DMD_CHICK
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 03-AUG-2022, entry version 152.
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.ENSGALP00000026200; -.
DR PaxDb; P11533; -.
DR PRIDE; P11533; -.
DR GeneID; 396236; -.
DR KEGG; gga:396236; -.
DR CTD; 1756; -.
DR VEuPathDB; HostDB:geneid_396236; -.
DR eggNOG; KOG4286; Eukaryota.
DR InParanoid; P11533; -.
DR OrthoDB; 72477at2759; -.
DR PhylomeDB; P11533; -.
DR PRO; PR:P11533; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 14.
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; IPR039959; Fimbrin/Plastin.
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; PTHR19961; PTHR19961; 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; 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; 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
