ID   DMD_CHICK               Reviewed;        3660 AA.
AC   P11533;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Dystrophin;
GN   Name=DMD;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3062582; DOI=10.1093/nar/16.24.11815;
RA   Lemaire C., Heilig R., Mandel J.-L.;
RT   "Nucleotide sequence of chicken dystrophin cDNA.";
RL   Nucleic Acids Res. 16:11815-11815(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=3072195; DOI=10.1002/j.1460-2075.1988.tb03311.x;
RA   Lemaire C., Heilig R., Mandel J.L.;
RT   "The chicken dystrophin cDNA: striking conservation of the C-terminal
RT   coding and 3' untranslated regions between man and chicken.";
RL   EMBO J. 7:4157-4162(1988).
CC   -!- FUNCTION: May play a role in anchoring the cytoskeleton to the plasma
CC       membrane.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane
CC       protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Postsynaptic cell
CC       membrane {ECO:0000250}. Note=Localizes to neuromuscular junctions.
CC       {ECO:0000250}.
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DR   EMBL; X13369; CAA31746.1; -; mRNA.
DR   PIR; S02041; S02041.
DR   RefSeq; NP_990630.2; NM_205299.2.
DR   SMR; P11533; -.
DR   STRING; 9031.ENSGALP00000071548; -.
DR   PaxDb; 9031-ENSGALP00000026200; -.
DR   GeneID; 396236; -.
DR   KEGG; gga:396236; -.
DR   CTD; 1756; -.
DR   VEuPathDB; HostDB:geneid_396236; -.
DR   eggNOG; KOG4286; Eukaryota.
DR   InParanoid; P11533; -.
DR   PhylomeDB; P11533; -.
DR   PRO; PR:P11533; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
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; 14.
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; 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; 21.
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; 19.
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; Postsynaptic cell membrane; Reference proteome; Repeat;
KW   Synapse; Zinc; Zinc-finger.
FT   CHAIN           1..3660
FT                   /note="Dystrophin"
FT                   /id="PRO_0000076078"
FT   DOMAIN          19..123
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          138..244
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          1470..1570
FT                   /note="Spectrin 10"
FT   REPEAT          1573..1678
FT                   /note="Spectrin 11"
FT   REPEAT          1681..1782
FT                   /note="Spectrin 12"
FT   REPEAT          1879..1981
FT                   /note="Spectrin 13"
FT   REPEAT          2013..2103
FT                   /note="Spectrin 14"
FT   REPEAT          2106..2211
FT                   /note="Spectrin 15"
FT   REPEAT          2214..2321
FT                   /note="Spectrin 16"
FT   REPEAT          2472..2574
FT                   /note="Spectrin 17"
FT   REPEAT          2577..2683
