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Database: UniProt
Entry: A0A3B3TEZ0_9TELE
LinkDB: A0A3B3TEZ0_9TELE
Original site: A0A3B3TEZ0_9TELE 
ID   A0A3B3TEZ0_9TELE        Unreviewed;      3420 AA.
AC   A0A3B3TEZ0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Dystrophin {ECO:0000256|ARBA:ARBA00040142};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000041857.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000041857.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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|PIRNR:PIRNR002341}. Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034100}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034109}.
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DR   STRING; 1676925.ENSPKIP00000041857; -.
DR   Ensembl; ENSPKIT00000022899.1; ENSPKIP00000041857.1; ENSPKIG00000017543.1.
DR   GeneTree; ENSGT00940000154342; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd00176; SPEC; 9.
DR   CDD; cd00201; WW; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 1.20.58.60; -; 14.
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; 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; PF09068; EF-hand_2; 1.
DR   Pfam; PF09069; EF-hand_3; 1.
DR   Pfam; PF00435; Spectrin; 14.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR   SMART; SM00150; SPEC; 21.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 17.
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   Actin-binding {ECO:0000256|PIRNR:PIRNR002341};
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|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|PIRNR:PIRNR002341};
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          2763..2796
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          3016..3072
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          134..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3239..3261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3313..3334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3401..3420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          454..488
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          850..880
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1017..1044
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1539..1566
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2232..2266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2318..2365
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2651..2688
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3277..3311
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        146..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3420 AA;  393733 MW;  BBFC52AD86706678 CRC64;
     MLYRSRKLCK FNIVLHLCKE TDFVYFLKYI KNKYSSLSSV SDVATTHPDK KSILMYVTSL
     FQVLPHGVTM EALREVERLP PAPMALEDHV QSKQRFSQQI TVNVAQGWVR SPSPTAKPRY
     KSYAYTQAAY VKSPEQKRRR FTSQSPDSQG EEASSSPNPH RDLQLERYQT ALEEVLTWLL
     SAEDSLQSQS PISNQVEVVK EQFHTHEGYM VELTSHQGSV GRVLQSGSML LAEGRLTEEE
     ENEIREQMNL LNSRWEHLRV ASMERQSRLH EVLMDLQNQQ LKQLTDWLEL TEGRINRMEA
     QPLGPDLVDI KHQVEEHKLL QEDLEMEQVR VNSLTHMVVV VDESNGDSAT AALEEKLQHL
     GDRWAAICKW TEERWVLLQE ILLKWQQFTE EQCSFDTWLV EKEEFVHTIQ CSGLKEQSGM
     VESLRKLAIV KGELEAKRQT MDRLCSLSQD LLSSVKNKDL ARKLEARLEN LTQRWESLLQ
     KLEKSSSQIS MSVTTAQTEL MKTTVMSSVT KVTTRGQVVV THTKEEVAPP LPQKKRQIVV
     DSELRKRFDV DFTELHSFMT RSEAILQSPE FSFSRKEGSV SELQEKVLAI EREKPEKMRK
