_RES 3610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 3617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 3659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11532"
FT CONFLICT 463
FT /note="D -> H (in Ref. 5; AAA37530)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="S -> F (in Ref. 5; AAA37530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3678 AA; 425832 MW; 53487B1E27104228 CRC64;
MLWWEEVEDC YEREDVQKKT FTKWINAQFS KFGKQHIDNL FSDLQDGKRL LDLLEGLTGQ
KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV
KNVMKTIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT SSWSDGLALN ALIHSHRPDL
FDWNSVVSQH SATQRLEHAF NIAKCQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP
QQVSIEAIQE VEMLPRTSSK VTREEHFQLH HQMHYSQQIT VSLAQGYEQT SSSPKPRFKS
YAFTQAAYVA TSDSTQSPYP SQHLEAPRDK SLDSSLMETE VNLDSYQTAL EEVLSWLLSA
EDTLRAQGEI SNDVEEVKEQ FHAHEGFMMD LTSHQGLVGN VLQLGSQLVG KGKLSEDEEA
EVQEQMNLLN SRWECLRVAS MEKQSKLHKV LMDLQNQKLK ELDDWLTKTE ERTKKMEEEP
FGPDLEDLKC QVQQHKVLQE DLEQEQVRVN SLTHMVVVVD ESSGDHATAA LEEQLKVLGD
RWANICRWTE DRWIVLQDIL LKWQHFTEEQ CLFSTWLSEK EDAMKNIQTS GFKDQNEMMS
SLHKISTLKI DLEKKKPTME KLSSLNQDLL SALKNKSVTQ KMEIWMENFA QRWDNLTQKL
EKSSAQISQA VTTTQPSLTQ TTVMETVTMV TTREQIMVKH AQEELPPPPP QKKRQITVDS
ELRKRLDVDI TELHSWITRS EAVLQSSEFA VYRKEGNISD LQEKVNAIAR EKAEKFRKLQ
DASRSAQALV EQMANEGVNA ESIRQASEQL NSRWTEFCQL LSERVNWLEY QTNIITFYNQ
LQQLEQMTTT AENLLKTQST TLSEPTAIKS QLKICKDEVN RLSALQPQIE QLKIQSLQLK
EKGQGPMFLD ADFVAFTNHF NHIFDGVRAK EKELQTIFDT LPPMRYQETM SSIRTWIQQS
ESKLSVPYLS VTEYEIMEER LGKLQALQSS LKEQQNGFNY LSDTVKEMAK KAPSEICQKY
LSEFEEIEGH WKKLSSQLVE SCQKLEEHMN KLRKFQNHIK TLQKWMAEVD VFLKEEWPAL
GDAEILKKQL KQCRLLVGDI QTIQPSLNSV NEGGQKIKSE AELEFASRLE TELRELNTQW
DHICRQVYTR KEALKAGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE
EMKRAKEEAL QKETKVKLLT ETVNSVIAHA PPSAQEALKK ELETLTTNYQ WLCTRLNGKC
KTLEEVWACW HELLSYLEKA NKWLNEVELK LKTMENVPAG PEEITEVLES LENLMHHSEE
NPNQIRLLAQ TLTDGGVMDE LINEELETFN SRWRELHEEA VRKQKLLEQS IQSAQEIEKS
LHLIQESLEF IDKQLAAYIT DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKDANQ
RVLSQIDVAQ KKLQDVSMKF RLFQKPANFE QRLEESKMIL DEVKMHLPAL ETKSVEQEVI
QSQLSHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK
VTERKQQLEK CLKLSRKMRK EMNVLTEWLA ATDTELTKRS AVEGMPSNLD SEVAWGKATQ