FT                   /note="Spectrin 18"
FT   REPEAT          2686..2799
FT                   /note="Spectrin 19"
FT   REPEAT          2802..2904
FT                   /note="Spectrin 20"
FT   REPEAT          2906..2928
FT                   /note="Spectrin 21"
FT   REPEAT          2931..3037
FT                   /note="Spectrin 22"
FT   DOMAIN          3052..3085
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   ZN_FING         3305..3361
FT                   /note="ZZ-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   REGION          1..244
FT                   /note="Actin-binding"
FT   REGION          3503..3526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3575..3660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3577..3647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         3310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         3313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         3334
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   VARIANT         1171
FT                   /note="Missing"
FT   VARIANT         1869
FT                   /note="Q -> H"
FT   VARIANT         1885
FT                   /note="K -> R"
SQ   SEQUENCE   3660 AA;  422881 MW;  85493DAF6D5B6D4A CRC64;
     MSAHVLWYEE VEDDYEREDV QKKTFTKWIN AQFAKCGRRC IEDLFNDFRD GRKLLELLEC
     LTGQKIAKEK GSTRVHALNN VNKALQILQR NNVDLVNIGS SDIVDGNHKL TLGLIWNIIL
     HWQVKDVMKN IMAGLQQTNS EKILLSWVRQ STRNYPQVNV INFTSSWSDG LAFNALLHSH
     RPDLFDWNAV ASQQSPVQRL DHAFNIARQH LGIEKLLDPE DVATACPDKK SILMYVTSLF
     QVLPQQVTME AIREVEMLPR HSRVTTEEHI QVHHQQHFSQ EITVNIPQRP SPSPKPRFKS
     YAYAQTAYVI PPDQKRRQVP PQFLETVEKR TYTTTVMRSE MDLDSYQTAL EEVLTWLLSA
     EDALQAQGDI SSDVEVVKEQ FHTHEGFMME LTAHQGRVGN VLQVGSQLLA MGKLSDDEEN
     EIQEQMNLLN SRWESLRVAS MEKQSNLHKI LMDLQNQQLA QLADWLTKTE ERTKKIDSEP
     LGPDLEDLKR QVEEHKAFQD DLEQEQVKVN SLTHMVVVVD ENSGDKATAA LEEQLQHFGS
     RWAAICRWTE DRWVLLQDIL RKWQHFAEEQ CLFDAWLTEK EGSLSKIQTS DFKDENEMLT
     SLRKLAILKG DIEMKKQMMS KLKSLSRDLL VAVKNKAVAQ KLESRLENFA QRWDSLVQKL
     ESDSKQVSQA VTTTQTSLTQ TTVMETVTMV TTREQILVKH AKEELPPPPP HKKRQLLVDS
     EIRKRFDSDT TELHSWMTRS EAVLQSPEFA IYRKEGNLSD LRERVNAIQR EKPEKYRKLQ
     DASRSAEALV EQMVNEGLNA DNIRQASEQL KSRWIEFCQL LSERLVWLEY QNSIIDFYSQ
     LQRLEQTAIT AENWLKAQPT PATDPATVKI QLEKCKDEII RMSTLQPQIE RLKAQSQALK
     EKEQCPVFLD ADLAAFTSHF KQILADMHTR EKQLQTIFDS LPPARYKDTV TTILSWIQQS
     ETKVSIPPVA VAEYEIMEQR LGELKALQSS LQEQQKGLKY LNTTVEDLSR KAPAEVSQKY
     RSEVELIVGR WKKLSSQLVE HCQKLEDLMT KLQRFQNDTK TLKKWMAEVD VFLKEEWPAL
     GDSEALEKQL EQCTALVNDI QTIQPSLNSV NEIGKKMKRE AEPEFASRIA TELKDLNAQW
     EHICQQAHAK KAALKGGLDK TVSLRKDLSE MHEWITQAEE EYLERDFEYK TPEELQKAVE
     ELKRAKEDAM QKEVKVKLIT DSVNNFIAKA PPAANEALKK ELDVLITSYQ RLCSRLNGKC
     KTLEEVWACW HELLSYLDAE NKWLNEVELK LKATENIQGG AEEISESLDS LERLMRHPED
