ID A0A0V1LRF8_9BILA Unreviewed; 3131 AA.
AC A0A0V1LRF8;
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:KRZ62067.1};
GN Name=Dmd {ECO:0000313|EMBL:KRZ62067.1};
GN ORFNames=T02_2292 {ECO:0000313|EMBL:KRZ62067.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ62067.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ62067.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ62067.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ62067.1}.
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DR EMBL; JYDW01000012; KRZ62067.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1LRF8; -.
DR Proteomes; UP000054721; 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; -; 8.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 6.10.140.70; -; 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:UP000054721};
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 2465..2498
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 2720..2776
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 2957..2990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 838..875
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 997..1056
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1260..1294
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1616..1685
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2905..2939
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3003..3051
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3131 AA; 359467 MW; 799BDCE460A5007E CRC64;
MYDEFLLLGS LIAITASDIA CLVNKAAARA EDPFHCLLLA TQRRNSSENY NGMFLAASKH
LRQLDKEEKT VSSEAKQQQR RISLPAHKQS LAQFQHHLTD EESNRLRDIY DLQGCSHATE
DDGSCADSDR KNSAEAGAAN DRLSRIRSGQ VTWSTISSNI TLNLNVLLTD VEKMSAPDLR
EMLSSLNEWL EYATCFIKFQ FAESRVSSKE ALDNLKEKVQ FLKKFESAVK RLLHVVECLL
QDGSVDSHIS AIQMTYESVS 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 KVLKIQLALL NSHQHQLHSC LEAAAGAIAK
DADRLHIIED DSGHLRRRWD SFMEKLKEEL ATRSSSTSES DDQASISLSM LFGKDGNNGD
NDESNDVSMI SEDTIRVGSS TPVASESSDF TDRLLVQTTE LAKSINSVEE LLGASEQDFK
MLQSKIGDVS NTIEACSTNV NQLLHQSEQA NKIELRPNVL SIVNKLEHMD SKLKLLDGKI
KSIIEANERF QQRYDTLNNN AKNLLSNLVF LETMNTDEVK NCQEGLTNVE NSLTDLLVTT
KEEFQHLDVA FPESSADSLY KLLQQAQSNI TVHVKQLEEK ANAKAKMDAF IVESAKVKEE
CSKLERKLSL CPESENFSFT GLTERETEFQ DLTENVEQLK DRIGKLWNLH DNVSHQYLDE
SEQANVKQIV DELNIHLDSL EKTYMEHFSL FQAALQQWQS LHQRLYSVMA WLEHVENRLI
PSISINDPEA TKITDSVMND INNSCKEIEN ITQALVDMQD KYSNCLSSTD VSLLKEKLEK
ATYRLNSLKT KMIENRNRVK HYDLELKEEI EELLFWFDES DTLFSTLCDP TDAKQLADFK
QRIEEKKSET VTKEQQLESL SSAVDNIDTD KGISEAVIID LKENVDSLKQ RLVQVKEDVD
QKLQLYDQKI NQCNQFWDQL RQMSIWAQNM KNLLLEYKSA TIYTPARFDP DALDAEIKSK
KEEIEDFIAS YNAIREEAEL SDVKLCSSTE HAVKQLYNSW AGILRMTELF ESSSRSTSEE
DEVKESEAER AFALLEKSSR SLELESARLN NEVRLENDDI IVPSLSEQES IGTSDIADAV
AAVQQDSSTA PEIQRLTSTD APISPMLNAG KNLQELIRWS HWLSDMTLES VVFCKLHDSS
EIRAAMKKEQ SFLSQLNANE KHVLKILETD QNVDVLFKAE LLHKEWKKRI TEVERRRIEL
VEMLENCRTW DDLRVEIEIF LSSTEKKISS AKVSDVPIDK LQRELVALEQ LATEMDIYRK
KMTDFNEISN FIVESYVHDD ASTLSQITSN MNTLWSKIND NLRIRKAVLE ASCRGRKDFF
TALQEFSCWL GKIESQVLSL DADSSLAQLL KDVAYRQELR DKWKGVSGEI EVHETVFHSL
CDTAKTLLMN SMFSEEKSDF QGELMQLNER WEQVVKLSDE IKQRLDLAQE QWERLTTQLQ
ELICWTEDAS RELLRQQPIA GDSEKIKLQN EFIQQLQTGI SNQEKAVKEI IQIARSYLLQ
QDLRPALQSS MDSDETEEML VGKKQSRRVG QMIKNDSDRL EELWADLTDS ANDWQKLVED
TFTKMILFDK AIEDCKIAIS EAEDLKKHWK PISDVKLDEL AECMEHARGF HQYLICHIRL
LLDDVNDHSS RLLADNVRLS PVMIHSLESL NLRYKELELT IGDRIVILQN ALRQFGPSSQ
HFLEGSVVLP WERAVSTNRI PYYINHETEK TQWDHPKMVE IINSFSEFNE VKFSAYRTAM
KLRSLQKNLY LDLISIEDLV DIFNQRKLQD ANDNQLDVSE MVMTLLPIYE LVQRDNMNLL
RSIPLAVDLC LNWLLNVYDP ARTGNTRVIS FKVALILMCR ASLSEKYRYL FNQVSYNKCS
LDQKKLALLL HECIQVPKFF GEVAAFGGTN IEPSVRSCFE MAKYPAEVTM QQCMDWLNCE
PQSIVWLAAM HRISISENEK HQAKCNVCKM FPIVGLRYRC LKCFNFDMCQ NCFFAQRTAK
NHKISHPMQE YYKAAKSGED VRDFGRVIRN RFKSKHYWKK HPRLGYLPVQ SVMEGHSLES
RDLVPTNPET QNIHVQIELY ASHLADMERS AITESNESED DEHAVISSLS STLTNDCHVK
QHPVNMAGAV RSPAQIMSVT DSAQKVELNG LLKHLQNENK NLMCEYEKLR NKMSAEVDKS
AASLHNSLST PMLPMTNGSL GRRGQHRSTS SLSRTHHQRI APPAAYDDPA MDLDMDTILS
EEKEIIANEA KALRQQKQRL EQRSKVLEEH NQQLEVQLRR IKQLIEEQKQ NGITCIDSSK
SQLMLSSGIS SQADAMTHCG NDDSLVLSDT CSSSSNRIGD LMSTVQDIGK AVGNLINAVT
SDDEVSMAEV E
//
