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Database: UniProt
Entry: W5MVZ5_LEPOC
LinkDB: W5MVZ5_LEPOC
Original site: W5MVZ5_LEPOC 
ID   W5MVZ5_LEPOC            Unreviewed;      3695 AA.
AC   W5MVZ5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
GN   Name=DMD {ECO:0000313|Ensembl:ENSLOCP00000012554.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012554.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000012554.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role in anchoring the cytoskeleton to the plasma
CC       membrane. {ECO:0000256|PIRNR:PIRNR002341}.
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|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR002341}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}. Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034109}.
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DR   EMBL; AHAT01003553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSLOCT00000012577.1; ENSLOCP00000012554.1; ENSLOCG00000010164.1.
DR   GeneTree; ENSGT00940000154342; -.
DR   HOGENOM; CLU_000246_2_0_1; -.
DR   Proteomes; UP000018468; Linkage group LG17.
DR   Bgee; ENSLOCG00000010164; Expressed in muscle tissue and 13 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:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
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; cd21233; CH_DMD_rpt2; 1.
DR   CDD; cd16246; EFh_DMD; 1.
DR   CDD; cd00176; SPEC; 13.
DR   CDD; cd00201; WW; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 1.20.58.60; -; 17.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
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; PF00307; CH; 2.
DR   Pfam; PF09068; EF-hand_2; 1.
DR   Pfam; PF09069; EF-hand_3; 1.
DR   Pfam; PF00435; Spectrin; 13.
DR   Pfam; PF00397; WW; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 21.
DR   SMART; SM00456; WW; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 19.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
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|ARBA:ARBA00023203,
KW   ECO:0000256|PIRNR:PIRNR002341}; Calcium {ECO:0000256|ARBA:ARBA00022837};
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|ARBA:ARBA00023212,
KW   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|ARBA:ARBA00023257,
KW   ECO:0000256|PIRNR:PIRNR002341};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
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          28..132
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          147..253
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          3065..3098
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          3318..3374
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          324..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3542..3563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3610..3695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          766..793
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1207..1312
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1927..1954
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2513..2557
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2932..2969
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3506..3540
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        3612..3683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3695 AA;  424590 MW;  CFFD7F3E73600E78 CRC64;
     MAEAGRPEEP VEDEFSGLIR TRTDEREDVQ KKTFTKWINS QFSKAGKPPI EDLFTDLRDG
     RRLLELLEGL AGHELAKEKG FTRVHALNNV NRALQILQKN NVELVNIGGA DIVDGNHKLT
     LGLIWSIILH WQVKDVMKNI MAGLQQTNSE KILLSWVRQS TRDYQQVNVV NFTNSWSDGL
     AFNALIHSHR PDLFEWSSVL KQQSAIEKLD HAFSTAKQHL GIERLLDPED VATPHPDKKS
     IIMYVTSLFQ VLPQQVTIEA IQEVETLPRH TKVTQEEHIQ IQHQHEQRYS QQITVSVAQG
     HVRTPSPSPK PRYKSYAYTQ AAYVQSPDQK RRRCTAQPAE APEDKSASSP LMEAEGHLDS
     YQSSLEEVLT WLLSAEDALQ SQGDISGDVE EVKEQFHTHE GFMMELTSHQ SSVGKVLQAG
