ID F6Z1L7_HORSE Unreviewed; 2329 AA.
AC F6Z1L7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 4.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
GN Name=DMD {ECO:0000313|Ensembl:ENSECAP00000019634.4,
GN ECO:0000313|VGNC:VGNC:112408};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019634.4, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000019634.4, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019634.4,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000019634.4}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019634.4};
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|PIRNR:PIRNR002341}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR AlphaFoldDB; F6Z1L7; -.
DR Ensembl; ENSECAT00000023688.4; ENSECAP00000019634.4; ENSECAG00000015834.5.
DR VGNC; VGNC:112408; DMD.
DR GeneTree; ENSGT00940000154342; -.
DR HOGENOM; CLU_001187_1_2_1; -.
DR TreeFam; TF333986; -.
DR Proteomes; UP000002281; Chromosome X.
DR Bgee; ENSECAG00000015834; Expressed in gluteus medius and 22 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: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; cd16246; EFh_DMD; 1.
DR CDD; cd00176; SPEC; 6.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 9.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 11.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR SMART; SM00150; SPEC; 14.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 11.
DR SUPFAM; SSF51045; WW domain; 1.
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|PIRNR:PIRNR002341};
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|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|PIRNR:PIRNR002341};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
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 1699..1732
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1952..2008
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 2172..2198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2247..2329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 568..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 845..875
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1152..1196
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1571..1605
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2213..2247
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2247..2317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2329 AA; 269242 MW; CDF39F838CCDD80C CRC64;
MSGRKLRNLS YRKAVRRQKL LEQSIQSAQE IEKSLHLIQE SLSSIDKQLT AYIADKVDAA
QMPQEAQKIQ SDLTSHEISL EEMKKRNQGK ETAQRVLSQI DVAQKKLQDV SMKFRLFQKP
ANFEQRLQES KMILDEVKMH LPALETKSVE QEVVQSQLNH CVNLYKSLSE VKSEVEMVIK
TGRQIVQKKQ TENPKELDER VTALKLHYNE LGAKVTERKQ QLEKCLKLSR KMRKEMNALT
EWLAATDMEL TKRSAVEGMP SNLDSEVAWG KATQKEIEKQ KVHLKSVTEL GEALKTVLGK
KETLVEDKLS LLNSNWIAVT SRAEEWLNLL LEYQKHMETF DQHVDHITNW IIQADTLLDE
SEKKKPQQKE DVLKRLKAEM NDMRPKVDST RDQAANLMAN RGDHCRKVVE PKISELNHRF
AAISHRIKTG KASIPLKELE QFNSDIQKLL EPLEAEIQQG VNLKEEDFNK DMSEDNEGTV
KELLQRGDNL QQRITDERKR EEIKIKQQLL QTKHNALKDL RSQRRKKALE ISHQWYQYKR
QADDLLKCLD DIEKKLASLP EPRDERKIKE IDRELQKKKE ELNAVRRQAE GLSEDGAAMA
VEPTQIQLSK RWREIESKFA QFRRLNFAQI HTVHEESVMV MTEDMPLEIS YVPSTYLTEI
THVSQALSEV EQLLNAPDLR AKDFEDLFKQ EESLKNIKDN LQQISGRIDV IHNKKTAALQ
SATPAERAKL QEALSQLDFQ WESVNKVYKD RQGRFDRSVE KWRRFHYDMK IFNQWLTEAE
QFLKKTQIPE NWEHAKYKWY LKELQDGIGQ RQTVVRVLNA TGEEIIQQSS KTDASILQEK
LGSLNLRWQE VCKQLAERKK RLEEQKNILS EFQRDLNEFV LWLEEADNVT SVPLEPGNEQ
QLKEKLDQVK LLAEELPLRQ GILKQLNETG GTVLVSAPIS PEDQDKLENK LKQTNLQWIK
VSRDLPEKQG EIEAHIKDLG QFEEQLNHLL LWLSPIRKQL EIYNQPDQTG PFDIKETEAA
VQAKQPDVEG ILSKGQHLYK EKPAPEPVKR KLEDLNSEWK AVTRLLQELR AKRPGPAPGL
TTVGASPSQT VTLVTQPVVT KETAISKLEM PSSLLLEVPA LADFNRAWTE LTDWLSLLDQ
VIKSQRVMVG DLEDINEMII KQKATLQDLE QRRPQLEELI TAAQNLKNKT SNQEARTIIT
DRIERIQSQW DEVQEHLQNR RQQLNEMLKD STQWLEAKEE AEQVLGQARA KLESWKEGPY
TMDAIQRKIT ETKQLAKDLR QWQINVDVAN DLALKLLRDY SADDTRKVHM ITENINASWA
SIHKRVSEQE AALEETHRLL QQFPLDLEKF LAWLTEAETT ANVLQDATHK ERLLEDSKGV
RELMKQWQDL QGEIEAHTDI YHNLDENGQK ILRSLEGSDD AIVLQRRLDN MNFKWSELRK
KSLNIRSHLE ASSDQWKRLH LSLQELLVWL QLKDDELSRQ APIGGDFPAV QKQNDVHRAF
KRELKTKEPV IMSTLETVRI FLTEQPLEGL EKLYQEPREL PPEERAQNVT RLLRKQAEEV
NTEWEKLNLH SADWQRKIDE ALERLQELQE ATDELDLKLR QAEVIKGSWQ PVGDLLIDSL
QDHLEKVKIA PLKENVSHVN DLARQLTTLG IQLSPYNLST LEDLNTRWKL LQVAVEDRIR
QLHEAHRDFG PASQHFLSTS VQGPWERAIS PNKVPYYINH ETQTTCWDHP KMTELYQSLA
DLNNVRFSAY RTAMKLRRLQ KALCLDLLSL SAACDALDQH NLKQNDQPMD ILQIINCLTT
IYDRLEQEHS NLVNVPLCVD MCLNWLLNVY DTGRTGRIRV LSFKTGIISL CKAHLEDKYR
YLFKQVASST GFCDQRRLGL LLHDSIQIPR QLGEVASFGG SNIEPSVRSC FQFANNKPEI
EAALFLDWMR LEPQSMVWLP VLHRVAAAET AKHQAKCNIC KECPIIGFRY RSLKHFNYDI
CQSCFFSGRV AKGHKMHYPM VEYCTPTTSG EDVRDFAKVL KNKFRTKRYF AKHPRMGYLP
VQTVLEGDNM ETPVTLINFW PVDSAPASSP QLSHDDTHSR IEHYASRLAE MENSNGSYLN
DSISPNESID DEHLLIQHYC QSLNQDSPLS QPRSPAQILI SLESEERGEL ERILADLEEE
NRNLQAEYDR LKQQHDHKGL SPLPSPPEMM PTSPQSPRDA ELIAEAKLLR QHKGRLEARM
QILEDHNKQL ESQLHRLRQL LEQPQAEAKV NGTTVSSPST SLQRSDSSQP MLLRVVGSQT
SESMGEEDLL SPPQDTSTGL EEVMEQLNNS FPSSRGRNTP GKPMREDTM
//
