ID   DMD_CANLF               Reviewed;        3680 AA.
AC   O97592;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Dystrophin;
GN   Name=DMD;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Golden retriever;
RX   PubMed=9655116;
RX   DOI=10.1002/(sici)1097-4598(199808)21:8<991::aid-mus2>3.0.co;2-0;
RA   Schatzberg S.J., Anderson L.V., Wilton S.D., Kornegay J.N., Mann C.J.,
RA   Solomon G.G., Sharp N.J.;
RT   "Alternative dystrophin gene transcripts in golden retriever muscular
RT   dystrophy.";
RL   Muscle Nerve 21:991-998(1998).
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   -!- SUBUNIT: Interacts with SYNM (By similarity). 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. Directly
CC       interacts with ANK2 and ANK3; these interactions do not interfere with
CC       betaDAG1-binding and are necessary for proper localization in muscle
CC       cells. Identified in a dystroglycan complex that contains at least PRX,
CC       DRP2, UTRN, DMD and DAG1 (By similarity). Interacts with DTNB (By
CC       similarity). Interacts with PGM5; the interaction is direct (By
CC       similarity). Interacts with NOS1; localizes NOS1 to sarcolemma in
CC       muscle cells (By similarity). {ECO:0000250|UniProtKB:P11530,
CC       ECO:0000250|UniProtKB:P11531, ECO:0000250|UniProtKB:P11532}.
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}.
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DR   EMBL; AF070485; AAC83646.1; -; mRNA.
DR   RefSeq; NP_001003343.1; NM_001003343.1.
DR   SMR; O97592; -.
DR   STRING; 9615.ENSCAFP00000031637; -.
DR   PaxDb; 9612-ENSCAFP00000031637; -.
DR   GeneID; 606758; -.
DR   KEGG; cfa:606758; -.
DR   CTD; 1756; -.
DR   eggNOG; KOG4286; Eukaryota.
DR   InParanoid; O97592; -.
DR   OrthoDB; 2880153at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR   GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR   GO; GO:0090257; P:regulation of muscle system process; IBA:GO_Central.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IBA:GO_Central.
DR   GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR   CDD; cd21231; CH_DMD_rpt1; 1.
DR   CDD; cd21233; CH_DMD_rpt2; 1.
DR   CDD; cd16246; EFh_DMD; 1.
DR   CDD; cd00176; SPEC; 10.
DR   CDD; cd00201; WW; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 1.20.58.60; -; 17.
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; 16.
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.
PE   2: Evidence at transcript level;
KW   Actin-binding; Calcium; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW   Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT   CHAIN           1..3680
FT                   /note="Dystrophin"
FT                   /id="PRO_0000076074"
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          340..448
FT                   /note="Spectrin 1"
FT   REPEAT          449..557
FT                   /note="Spectrin 2"
FT   REPEAT          560..668
FT                   /note="Spectrin 3"
FT   REPEAT          720..829
FT                   /note="Spectrin 4"
FT   REPEAT          831..935
FT                   /note="Spectrin 5"
FT   REPEAT          944..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..2320
FT                   /note="Spectrin 18"
FT   REPEAT          2321..2418