     SQLLSEGRLS DDEENEVREQ MNLLNTRWEH LRVTSMERQS KLHEVLMDLQ HQQLKQLSDW
     LAVTESRVKK METQPLGPDL EDIKHQVEEH KLLQEDLEME QVRVNSLTHM VVVVDENSED
     GATAALEEKL QHLGERWADI CRWTEERWIL LQEILLKWQH FTEEQCLFDA WLMEKEEAVN
     KIQTSGFKEQ QEMVANLRKL AILKGDLEMK RQTMDKLCSL SQDLLSAVRN KDVAKKLEAR
     LENFAQRWDS LVQTLERSSS QISQTVTTAQ TALSASTVME TVTMVTTREQ ILVKHAKEEI
     PPPPPQKKRQ IVVDSELRKR FNVDTTELHS WMTRSEAVLQ NPEFSESRKE GNLSDLQERV
     NAIEREKPEK HRKLQDASRS AQALVEQMVN EGLKADDIKQ ASEQLNSRWV EFCQLLEDRL
     AWLAYHNKII AFYSHFQLLE QAVVAAENWL KSQQPLAPES ETVRVQLDKC KDEGSRLSAL
     QPQVEMLKER GKELNAKEEA PMFLEADITA FTDRYNQVLA DLQAREQHLK NILESLPPAR
     YRETVTSLLF WIQQSESRLV VPQFAVTEYQ AMEQRLKEIK ALQVSLQEQQ SGLNYLTSTM
     DELCQKAPVE ISQKYRLEIE AILLRWKRLS AQLGEQSQKL EELMTKLQQF QNDTKTLKKW
     MAEVDVFLNE EWPALGDSEA LEKQLEQCTA LVNDINTIQP SLNGINDVGQ TLRKEAEPAF
     ASKLQKEISD LNIQWDNVCK QAYAKKSALK GGLDKTVSLR KDLSEMQEWI TQAEEDFLER
     DFEYKTPEEL KKAVEELKRA KEEVQQKEVK VKLLTDSVNS FIAKAPPAAH EALKSELEVL
     TSNYQRLCSR LNGKCKTLEE VWACWCELLS YLEAENRWLD ELELKLRNTE NIQGGAEEIS
     EALDSLESSL RHPEDNRNQI RELAQTLTDG RVLDELINEK LETFNTRCEE LLQQAVRRQQ
     MLEQSIQSAQ ETDKALRLIQ ESLATIDRHL SAYIADHVDA GQIPQEAQKI QSELSSHEIS
     LDEMKKRNEG KALSERVQSQ INMTQKKLQE VSTKFRLFQK PANFDQRFLE CKTVLDEVKS
     QLPVLAMRSV EQDVVQSQLD QCMKFYKSLS EVKSEVETVI KTGRQIVQRQ QTESPKELDE
     RLTALKLQYN ELGAQVTEGK QELEKSLKLS RKLRKEVNAL TEWLAITDAE LTRRSSVEGM
     PTHLDAEVAW AKAIQKDTEK HLQQLKNISD LAEALKAVLH GKENLVDDKV SLLNCNWIAV
     TSRAEEWLNL LRDYQKQMEM FDQSIAQITA WIYRAEILLD ESEKQESQQE VLKGLKDELS
     DIRLKVETVQ GQAEDLIKNR GDHCRVVVEP KLSELNQRFE AISQRIKIGK AFVTPRELEL
     YHTEAQKWLE RLEAEVQEGD NLKEEDFQKD TEDNEEGAVK EFLEKGEKLH HRVPDEKKRE
     EIRIKLNLLH AKYNTVKDLR SLRKKKALAI SPQWYQYKKQ SHDLLQWLDD IEKRVASLPD
     PRDEERIKEI DAELEQKRED LNAVNRQAQS LSRDGAAKAV EPNLIQLNKR WQEIESKFAQ
     FRRQNFAQIH SVYEETRVVK TEGPAAESPH VPSTYLAELR QLLHSVAEIE FLLNSPEYWA
     GAYHDLVKQE DCLKDAKVSL TKLAGPVGNA QSRRSAVLQN ASPVEYSHIQ DSARQLDTNW
     EKVNKLYKDR QVRYEKSAEK WRRFHADMKS LTQWLSEAER TLAETGAGSG SQDHSKAKER
     LKELQNGIRH QQALVSSLNA TGEEIAQQST SEDAILFKER LTGVNVRWEE VCRQVAERRR
     RSEEEKHIIS ELQEDLNEFL SWLDKAESIV SLELESGDEH QLKDSLEKIK LRVEELPSRK
     KILKELNESG GHPHGSTALP SEEQRRLECD LKLANSRWTK VSRELPEKQK TTEALLKELV
     QFQQHLNQLA FWASTTKDQL ELYLKVGLPG AFDTKETEDS VQAKQADVEA ILSRGHQLYK
     DKPITQPIKV KLEDLSSDWK AIHILLTQFK GKPDPSAAVS CTTKIASIGQ TVTVVTQTLV
     TKETVVSKLE MPSSLLMEVP ALADFNKAWA ELTDWLSLLD HMIRTQIVTV GDLEEINDMI
     VKQKSTLQDL EQRRPQLENL ITAAQNLKNK TNNQEVRSII TDRIDKVQAQ WEEVQGALQG
     RRLQLQDMLK DSSQWLEAKQ EAAPLLQRAT ARLESWKDIS YTVEALKRQN ADLKQFVKEL
     RQWQINIDVA NDLARKLLRD YSADDTRKVN LVTEDMNNSW ANVNKKVGDR EAALEAALRL
     LQQFYVDLEK FLSWLTEAET TANVLQDATH KEGILEDPHV VRELMKQWQD LQAEIEAHTE
     TFHTLDDNGQ RILKSLEGSE DATLLQRRLD NMNVRWNELR KKSISIRSHL EASSEQWKRL
     HLSLQELLAW LQLKNDELAQ QKPIGGDVPT VQKQLDTHRA FRRELKAKDL VVSNALDAVR
     VFLAEQPAEG LARLQQEQRE VSPEERAQNI SRVLRKESED VRAGWEGLRG RAADWQRRLD
     GALERLLELQ EAADELELKL RQAEMVKQSW QPVGDLLIDS LQDHIEKVKA FRAEVAPIKE
     NVTQVNDLAS LFGPPDVQLS QFNLSRVEDL NTRWELLQVS IEERLKQLHE AHRDFGPTSQ
     HFLSTSVQGP WERAISPNKV PYYINHQTQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM
     KLRRLQKALC LDLLGLSAAC EAFEQHNLKQ NEQLMDIMQI INCLTTIYDR LEQEHNTLVN
     VPVCVDMCLN WLLNVYDTGR TGKIRVLSFK TGIVSLCKAH LEDKYRYLFK QVASPTGFCD
     QRRLGLLLHD SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPELEAAV FLDWMRLEPQ
     SMVWLPVLHR VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRIAKGH
     KMQYPMVEYC TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV
     TLINFWPVDY APTSSPQLSH DDTHSRIEHY ASRLAEMENR NGSYLNDSIS PNESIDDEHL
     LIQHYCQSLN QESPLSQPRS PAQILISLEG EERGELEKVL SDLEEENKSL QAEYDRLKQA
     HDHKGLSPLP SPPEMLPVSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL
     HRLRQLLEQP QAEAKVNGTT VSSPSTSSQR SDSSQPMLVR VVGSQTTDTM GEDDLLSPSQ
     DPSTGLEEVM EQLNNSFPTN QGRSGPGKPV REVTM
//
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