ID A0A0V1NGJ8_9BILA Unreviewed; 2779 AA.
AC A0A0V1NGJ8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dystrophin {ECO:0000313|EMBL:KRZ83106.1};
GN Name=Dmd {ECO:0000313|EMBL:KRZ83106.1};
GN ORFNames=T08_3703 {ECO:0000313|EMBL:KRZ83106.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ83106.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ83106.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ83106.1};
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:KRZ83106.1}.
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DR EMBL; JYDM01000229; KRZ83106.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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; 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; 8.
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; 7.
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:UP000054924};
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 2138..2171
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 2368..2424
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 2605..2638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 508..545
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 667..726
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 930..964
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1286..1355
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2553..2587
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2651..2699
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2779 AA; 319108 MW; 85EEF2745F8FF5BC CRC64;
MLSKSCVAIT SSAQSSHSLN DCKACSKCGA EMTYESVSNQ FDRTPAPHLE QALQSLSEWL
DCAEDVIATQ DLDSIDELDI TAAKIQRLQD LQNEMTVQRE NLNFVANAAD ELLREGTGAY
DKLSKKLRSV VPRWTDIERV LTNQLTRLKA GMSKLQDWEF RASELENWML QVKEFIQAEK
PALGNTETLK AQLEQSQALM NDIETLVPKI QQMETWVHEL ELNCKPRVGE YLRARMEDID
SRWTDVVRVT EAKHESLNKA YTQSKVIFDE VQQLTQWLWS VEQEMQTFGN PSSGKELHTM
IKQHKEFERL MEGSGGHNRI IEIANTLNNE NFLSNAVRNE LAKYMAKRDK VLEPAKERQK
FLETDAREAQ KIEQQLHECL SWISRVDFIT RARSECDILA SDIPQEYKML FSRGELLLKL
YDEFDEHKEC IFDLEKQVAQ YQQLGLQQAA GRLAEQVNHL KKQMCDVQSR LEQYKQPSEL
DDRLRRVERI LQDLEQSFTL LTVATDDLDE IDQLLEKVEV TLEALNELQC EIEDLKDTAS
KQNARSSVAL 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 TPIASESSDF
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 VSLLKDKLEK 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 AVVQQDSSTA 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 HFLEGDAGSV VLPWERAVST NRIPYYINHE
TEKTQWDHPK MVEIINSFMD LISIEDLVDI FNQRKLQDAN DNQLDVSEMV MTLLPIYELV
QRDNMNLLRS IPLAVDLCLN WLLNVYDPAR TGNTRVISFK VALILMCRAS LSEKYRYLFN
QVSYNKCSLD QKKLALLLHE CIQVPKFFGE VAAFGGTNIE PSVRSCFEMA KYPAEVTMQQ
CMDWLNCEPQ SIVWLAAMHR ISISENEKHQ AKCNVCKMFP IVGLRYRCLK CFNFDMCQNC
FFAQRTAKNH KISHPMQEYY KAAKSGEDVR DFGRVIRNRF KSKHYWKKHP RLGYLPVQSV
MEGHSLESRD LVPTNPETQN IHVQIELYAS HLADMERSAI TESNESEDDE HAVISSLSST
LTNDCHVKQH PVNMAGAVRS PAQIMSVTDS AQKVELNGLL KHLQNENKNL MCEYEKLRNK
MSAEVDKSAA SLHNSLSTPM LPMTNGSLGR RGQHRSTSSL SRTHHQRIAP PAAYDDPAMD
LDMDTILSEE KEIIANEAKA LRQQKQRLEQ RSKVLEEHNQ QLEVQLRRIK QLIEEQKQNG
ITCIDSSKSQ LMLSSGISSQ ADAMTHCGND DSLVLSDTCS SSSNRIGDLM STVQDIGKAV
GNLINAVTSD DEVSMAEVE
//