FT                   /note="Spectrin 19"
FT   REPEAT          2470..2572
FT                   /note="Spectrin 20"
FT   REPEAT          2575..2681
FT                   /note="Spectrin 21"
FT   REPEAT          2684..2797
FT                   /note="Spectrin 22"
FT   REPEAT          2803..2925
FT                   /note="Spectrin 23"
FT   REPEAT          2930..3035
FT                   /note="Spectrin 24"
FT   DOMAIN          3050..3083
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   ZN_FING         3303..3359
FT                   /note="ZZ-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   REGION          1..237
FT                   /note="Actin-binding"
FT   REGION          63..72
FT                   /note="ANK2- and ANK-3 binding"
FT                   /evidence="ECO:0000250"
FT   REGION          310..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1418..1915
FT                   /note="Interaction with SYNM"
FT                   /evidence="ECO:0000250"
FT   REGION          3053..3403
FT                   /note="Interaction with SYNM"
FT                   /evidence="ECO:0000250"
FT   REGION          3461..3513
FT                   /note="Binds to SNTB1"
FT                   /evidence="ECO:0000250"
FT   REGION          3524..3549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3595..3680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3597..3668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         3308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         3311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         3332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         3335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   MOD_RES         3478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3607
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3608
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3618
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3619
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
FT   MOD_RES         3661
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11532"
SQ   SEQUENCE   3680 AA;  425653 MW;  539F1C9D72377872 CRC64;
     MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ
     KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV
     KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL
     FDWNSVVCQQ SATQRLEHAF NIAKYQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP
     QQVSIEAIQE VEMLPRPSQV TREEHFQIHH QMHYSQQITV SLAQGYERAP SFPKPRFKSY
     AYTQAAYVTT SDPTRSPLPS QHLETPEDKS FGRSLTETEA NLDSYQTALE EVLSWLLSAE
     DALQAQGEIS NDVEEVKEQF HTHEGYMMDL TSHQGRVGNV LQLGSQLIGT GKLSEDEETE
     VQEQMNLLNS RWECLRVASM EKQSNLHKVL MDLQNQQLKE LNDWLTKTEE RTRKMEKEPL
     GPDIEDLKRQ VQQHKVLQED LEQEQVRVNS LTHMVVVVDE SSGDHATAAL EEQLKVLGDR
     WANICRWTED RWVLLQDILL KWQRFTEEQC LFSAWLSEKE DAVNKIHTTG FKDQSEVLSN
     LQKLAVLKTD LEKKKQTMDK LCSLNQDLLS ALKNTVVAHK MEAWLDNFAQ RWDNLVQKLE
     KSSAQISQAV TTTQPSLTQT TVMETVTMVT TREHILVKHA QEELPPPPPQ KKRQIIVDSE
     IRKRLDVDIT ELHSWITRSE AVLQSPEFAI YRKEGNFSDL KEKVNAIERE KAEKFRKLQD
     ASRSAQALVE QMVNEGVNAD SIKQASEQLN SRWIEFCQLL SERLNWLEYQ NNIITFYNQL
     QQLEQMTTTA ENWLKTQPTT TSEPTAIKSQ LKICKDEINR LSALQPQIER LKIQSIALKE
     KGQGPMFLDA DFVAFTNHFN QVFADVQARE KELQTIFDSL PPMRYQETMS TILTWIQQSE
