ID A0A0V0U9X5_9BILA Unreviewed; 3023 AA.
AC A0A0V0U9X5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dystrophin {ECO:0000313|EMBL:KRX47571.1};
GN Name=DMD {ECO:0000313|EMBL:KRX47571.1};
GN ORFNames=T05_4338 {ECO:0000313|EMBL:KRX47571.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47571.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX47571.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX47571.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX47571.1}.
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DR EMBL; JYDJ01000041; KRX47571.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:UniProt.
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 GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
DR CDD; cd16242; EFh_DMD_like; 1.
DR CDD; cd00176; SPEC; 3.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 9.
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:SF14; DYSTROPHIN-1; 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; 9.
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; 9.
DR SUPFAM; SSF51045; WW domain; 1.
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 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:UP000055048};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 2382..2415
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 2612..2668
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2849..2882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 62..114
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 868..905
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1027..1086
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1237..1271
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1593..1662
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2797..2831
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2895..2943
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3023 AA; 347468 MW; F317F5ED3F268634 CRC64;
MNERHELCIA VVVNDILTMF RVVAEEVVNL IAITASDIAC LVNKAAARAE DPFHCLLLAT
QRRNSSENYN AKEEEEEEEN SQARRMFLAA SKHLRQLDKE EKTVSSEAKQ QQRRISLPAH
KQSLAQFQHH LTDEESNRLR DIYDLQGCSH ATEDDGSCAD SDRKNSAEAG AANDRLSRIR
SGQVTWSTIS SNITLNLNVL LTDVEKMSAP DLREMLSSLN EWLEYATCFI KFQFAESRVS
SKEALDNLKE KVQFLKKFES AVKRLLHVVE CLLQDGSVDS HIKMTYESVS NQFDRTPAPH
LEQALQSLSE WLDCAEDVIA TQDLDSIDEL DITAAKIQRL QDLQNEMTVQ RENLNFVANA
ADELLREGTG AYDKLSKKLR SVVPRWTDIE RVLTNQLTRL KAGMSKLQDW EFRASELENW
MLQVKEFIQA EKPALGNTET LKAQLEQSQA LMNDIETLVP KIQQMETWVH ELELNCKPRV
GEYLRARMED IDSRWTDVVR VTEAKHESLN KAYTQSKVIF DEVQQLTQWL WSVEQEMQTF
GNPSSGKELH TMIKQHKQIL DELRSKAEIV EHAALMGEQI VEAANEASDA SLQLKRRFLN
TREQWSAICQ QMEARLSVLT DAFELWKEFQ ELVAAEKISL DRLEQMLNEP MKSATDAEEF
