DMD_CANLF
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 03-AUG-2022, entry version 134.
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). {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; 9612.ENSCAFP00000031637; -.
DR PaxDb; O97592; -.
DR GeneID; 606758; -.
DR KEGG; cfa:606758; -.
DR CTD; 1756; -.
DR eggNOG; KOG4286; Eukaryota.
DR InParanoid; O97592; -.
DR OrthoDB; 72477at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
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 CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 10.
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 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
