ID A0A3Q7SR69_VULVU Unreviewed; 622 AA.
AC A0A3Q7SR69;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dystrophin isoform X3 {ECO:0000313|RefSeq:XP_025853202.1};
GN Name=DMD {ECO:0000313|RefSeq:XP_025853202.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025853202.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025853202.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025853202.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025853202.1};
RG RefSeq;
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}.
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DR RefSeq; XP_025853202.1; XM_025997417.1.
DR AlphaFoldDB; A0A3Q7SR69; -.
DR STRING; 9627.ENSVVUP00000010332; -.
DR Proteomes; UP000286640; Unplaced.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 240..296
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 447..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 70755 MW; F73BF0D54693A684 CRC64;
MREQLKGHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA
ACDALDQHNL KQNDQPMDIL QVINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT
GRTGRIRVLS FKTGIISLCK AHLEDKYRYL FKQVASSTGF CDQRRLGLLL HDSIQIPRQL
GEVASFGGSN IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE PQSMVWLPVL HRVAAAETAK
HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE YCTPTTSGED
VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET PASSPQLSHD DTHSRIEHYA
SRLAEMENSN GSYLNDSISP NESIDDEHLL IQHYCQSLNQ DSPLSQPRSP AQILISLESE
ERGELERILA DLEEENRNLQ AEYDRLKQQH EHKGLSPLPS PPEMMPTSPQ SPRDAELIAE
AKLLRQHKGR LEARMQILED HNKQLESQLH RLRQLLEQPQ AEAKVNGTTV SSPSTSLQRS
DSSQPMLLRV VGSQTSESMG EEDLLSPPQD TSTGLEEVME QLNHSFPSSR GHNVGSLFHL
ADDLGRAMES LVSVMTDEEG AE
//