     LLEATRSAQA VVDQLASEGL KADDIKQAAD QLNSRWVEFC ALLDERLAWL AYQTKVLAFY
     NQFQQLEQAV VTAENWLKVQ QPPASELEPL RIQVDRCKDE VARLSALQPQ VNQLKEQVKD
     LREKEEAPVF FDADIKALTD HYKQVLADLQ ARLSQLQLIQ DSLPPVRYRD TATSLFAWLQ
     QCEAQLPVPS TAVNEYPIME QRLKDMKALQ VSLQEHQSSL DYLTVTVEQV CQKAPYEISQ
     KYRMELDAIM MRWKRMSTQL EEQIQRLQEL MAKLQQFQND TKTLRKWMVE VDVFLNEEWP
     ALGDSEALEK QLEQCTALVN DINTIQPSVN GINEVGHALK KEAEPVFASK LQEEITQLNA
     QWENICKQAY AKKSALKGGL DKTVSLRKDL SEMQEWITQA EEEFLERDFQ YKTPEELRKG
     VEEIKRAQEE VHQKEVKVKM LTDSVNSFIA KAPPVAHEAL KTELNILTTN YQRLCSRLDG
     KCKTLEEVWS CWCELLSYLG LENGWLDQLE NKLNETESIH GGAEEISEAL DSLESLLRHP
     EDNRNQIREL AQTLMDGGVL DELINQKLEA FNTRWDELME RAAQRQKCLE MSIQSAQEHD
     KALRLIQESL HTTDRHLSAY IADHLDAGQL PQEAQKIQTE LNSHELSLDE MRKKNANKDP
     SDRVYSQIDI TQKKLQEVIK KFRLFQKPAN FDERLQVCER VLDEVKTQLG VLGVRSVDQE
     VVQSQLDQCM RFYKSLSEVK AEVETVIKTG RQIVQRQQTE NPKDLDERLT ALKLLYNELG
     AQVTESKQEL EKSLKLSRKL RKEVNSLTEW LAVTDAELTR RSDVDGMPDS LGAEVAWAKA
     KQKETEQHEQ QLKGVAELAD ALKAVLQGQE SLVEDKVSLL KCNWIAVTSR SEEWLHLLLD
     YQSQVDTLDQ NISQINAWMH RSETLLDESE PLGTKDHVIK GLRVELEDMR AKLEAVQSQA
     QEMMKNQGEH CRALVEPKLD QLNQRFEAIA RRIRTSQVTA SEREVEQYHS EAMIWLRLLD
     EEVRQGDNLK EEDFEQDRDC EEGAVKELLE KGEKLQKRVP DENKRKEIRI RHDQLNTKYN
     TVKDLRSLRK KKALAIAPQW YQYRRKSDDL LQWLDDIERS MAELTDPPEE QRVKVWRAEE
     RPHRPALSDL QVQAKVLADG GAAQLVDPRL AQLNKRWGEV QSTFAPYHHS KDKTLFVFLL
     GDSNILKILL QHSYLCELQE LLHSIANTEF QLNSPEYWAG VFYELPKQEK CLQVGSSVLE
     KLGTPVVRAQ GRKEEILRKA SPVEAQRIQD TLLLLSTNWE KVNKLYCDRL AYLSQDKLQH
     FNKNLKALSE WLGDAERSLA QAERQPVQRR EHLKELQDAA SAQESAMIAL NTTGQDIILQ
     SSQEEGARLK EQLGSMNKRW EEVCRQFAQW KRRSAEMHNT VSDLQEDLSE FLSWLDDAEN
     VAAIAPHPGD QQQLSSLLEK VQARVQEVPN RKLNLKELND RGCSVHALLC RLNLPYQVSR
     DLPEKQQQIE GLLKDLSQFH LELSQLSQWA AGFKDQLELS RQAADNKFSV PNLSLCAFPP
     FLQVKFEGLS TDWRIIQDLL KEMKMKSQPT TTVIRETIPA LVQFNKTLSE LTNWLSVLDH
     MTQTQRVMVG NLEEINDMMK KQKATLQDLE QRRPQMESQI TAAQNLKNKT NNQEARVTIT
     DRIDRLQTQF EEVHGRLSDR ALELQRMLKD SSHWLKAKQE VESLLKRANE KLESWKELSY
     TVDALKNQNA DLKHFVKELH QWQRQVDETN DLARKLLVQY AADDTHRVSM LTDSMNSTWS
     HVTKQVGERE AALEAALRLL QQFYLDLEKF LNWLAEAETT ANVLQDATHK EGMQEDPSAG
     RQLLRQWQDL QTEIEAHTEA FHTLDENGQR IMRSLEGSED AALLQRRLDN MDQRWNELRS
     KSLSIRSHLD AGTGQWKCLH LSLQELLTWL QQKNEELDHM APTGGDIPMV QQQLEAHRAF
     RIEVKAKEPA VSGALNAVGA FLADQHTETS LLGRVASAEV SPEERAQNMS RVLRKEAEDV
     RSGWERLRSR SVSWQRRLDQ ALEHLQELQE AEDKLDLKLR QAEMVKQSWE PVGDLLIDSL
     QEHIDRVTAF QAEVAPIKDD LTQVNCFAST FCPMNIQLSE YNINRLEDLN TRWRLLQVHN
     RHASVQHPFE RSVSPNNVPY YINHQAQTTC WDHPKMAELY QSLADLNNVR FSAYRTAMKL
     RRLQKALCLD LLGMSAACEA FDQHNLKQNE QLLDIMQIIN CLTSIYNRLE QQHSNLVNVP
     LCVDMCLNWL LNVYDTGRTG KIRALSFKTG IISLCKAHLE DKYRFLFRQV ASATGFCDQR
     HLGLLLHDSI QIPRQLGEVA SFGGSNIEPS VRSCFQFANN KPELEAAVFL DWMRLEPQSM
     VWLPVLHRVA AAETAKHQAK CNICKECPII GFRYRSLKHF NYDICQSCFF SGRVAKGHKM
     QYPMVEYCTP TTSGEDVRDF AKVLKNKFRT KRYFAKHPRM GYLPVQTVLE GDNIETPVTL
     INFWPVDYAP TSSPQLSHDD THSRIEHYAS RLAEMETRNG TCISDGISPN ESIDDEHLLI
     QHYCQSLNQE SPLSQPRSPA QILISLETEE RGELERVLSD LEEENRNLQA EYDRLKQAHD
     RKGLSPLPSP PEMLPVSPQS PRDAELIAEA KLLRQHKGRL EARMQILEDH NKQLESQLQR
     LRQLLEQVDT KLNGTTALSS PSTSSQRSDS SLPHLRVVAS QTTETMGDDE LSSPSQDTST
     GLEEVMEQLN NSFPHTQGHA VGSLFHMADD LSRAMESLVS VMTAEQGQEE RRAPPPSMLL
//
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