ID A0A2R9CNP5_PANPA Unreviewed; 3513 AA.
AC A0A2R9CNP5;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
GN Name=DMD {ECO:0000313|Ensembl:ENSPPAP00000039897.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000039897.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000039897.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000039897.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037032}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR002341}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR EMBL; AJFE02060024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02060033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPPAT00000062809.1; ENSPPAP00000039897.1; ENSPPAG00000042470.1.
DR GeneTree; ENSGT00940000154342; -.
DR OMA; XVATTYP; -.
DR Proteomes; UP000240080; Chromosome X.
DR Bgee; ENSPPAG00000042470; Expressed in heart and 6 other cell types or tissues.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 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; 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; 17.
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 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|PIRNR:PIRNR002341}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR002341}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR002341};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR002341};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002341};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|PIRNR:PIRNR002341};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|PIRNR:PIRNR002341};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 11..115
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 130..236
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 3051..3084
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 3304..3360
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT COILED 453..502
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 752..779
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1186..1216
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1908..1935
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2185..2215
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2312..2339
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2499..2605
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2918..2952
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3513 AA; 406850 MW; B5C1DD71F64804ED CRC64;
MSEVSSDERE DVQKKTFTKW VNAQFSKFGK QHIENLFSDL QDGRRLLDLL EGLTGQKLPK
EKGSTRVHAL NNVNKALRVL QNNNVDLVNI GSTDIVDGNH KLTLGLIWNI ILHWQVKNVM
KNIMAGLQQT NSEKILLSWV RQSTRNYPQV NVINFTTSWS DGLALNALIH SHRPDLFDWN
SVVCQQSATQ RLEHAFNIAR YQLGIEKLLD PEDVATTYPD KKSILMYITS LFQVLPQQVS
IEAIQEVEML PRPPKVTKEE HFQLHHQMHY SQQITVSLAQ GYERTSSPKP RFKSYAYTQA
AYVTTSDPTR SPFPSQHLEA PEDKSFGSSL MESEVNLDGY QTALEEVLSW LLSAEDTLQA
QGEISNDVDV VKEQFHTHEG YMMDLTAHQG RVGNILQLGS KLIGTGKLSE DEETEVQEQM
NLLNSRWECL RVASMEKQSN LHRVLMDLQN QKLKELNDWL TKTEERTRKM EEEPLGPDLE
DLKRQVQQHK VLQEDLEQEQ VRVNSLTHMV VVVDESSGDH ATAALEEQLK VLGDRWANIC
RWTEARWVLL QDILLKWQRL TEEQCLFSAW LSEKEDAVNK IHTTGFKDQN EMLSSLQKLA
VLKADLEKKK QSMGKLYSLK QDLLSTLKNK SVTQKTEAWL DNFARCWDNL VQKLEKSTAQ
