ID A0A2K6BBD6_MACNE Unreviewed; 634 AA.
AC A0A2K6BBD6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Dystrophin {ECO:0000313|Ensembl:ENSMNEP00000008728.1};
GN Name=DMD {ECO:0000313|Ensembl:ENSMNEP00000008728.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000008728.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000008728.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR AlphaFoldDB; A0A2K6BBD6; -.
DR Ensembl; ENSMNET00000032898.1; ENSMNEP00000008728.1; ENSMNEG00000027978.1.
DR GeneTree; ENSGT00940000154342; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000027978; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16246; EFh_DMD; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
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; PF00569; ZZ; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 239..295
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 459..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 500..534
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 634 AA; 72013 MW; DA870FE393B6C3FF CRC64;
VRENLNCTTQ TTCWDHPKMT ELYQSLADLN NVRFSAYRTA MKLRRLQKAL CLDLLSLSAA
CDALDQHNLK QNDQPMDILQ IINCLTTIYD RLEQEHNNLV NVPLCVDMCL NWLLNVYDTG
RTGRIRVLSF KTGIISLCKA HLEDKYRYLF KQVSSSTGFC DQRRLGLLLH DSIQIPRQLG
EVASFGGSNI EPSVRSCFQF ANNKPEIEAA LFLDWMRLEP QSMVWLPVLH RVAAAETAKH
QAKCNICKEC PIIGFRYRSL KHFNYDICQS CFFSGRVAKG HKMHYPMVEY CTPTTSGEDV
RDFAKVLKNK FRTKRYFAKH PRMGYLPVQT VLEGDNMETP VTLINFWPVD SAPASSPQLS
HDDTHSRIEH YASRLAEMEN SNGSYLNDSI SPNESIDDEH LLIQHYCQSL NQDSPLSQPR
SPAQILISLE SEERGELERI LADLEEENRN LQAEYDRLKQ QHEHKGLSPL PSPPEMMPTS
PQSPRDAELI AEAKLLRQHK GRLEARMQIL EDHNKQLESQ LHRLRQLLEQ PQAEAKVNGT
TVSSPSTSLQ RSDSSQPMLL RVVGSQTSDS MGEEDVLSPP QDTSTGLEEV MEQLNNSFPS
SRGHNVGSLF HMADDLGRAM ESLVSVMTDE EGAE
//
