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 27-MAR-2024, entry version 218. 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 INTERACTION WITH NOS1. RX PubMed=7545544; DOI=10.1016/0092-8674(95)90471-9; RA Brenman J.E., Chao D.S., Xia H., Aldape K., Bredt D.S.; RT "Nitric oxide synthase complexed with dystrophin and absent from skeletal RT muscle sarcolemma in Duchenne muscular dystrophy."; RL Cell 82:743-752(1995). RN [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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, RC Pancreas, 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 [21] 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 [22] 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 Interacts with NOS1; localizes NOS1 to sarcolemma in muscle cells CC (PubMed:7545544). {ECO:0000250|UniProtKB:P11532, CC ECO:0000269|PubMed:10893187, ECO:0000269|PubMed:11430802, CC ECO:0000269|PubMed:11520903, ECO:0000269|PubMed:16777071, CC ECO:0000269|PubMed:19109891, ECO:0000269|PubMed:20634290, CC ECO:0000269|PubMed:7545544, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 48. DR CORUM; P11531; -. DR DIP; DIP-32899N; -. DR IntAct; P11531; 48. DR MINT; P11531; -. DR STRING; 10090.ENSMUSP00000109633; -. DR ChEMBL; CHEMBL5169117; -. DR GlyGen; P11531; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P11531; -. DR PhosphoSitePlus; P11531; -. DR SwissPalm; P11531; -. DR EPD; P11531; -. DR jPOST; P11531; -. DR MaxQB; P11531; -. DR PaxDb; 10090-ENSMUSP00000109633; -. DR PeptideAtlas; P11531; -. DR ProteomicsDB; 277346; -. [P11531-1] DR Pumba; P11531; -. DR Antibodypedia; 476; 704 antibodies from 38 providers. DR DNASU; 13405; -. DR Ensembl; ENSMUST00000114000.8; ENSMUSP00000109633.2; ENSMUSG00000045103.20. [P11531-1] DR GeneID; 13405; -. DR KEGG; mmu:13405; -. DR UCSC; uc009tri.2; mouse. [P11531-1] DR AGR; MGI:94909; -. 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; XVATTYP; -. DR OrthoDB; 2880153at2759; -. DR PhylomeDB; P11531; -. DR TreeFam; TF320178; -. DR Reactome; R-MMU-390522; Striated Muscle Contraction. DR BioGRID-ORCS; 13405; 0 hits in 81 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 278 other cell types or tissues. DR ExpressionAtlas; P11531; baseline and differential. 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: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: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: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:0099572; C:postsynaptic specialization; IDA:SynGO. 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: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:0006915; P:apoptotic process; IMP:MGI. DR GO; GO:0060348; P:bone development; IGI:MGI. 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:0061448; P:connective tissue development; IGI:MGI. DR GO; GO:0008340; P:determination of adult lifespan; IGI:MGI. 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:0010467; P:gene expression; IMP:MGI. DR GO; GO:0006954; P:inflammatory response; IMP:MGI. DR GO; GO:0060173; P:limb development; IGI:MGI. DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI. DR GO; GO:0032504; P:multicellular organism reproduction; IGI:MGI. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI. DR GO; GO:0055001; P:muscle cell development; IMP: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: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:1903409; P:reactive oxygen species biosynthetic process; IMP:MGI. 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:0090287; P:regulation of cellular response to growth factor stimulus; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP: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: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:0009410; P:response to xenobiotic stimulus; IMP:MGI. DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI. DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI. DR GO; GO:0055002; P:striated muscle cell development; IGI:MGI. DR GO; GO:0006941; P:striated muscle contraction; IGI:MGI. DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central. DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI. DR GO; GO:0090659; P:walking behavior; IGI:MGI. DR CDD; cd21231; CH_DMD_rpt1; 1. DR CDD; cd21233; CH_DMD_rpt2; 1. DR CDD; cd16246; EFh_DMD; 1. DR CDD; cd00176; SPEC; 11. DR CDD; cd00201; WW; 1. DR CDD; cd02334; ZZ_dystrophin; 1. DR Gene3D; 1.20.58.60; -; 16. DR Gene3D; 2.20.70.10; -; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 1.10.238.10; EF-hand; 2. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. 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 PANTHER; PTHR12268:SF25; DYSTROPHIN; 1. DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1. 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; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF46966; Spectrin repeat; 15. DR SUPFAM; SSF51045; WW domain; 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. DR Genevisible; P11531; MM. 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 //