     TKLSIPQVTV TEYDIMEQRL GELQALQSSL QEQQNGLNYL STTVKEMSKK APLSDISRKY
     QSEFEEIEGR WKKLSSQLVE HCQKLEEQMA KLRKIQNHIK TLKKWITEVD VFLKEEWPAL
     GDSEILKRQL KQCRLLVNDI QTIQPSLNSV NEGAQKMKNE AEPEFAGRLE TELRELNTQW
     DYMCRQVYAR KEALKGGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE
     EMKRAKEEAQ QKEAKVKLLT ESVNSVIAQA PPAAQEALKK ELDTLTTNYQ WLCTRLNGKC
     KTLEEVWACW HELLSYLEKA NKWLSEVEVK LKTTENISGG AEEIAEVLDS LENLMQHSED
     NPNQIRILAQ TLTDGGVMDE LINEELETFN SRWRELHEEA VRRQKLLEQS IQSAQEIEKS
     LHLIQESLSS IDKQLAAYIA DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKETAQ
     RVLSQIDVAQ KKLQDVSMKF RLFQKPANFE QRLQESKMIL DEVKMHLPAL ETKSVEQEVV
     QSQLNHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK
     VTERKQQLEK CLKLSRKMRK EMNALTEWLA ATDMELTKRS AVEGMPSNLD SEVAWGKATQ
     KEIEKQKVHL KSVTEVGEAL KTVLGKKEML VEDKLSLLNS NWIAVTSRAE EWLNLLLEYQ
     KHMETFDQNV DYITNWIIQA DALLDESEKK KPQQKEDILK RLKAEMNDIR PKVDSTRDQA
     ANLMANRGDH CRKVVEPKIS ELNHRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE
     AEIQQGVNLK EEDFNKDMSE DNEGTVKELL QRGDNLQQRI TDERKREEIK IKQQLLQTKH
     NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDDIEK KLASLPEPRD ERKIKEIDRE
     LQKKKEELNA VRRQAEGLSE DGAAMAVEPT QIQLSKRWRE IESKFAQFRR LNFAQIHTVH
     EESVVAMTED MPLEISYVPS TYLTEITHVS QALSEVEELL NAPDLCAQDF EDLFKQEESL
     KNIKDSLQQI SGRIDIIHNK KTAALHSATP AERAKLQEAL SRLDFQWERV NNMYKDRQGR
     FDRSVEKWRR FHYDMKILNQ WLTEAEQFLK KTQIPENWEH AKYKWYLKEL QDGIGQRQSV
     VRVLNATGEE IIQQSSKTDA SILQEKLGSL NLRWQEVCKQ LAERKKRLEE QKNILSEFQR
     DVNEFVLWLE EADNVANIPL EPGNEQQLKE KLEQVKLLAE ELPLRQGILK QLNETGGTVL
     VSAPLSPEEQ DKLENKLKQT NLQWIKVSRN LPEKQEEIEA HVKDLGQLEE QLNHLLLWLS
     PIRNQLEIYN QPNQTGPFDI KEIEVAVQAK QPDVEGILSK GQHLYKEKPA TQPAKRKLED
     LSSDWKVVTQ LLQELRAKQP GPAPGLTTVR APPSQTVTLV TQPAVTKETA ISKLEMPSSL
     LLEVPALADF NRAWTELTDW LSLLDRVIKS QRVMVGDLED INEMIIKQKA TLQDLEQRRP
     QLEELITAAQ NLKNKTSNQE ARTIITDRIE RIQSQWDEVQ EHLQNRRLQL TEMLKDSTQW
     LEAKEEAEQV LGQARAKLES WKEAPYTVDA IQKKITETKQ LAKDLRQWQI NVDVANDLAL
     KLLRDYSADD TRKVHMITEN INASWASIHK RLSEREAALE ETHRLLQQFP LDLEKFLAWL
     TEAETTANVL QDATHKERLL EDSKGVRELM KQWQDLQGEI EAHTDIYHNL DENGQKVLRS
     LEGSDDAALL QRRLDNMNFK WSELRKKSLN IRSHLEASSD QWKRLHLSLQ ELLVWLQLKD
     DELSRQAPIG GDFPAVQKQN DVHRAFKREL KTKEPVIMST LETVRIFLTE QPLEGLEKLY
     QEPRELPPEE RAQNVTRLLR KQAEEVNTQW EKLNVHSADW QRKIDEALER LQELQEATDE
     LDLKLRQAEV IKGSWQPVGD LLIDSLQDHL EKVKALRGEI TPLKENVSYV NDLARQLTTL
     GIQLSPYNLN TLEDLNTRWK LLQVAIEDRI RQLHEAHRDF GPASQHFLST SVQGPWERAI
     SPNKVPYYIN HETQTTCWDH PKMTELYQSL ADLNNVRFSA YRTAMKLRRL QKALCLDLLS
     LSAACDALDQ HNLKQNDQPM DILQVINCLT TIYDRLEQEH NNLVNVPLCV DMCLNWLLNV
     YDTGRTGRIR VLSFKTGIIS LCKAHLEDKY RYLFKQVASS TGFCDQRRLG LLLHDSIQIP
     RQLGEVASFG GSNIEPSVRS CFQFANNKPE IEAALFLDWM RLEPQSMVWL PVLHRVAAAE
     TAKHQAKCNI CKECPIIGFR YRSLKHFNYD ICQSCFFSGR VAKGHKMHYP MVEYCTPTTS
     GEDVRDFAKV LKNKFRTKRY FAKHPRMGYL PVQTVLEGDN METPVTLINF WPVDSAPASS
     PQLSHDDTHS RIEHYASRLK KMENSNGSYL NDSISPNESI DDEHLLIQHY WRSLNQESPL
     SQPRSPAQIL ISLESEERGE LERILADLEG RNRNLQAEYD RLKQQHEHKG LSPLPSPPEM
     MPTSPQSPRD AELIAEAKLL RQHKGRLEAR MQILEDHNKQ LESQLHRLRQ LLEQPQAEAK
     VNGTTVSSPS TSLQRSDSSQ PMLLRVVGSQ TSESMGEEDL LSPPQDTSTG LEEVMEQLNH
     SFPSSRGRNT PGKPMREDTM
//