ID A0A3Q0THR5_AMPCI Unreviewed; 1168 AA.
AC A0A3Q0THR5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000031582.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000031582.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR Ensembl; ENSACIT00000032410.1; ENSACIP00000031582.1; ENSACIG00000024399.1.
DR GeneTree; ENSGT00940000154342; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00176; SPEC; 3.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 5.
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; 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; 2.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 5.
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; 4.
DR SUPFAM; SSF51045; WW domain; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 564..597
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 817..873
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 1036..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 145..175
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 430..467
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 939..966
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1078..1112
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1116..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 134096 MW; 4A359F41128E0786 CRC64;
QPSSLPEYTA LAQFNKSWAE LIEWLTTLDN MVQNKRVVVA DLDDISNNIR QLKASLQDLD
QRRPLLENQI TAAQNLKNKT SSQETLDKLQ AYWEDSQTKL SDRMKQLHNM LQDSTNWLDA
KKGVDHLIKQ ANERLDSWQE ITYTVETLKK QNAELKLLMK ELQQSQIQVE ETNALANKLL
TLYTNDDTHK VTQINNNMEA TCAHINKRVS DREAALEAGL KLLQQFYLDL EKFLNWLTEA
ETTCNVLIDA TTKERMQEQP EAARNLLAQW KDLQTEIDSH TELYHSLDES GQRVLTSLGD
SEDGVLLRRR LGNMTQRWND LCNKTLSMRA HLDSEMAPWK RVHMSLQELL NWLRLKSQQL
EQEPPVGGDV PAVQAQLDIH RVGGHALQTT LVPDYQQLFL PEEXAHNVGR ILRKEADDMI
SKWDRLNADS ADWQRRLELA LDKLMELQKA EDLLDGQLRQ AEMVKDAWEP VGDILIDSLP
DHIDRVKEFQ EEIAPIKDDV THMNQLASTF NLSDIQLSSR NLERIEDLNT RWSLLQVLTN
AHIHTLPQIE IIINISWFSS VSAGSVESPF EQGISPNNVP YYINHQTQTT CWDHPKMAEL
YQSLADLNNV RFSAYRTAMK LRRLQKALCL DLLSMPTACE VFDQHSLKQN EQLLDISQLV
TCLTSLYQRL EQSHSHLVNV PLCVDMCLNW LLNVYDTGRT GKIRTLSFKT GIISLCKAHL
EDKYRFLFRQ VASATGFCDQ RRLGLLLHDS IQIPRQLGEV ASFGGSNIEP SVRSCFQFAN
NKPELEASVF LDWMRLEPQS MVWLPVLHRV AAAETAKHQA KCNICKECPI IGFRYRSLKH
FNYDICQSCF FSGRVAKGHK MQYPMVEYCT PTTSGEDVRD FAKVLKNKFR TKRYFAKHPR
MGYLPVQTIL EGDNMETPVT LINFWPVDHA PGSSPQLSHD DTHTRIEHYA NRLAEMENRN
GSYLNDSISP NESIDDEHML IQHYCQSLNQ GSPLSQPRSP AQILISMETE EKGELERVLN
DLEQENRSLQ AEYDRLKKAH DRKGLSPLPS PPEMLPVSPQ SARDAELIAE AKLLRQHKGR
LEARMQILED HNKQLESQLH RLRQLLEQVY TTNGSSSTHL QMSVSPLSDD ELSSPSQDVI
GLEEVMEQLN NTFPHSQARR EKGTPMRG
//