SEQLDEFERL MEGSGGHNRI IEIANTLNNE NFLSNAVRNE LAKYMAKRDK VLEPAKERQK
FLETDAREAQ KIEQQLHECL SWISRVDFIT RARSECDILA SDIPQEYKML FSRGELLLKL
YDEFDEHKEC IFDLEKQVAQ YQQLGLQQAA GRLAEQVNHL KKQMCDVQSR LEQYKQPSEL
DDRLRRVERI LEDLEQSFTL LTVATDDLDE IDQLLEKVEV TLEALNELQC EIDDLKDTAS
KQNARSSIAL DDIDDVENHL KAFYSKISET KENFQEIRRM LATASTNLQN CNELLNEMET
NLRKWDPEDP QNFDERCKRC LNYRREISNC NQYLKEMESY VKKFMHLTQG QSTSKLDGIL
LVFRNRIKNL TNKLDEWSMD YQHSKLEQVE AQKKFYNLHA AVSSMLNTAE KEITSSNRDL
KVLKEELATR SSSTSESDDQ ASISLSMLFG KDGNNGDNDE SNDVSMISED TIRVGSSTPI
ASESSDFTDR LLVQTTELAK SINSVEELLG ASEQDFKMLQ SKIGDVSNTI EACSTNVNQL
LHQSEQANKI ELRPNVLSIV NKLEHMDSKL KLLDGKIKSI IEANERFQQR YDTLNNNAKN
LLSNLVFLET MNTDEVKNCQ EGLTNVENSL TDLLVTTKEE FQHLDVAFPE SSADSLYKLL
QQAQSNITVH VKQLEEKANA KAKMDAFIVE SAKVKEECSK LERKLSLCPE SENFSFTGLT
ERETEFQDLT ENVEQLKDRI GKLWNLHDNV SHQYLDESEQ ANVKQIVDEL NIHLDSLEKT
YMEHFSLFQA ALQQWQSLHQ RLYSVMAWLE HVENRLIPSI SINDPEATKI TDSVMNDINN
SCKEIENITQ ALVDMQDKYS NCLSSTDVSL LKDKLEKATY RLNSLKTKMI ENRNRVKHYD
LELKEEIEEL LFWFDESDTL FSTLCDPTDA KQLADFKQRI EEKKSETVTK EQQLESLSSA
VDNIDTDKGI SEAVIIDLKE NVDSLKQRLV QVKEDVDQKL QLYDQKINQC NQFWDQLRQM
SIWAQNMKNL LLEYKSATIY TPARFDPDAL DAEIKSKKEE IEDFIASYNA IREEAELSDV
KLCSSTEHAV KQLYNSWAGI LRMTELFESS SRSTSEEDED SSTAPEIQRL TSTDAPISPM
LNAGKNLQEL IRWSHWLSDM TLESVVFCKL HDSSEIRAAM KKKQSFLSQL NANEKHVLKI
LETDQNVDVL FKAELLHKEW KKRITEVERR RIELVEMLEN CRTWDDLRVE IEIFLSSTEK
KISSAKVSDV PIDKLQRELV ALEQLATEMD IYRKKMTDFN EISNFIVESY VHDDASTLSQ
ITSNMNTLWS KINDNLRIRK AVLEASCRGR KDFFTALQEF SCWLGKIESQ VLSLDADSSL
AQLLKDVAYR QELRDKWKGV SGEIEVHETV FHSLCDTAKT LLMNSMFSEE KSDFQGELMQ
LNERWEQVVK LSDEIKQRLD LAQEQWERLT TQLQELICWT EDASRELLRQ QPIAGDSEKI
KLQNEFIQQL QTGISNQEKA VKEIIQIARS YLLQQDLRPA LQSSMDSDET EEMLVGKKQS
RRVGQMIKND SDRLEELWAD LTDSANDWQK LVEDTFTKMI LFDKAIEDCK IAISEAEDLK
KHWKPISDVK LDELAECMEH ARGFHQYLIC HIRLLLDDVN DHSSRLLADN VRLSPVMIHS
LESLNLRYKE LELTIGDRIV ILQNALRQFG PSSQHFLEGD AGSVVLPWER AVSTNRIPYY
INHETEKTQW DHPKMVEIIN SFMDLISIED LVDIFNQRKL QDANDNQLDV SEMVMTLLPI
YELVQRDNMN LLRSIPLAVD LCLNWLLNVY DPARTGNTRV ISFKVALILM CRASLSEKYR
YLFNQVSYNK CSLDQKKLAL LLHECIQVPK FFGEVAAFGG TNIEPSVRSC FEMAKYPAEV
TMQQCMDWLN CEPQSIVWLA AMHRISISEN EKHQAKCNVC KMFPIVGLRY RCLKCFNFDM
CQNCFFAQRT AKNHKISHPM QEYYKAAKSG EDVRDFGRVI RNRFKSKHYW KKHPRLGYLP
VQSVMEGHSL ESRDLVPTNP ETQNIHVQIE LYASHLADME RSAITESNES EDDEHAVISS
LSSTLTNDCH VKQHPVNMAG AVRSPAQIMS VTDSAQKVEL NGLLKHLQNE NKNLMCEYEK
LRNKMSAEVD KSAASLHNSL STPMLPMTNG SLGRRGQHRS TSSLSRTHHQ RIAPPAAYDD
PAMDLDMDTI LSEEKEIIAN EAKALRQQKQ RLEQRSKVLE EHNQQLEVQL RRIKQLIEEQ
KQNGITCIDS SKSQLMLSSG ISSQADAMTH CGNDDSLVLS DTCSSSSNRI GDLMSTVQDI
GKAVGNLINA VTSDDEVSMA EVE
//