ISQAVTTTQP SLTQTTVMET VTTVTTREQI LVKHAQEELP PPPPQKKRQI TVDSEIRKRL
DVDITELHSW ITRSEAVLQS PEFAIFRKEG NFSDLKEKVN AIEREKAEKF RKLQDASRSA
QALVEQMVNE GVNADSIKQA SEQLNSRWIE FCQLLSERLN WLEYQNNIIA FYNQLQQLEQ
MTTTAENWLK IQPTTPSEPT AIKSQLKICK DEVNRLSGLQ PQIERLKIQS IALKEKGQGP
MFLDADFVAF TNHFKQVFSD VQAREKELQT IFDTLPPMRY QETMSAIRTW VQQSETKLSI
PQLSVTDYEI MEQRLGELQA LQSSLQEQQS GLNYLSTTVK EMSKKAPSEI SRKYQSEFEE
IEGRWKKLSC QLVEHCQKLE EQMNKLRKIQ NHIQTLKKWM AEVDVFLKEE WPALGDSEIL
KKQLKQCRLL VNDIQTIQPS LNSVNEGGQK IKNEAEPEFA SRLEKELKEL NTQWDHMCQQ
VYARKEALKG GLEKTVSLQK DLSEMHEWMT QAEEEYLERD FEYKTPDELQ KAVEEMKRAK
EEAQQKEAKV KLLTESVNSV IAQAPPVAQE ALKKELETLT TNYQWLCTRL NGKCKTLEEV
WACWHELLSY LEKANKWLNE VEFKLKTTEN IPGGAEEISE VLDSLENLMR HSEDNPNQIR
ILAQTLTDGG VMDELINEEL ETFNSRWREL HEEAVRRQKL LEQSIQSAQE TEKSLHLIQE
SLTFIDKQLA AYIADKVDAA QMPQEAQKIQ SDLTSHEISL EEMKKHNQGK EAAQRVLSQI
DVAQKKLQDV SMKFRLFQKP ANFEQRLQES KMILDEVKMH LPALETKSVE QEVVQSQLNH
CVNLYKSLSE VKSEVEMVIK TGRQIVQKKQ TENPKELDER VTALKLHYNE LGAKVTERKQ
QLEKCLKLSR KMRKEMNVLT EWLAATDMEL TKRSAVEGMP SNLDSEVAWG KATQKEIEKQ
KVHLKSITEV GEALKTVLGK KETLVEDKLS LLNSNWIAVT SRAEEWLNLL LEYQKHMETF
DQNVDHITKW IIQADTLLDE SEKKKPQQKE DVLKRLKAEL NDIRPKVDST RDQAANLMAN
RGDHCRKLVE PQISELNHRF AAISHRIKTG KASIPLKELE QFNSDIQKLL EPLEAEIQQG
VNLKEEDFNK DMNEDNEGTV KELLQRGDNL QQRITDERKR EEIKIKQQLL QTKHNALKDL
RSQRRKKALE ISHQWYQYKR QADDLLKCLD DIEKKLASLP EPRDERKIKE IDRELQKKKE
ELNAVRRQAE GLSEDGAAMA VEPTQIQLSK RWREIESKFA QFRRLNFAQI HTVREETMMV
MTEDMPLEIS YVPSTYLTEI THVSQALSEV EQLLNAPDLC AKDFEDLFKQ EESLKNIKDS
LQQSSGRIDI IHSKKTAALQ SATPVERVKL QEALSQLDFQ WEKVNKMYKD RQGRFDRSVE
KWRRFHYDIK IFNQWLTEAE QFLRKTQIPE NWEHAKYKWY LKELQDGIGQ RQTVVRALNA
TGEEIIQQSS KTDASILQEK LGSLNLRWQE VCKQLSDRKK RLEEQKNILS EFQRDLNEFV
LWLEEADNIA SIPLEPGNEQ QLKEKLEQVK LLVEELPLRQ GILKQLNETG GPVLVSAPIS
PEEQDKLENK LKQTNLQWIK VSRALPEKQG EIEAQIKDLG QLEKKLEDLE EQLNHLLLWL
SPIRNQLEIY NQPNQEGPFD IKETEIAVQA KQPDVEEILS KGQHLYKEKP ATQPVKRKLE
DLSSEWKAVN RLLQELRAKQ PDLAPGLTTI GASPTQTVTL VTQPVVTKET AISKLEMPSS
LMLEVPALAD FNRAWTELTD WLSLLDRVIK SQRVMVGDLE DINEMIIKQK ATMQDLEQRR
PQLEELITAA QNLKNKTSNQ EARTIITDRI ERIQNQWDEV QEHLQNRRQQ LNEMLKDSTQ
WLEAKEEAEQ VLGQARAKLE SWKEGPYTID AIQKKITETK QLAKDLRQWQ INVDVANDLA
LKLLRDYSAD DTRKVHMITE NINASWGSIH KRVSEREAAL EETHRLLQQF PLDLEKFLAW
LTEAETTANV LQDATRKERL LEDSKGVKEL MKQWQDLQGE IEAHTDVYHN LDENSQKILR
SLEGSDDAVL LQRRLDNMNF KWSELRKKSL NIRSHLEASS DQWKRLHLSL QELLVWLQLK
DDELSRQAPI GGDFPAVQKQ NDVHRAFKRE LKTKEPVIMS TLETVRIFLT EQPLEGLEKL
YQEPRELPPE ERAQNVTRLL RKQAEEVNTE WEKLNLHSTD WQRKIDETLE RLQELQEATD
ELDLKLRQAE VIKGSWQPVG DLLIDSLQDH LEKVKALRGE IAPLKENVSH VNDLARQLTT
LGIQLSPYNL STLEDLNTRW KLLQVAVEDR VRQLHEAHRD FGPASQHFLS TSVQGPWERA
ISPNKVPYYI NHETQTTCWD HPKMTELYQS LADLNNVRFS AYRTAMKLRR LQKALCLDLL
SLSAACDALD QHNLKQNDQP MDILQIINCL TTIYDRLEQE HNNLVNVPLC VDMCLNWLLN
VYDTGRTGRI RVLSFKTGII SLCKAHLEDK YRYLFKQVAS STGFCDQRRL GLLLHDSIQI
PRQLGEVASF GGSNIEPSVR SCFQFANNKP EIEAALFLDW MRLEPQSMVW LPVLHRVAAA
ETAKHQAKCN ICKECPIIGF RYRSLKHFNY DICQSCFFSG RVAKGHKMHY PMVEYCTPTT
SGEDVRDFAK VLKNKFRTKR YFAKHPRMGY LPVQTVLEGD NMETPVTLIN FWPVDSAPAS
SPQLSHDDTH SRIEHYASRL AEMENSNGSY LNDSISPNES IDDEHLLIQH YCQSLNQDSP
LSQPRSPAQI LISLESEERG ELERILADLE EEN
//
