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Database: UniProt
Entry: A0A3P9PJB1_POERE
LinkDB: A0A3P9PJB1_POERE
Original site: A0A3P9PJB1_POERE 
ID   A0A3P9PJB1_POERE        Unreviewed;       940 AA.
AC   A0A3P9PJB1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000021952.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000021952.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000021952.1};
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   AlphaFoldDB; A0A3P9PJB1; -.
DR   Ensembl; ENSPRET00000022183.1; ENSPREP00000021952.1; ENSPREG00000014502.1.
DR   GeneTree; ENSGT00940000154342; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000014502; Expressed in head and 1 other cell type or tissue.
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; 1.
DR   CDD; cd00201; WW; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 1.20.58.60; -; 2.
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; 1.
DR   Pfam; PF00397; WW; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00150; SPEC; 2.
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; 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000242638};
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          322..355
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          575..631
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          785..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          9..104
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          192..229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          684..711
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          750..784
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          823..857
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        858..920
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   940 AA;  108049 MW;  208D23A0CCE6AC39 CRC64;
     MLRRKVYQVQ DLQAEVDGHE ELYHSLDENG QRILTSLRDP EDRVLLQRRL DNMRQRWNDL
     RRKSVCLFGR SQLDSEMAPW KRLHMSLQEL LNWLRLKSQQ LEQEKPVGGD VPTVQSQLDT
     HRGFKMELRA KDPVVTKALD DAGFFLSELP REPGLSQTSD ISPEERAQNV GRVLRKEADD
     VVSRWDRLNV DSADWQRRLE LALDRLMELQ EAEDLLDKQL KQAEMVKQGW EPVGELLIDS
     LPEHISRVKE FQEEIALIKD DVTHMNHLAS TFDPSDIQLS PSNLERIEDL NTRWRLLQVC
     TLKHSHTHTP THTPAPTHTH TRSVERPFEQ GISPNNVPYY INHQTQTTCW DHPKMTELYQ
     SLSDLNNVRF SAYRTAMKLR RLQKALCLDL LSMQTACEVF EQHTLKQNEQ LLDISQLMTC
     LTSLYQRLEQ SHSHLVNVQL SVDMCLNWLL NVYDTGRTGK IRTLSFKTGI ISLCKAHLED
     KYRFLFRQVA SATGFCDQRR LGLLLHDSIQ IPRQLGEVAS FGGSNIEPSV RSCFQFANNK
     PELEASMFLD WMRLEPQSMV WLPVLHRVAA AETAKHQAKC NICKECPIIG FRYRSLKHFN
     YDICQSCFFS GRVAKGHKMQ YPMVEYCTPT TSGEDVRDFA KVLKNKFRTK RYFAKHPRMG
     YLPVQTILEG DNMETPGSSP QLSHDDTHSR IEHYANRLAE MENRNGSYLN DSISPNESID
     DEHMLIQHYC QSLNQGSPLS QPRSPAQILI SMETEEKGEL ERVLGDLEQE NRSLQAEYDR
     LKKAHDRKGL SPLPSPPEML PVSPQSARDA ELIAEAKLLR QHKGRLEARM QILEDHNKQL
     ESQLHRLRQL LEQTDSKVNG TALSSPSTSS QRSDSSLPLL RVAASQTTDT MGDDEFSSPS
     QDASGLEEVV EQLNNTFPHS QGKKTRKDSL LANVQLFDST
//
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