     NRNQIRELAQ TLTDGGILDE LINEKLEKFN TRWEELQQEA VRRQKSLEQS IQSAQETDKT
     LRLIQESLAA IDKQLTAYTA DRVDAAQVPQ EAQKIQSELT SHEISLEEMK KRNRGKESAK
     RVLSQIDVAQ KKLQDVSMKF RLFQKPANFE QRLQECKRIL DEVKLQVPKL ETKSVEQEVV
     QSHLDHCMKL YKSLSEVKSE VETVIKTGRQ IVQKQQTENP KELDERLTAL KLQYNELGAK
     VTEKKQELEK CLKLSRKLRK EINSLTEWLA ATDVELTKRS AVQGMPSNLD AEIAWGKATR
     KEIEKRQVQL KNICDLGENL KTVLKGKESL VEDKLSLLNS NWIAVTSRAE EWLNLLMEYQ
     KHMEAFDQKV ANVTTWIYRA EILLDESDKQ KPQQKEETLK RLKAELNDMH PKVDSVRDQA
     VDLMTNRGDH CRKVIEPKLS ELNHRFAAIS QRIKSGKPFI PLKELEQFDF DIQKLLEPLE
     VEIQQGVNLK EEDFNKDMSE DDESTVKELL QRGDTLQKRI TDERKREEIK IKQQLLQTKH
     NALKDLRSQR RKKALEISHQ WYQYKRQADD LMTWLDDIEK KLASLPDHKD EQKLKEIGGE
     LEKKKEDLNA VNRQAERLSK DGAAKAVEPT LVQLSKRWRD FESKFAQFRR LNYAQIQTVL
     EDTTFVMTES MTVETTYVPS TYLAEILQLL QALSEVEERL NSPVLQAKDC EDLLKQEECL
     KNIKDCLGRL QGHIDIIHSK KTPALQSATP RETANIQDKL TQLNSQWEKV NKMYRDRQAR
     FDKSKEKWRL FHCEMKSFNE WLTETEEKLS RAQIEAGDVG HVKTKQFLQE LQDGIGRQQT
     VVKTLNVTGE EIIEQSSAAD ANVLKEQLGN LNTRWQEICR QLVEKRKRIE EEKNILSEFQ
     EDLNKLILWL EETENVIAIP LEPGNEDQLR DCLGKVKLRV EELLPHKGIL KRLNETGGTT
     LGSASLNPER KHKLESTLKE ASRRLLKVSR DLPEKQKEIE ILLKDFIELN QQINQLTLWI
     TPVKNQLELY NQVGQPGAFD IKETEAAVQA KQPNVEEVLS KGCHLYKEKP ATHPVKKKLE
     DLNADWKAIN HLILQLKEKP TFGEPALTSP GVLTSGQTVA VDTQARVTKE TTSFTPEMPS
     SVLLEVPALA DFNKAWAELT DWLSRLDREI KAQRVTVGDL DDINDMIIKQ KANMQDLEQR
     RPQLDELITA AQNLKNKTSN QEARTIITDR IEKIQSQWDD VHGYLQNRRQ QLHEMQKDST
     QWLEAKQEAE QVLEQAKAKL ESWKEISYTV EALKKQNSEL KQFSKEIRQW QMNIEGVNDV
     ALKPVRDYSA DDTRKVELMT DNINATWATI NKRVSEREAA LESALLMLQE FYLDLEKFLA
     WLTEAETTAN VLQDATHKEK TLEDPQMVRE LMKQWQDLQA EIDAHTDIFH NLDENGQKIL
     RSLEGSEDAV LLQRRLDNMN FRWSELRKKS LNIRSHLEAS TDQWKRLHLS LQELLAWLQL
     KEDELKQQAP IGGDIPTVQK QNDVHRTFKR ELKTKEPVIM NALETVRLFL ADQPVEGLEK
     VYPEPRDLSP EERAQNVTKV LRRQADDVRT EWDKLNLRSA DWQKKIDDAL ERLQGLQEAM
     DELDLKLRQA EAFKGSWQPV GDLLIDSLQD HLEKVKVYRA EMVPLKEKVH QVNELAHRFA
     PPDIQLSPYT LSCLEDLNTR WKVLQVAIDE RIRQLHEAHR DFGPTSQHFL TTSVQGPWER
     AISPNKVPYY INHETQTTCW DHPKMTELYQ SLADLNNVRF SAYRTAMKLR RLQKALCLDL
     LNLSAACDAL DQHNLKQNDQ PMDILQIINC LTTIYDRLEQ EHNNLVNVPL CVDMCLNWLL
     NVYDTGRTGR IRVLSFKTGV VSLCKAHLED KYRYLFKQVA SSTGFCDQRR LGLLLHDSIQ
     IPRQLGEVAS FGGSNIEPSV RSCFQFANNK PEIEAALFLD WMRLEPQSMV WLPVLHRVAA
     AETAKHQAKC NICKECPIIG FRYRSLKHFN YDICQSCFFS GRVAKGHKMH YPMVEYCTPT
     TSGEDVRDFA KVLKNKFRTK RYFAKHPRMG YLPVQTVLEG DNMETPVTLI NFWPVDSALA
     EMENSNGSYL NDSISPNESI DDEHLLIQHY CQSLNQESPL SQPRSPAQIL ISLESEERGE
     LERILADLEE ENRNLQAEYD RLKQQHDHKG LSPLPSPPEM MPVSPQSPRD AELIAEAKLL
     RQHKGRLEAR MQILEDHNKQ LESQLHRLRQ LLEQPQADAK VNGTTLSSPS TSLQRSDSSQ
     PMLLRVVGSQ TSETMGEDDL LSPPQDTSTG LEEVMEQLNN SFPSSRGRNA PGKPVREATM
//