KEIEKQKAHL KSVTELGESL KMVLGKKETL VEDKLSLLNS NWIAVTSRVE EWLNLLLEYQ
KHMETFDQNI EQITKWIIHA DELLDESEKK KPQQKEDILK RLKAEMNDMR PKVDSTRDQA
AKLMANRGDH CRKVVEPQIS ELNRRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE
AEIQQGVNLK EEDFNKDMSE DNEGTVNELL QRGDNLQQRI TDERKREEIK IKQQLLQTKH
NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDEIEK KLASLPEPRD ERKLKEIDRE
LQKKKEELNA VRRQAEGLSE NGAAMAVEPT QIQLSKRWRQ IESNFAQFRR LNFAQIHTLH
EETMVVTTED MPLDVSYVPS TYLTEISHIL QALSEVDHLL NTPELCAKDF EDLFKQEESL
KNIKDNLQQI SGRIDIIHKK KTAALQSATS MEKVKVQEAV AQMDFQGEKL HRMYKERQGR
FDRSVEKWRH FHYDMKVFNQ WLNEVEQFFK KTQNPENWEH AKYKWYLKEL QDGIGQRQAV
VRTLNATGEE IIQQSSKTDV NILQEKLGSL SLRWHDICKE LAERRKRIEE QKNVLSEFQR
DLNEFVLWLE EADNIAITPL GDEQQLKEQL EQVKLLAEEL PLRQGILKQL NETGGAVLVS
APIRPEEQDK LEKKLKQTNL QWIKVSRALP EKQGELEVHL KDFRQLEEQL DHLLLWLSPI
RNQLEIYNQP SQAGPFDIKE IEVTVHGKQA DVERLLSKGQ HLYKEKPSTQ PVKRKLEDLR
SEWEAVNHLL RELRTKQPDR APGLSTTGAS ASQTVTLVTQ SVVTKETVIS KLEMPSSLLL
EVPALADFNR AWTELTDWLS LLDRVIKSQR VMVGDLEDIN EMIIKQKATL QDLEQRRPQL
EELITAAQNL KNKTSNQEAR TIITDRIERI QIQWDEVQEQ LQNRRQQLNE MLKDSTQWLE
AKEEAEQVIG QVRGKLDSWK EGPHTVDAIQ KKITETKQLA KDLRQRQISV DVANDLALKL
LRDYSADDTR KVHMITENIN TSWGNIHKRV SEQEAALEET HRLLQQFPLD LEKFLSWITE
AETTANVLQD ASRKEKLLED SRGVRELMKP WQDLQGEIET HTDIYHNLDE NGQKILRSLE
GSDEAPLLQR RLDNMNFKWS ELQKKSLNIR SHLEASSDQW KRLHLSLQEL LVWLQLKDDE
LSRQAPIGGD FPAVQKQNDI HRAFKRELKT KEPVIMSTLE TVRIFLTEQP LEGLEKLYQE
PRELPPEERA QNVTRLLRKQ AEEVNAEWDK LNLRSADWQR KIDEALERLQ ELQEAADELD
LKLRQAEVIK GSWQPVGDLL IDSLQDHLEK VKALRGEIAP LKENVNRVND LAHQLTTLGI
QLSPYNLSTL EDLNTRWRLL QVAVEDRVRQ LHEAHRDFGP ASQHFLSTSV QGPWERAISP
NKVPYYINHE TQTTCWDHPK MTELYQSLAD LNNVRFSAYR TAMKLRRLQK ALCLDLLSLS
AACDALDQHN LKQNDQPMDI LQIINCLTTI YDRLEQEHNN LVNVPLCVDM CLNWLLNVYD
TGRTGRIRVL SFKTGIISLC KAHLEDKYRY LFKQVASSTG FCDQRRLGLL LHDSIQIPRQ
LGEVASFGGS NIEPSVRSCF QFANNKPEIE AALFLDWMRL EPQSMVWLPV LHRVAAAETA
KHQAKCNICK ECPIIGFRYR SLKHFNYDIC QSCFFSGRVA KGHKMHYPMV EYCTPTTSGE
DVRDFAKVLK NKFRTKRYFA KHPRMGYLPV QTVLEGDNME TPVTLINFWP VDSAPASSPQ
LSHDDTHSRI EHYASRLAEM ENSNGSYLND SISPNESIDD EHLLIQHYCQ SLNQDSPLSQ
PRSPAQILIS LESEERGELE RILADLEEEN RNLQAEYDRL KQQHEHKGLS PLPSPPEMMP
TSPQSPRDAE LIAEAKLLRQ HKGRLEARMQ ILEDHNKQLE SQLHRLRQLL EQPQAEAKVN
GTTVSSPSTS LQRSDSSQPM LLRVVGSQTS ESMGEEDLLS PPQDTSTGLE EVMEQLNNSF
PSSRGRNAPG KPMREDTM
