ID A0A1I7UTD3_9PELO Unreviewed; 3290 AA.
AC A0A1I7UTD3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dystrophin {ECO:0000313|WBParaSite:Csp11.Scaffold630.g19154.t2};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold630.g19154.t2};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold630.g19154.t2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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}.
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DR STRING; 1561998.A0A1I7UTD3; -.
DR WBParaSite; Csp11.Scaffold630.g19154.t2; Csp11.Scaffold630.g19154.t2; Csp11.Scaffold630.g19154.
DR eggNOG; KOG4286; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
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; -; 7.
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; IPR013087; Znf_C2H2_type.
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; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 6.
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; PS50135; ZF_ZZ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 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 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 2783..2817
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 3037..3093
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 57..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2133..2209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3219..3246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..396
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 524..551
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 739..821
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 845..898
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1035..1062
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1257..1302
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1451..1478
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1759..1793
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1960..1987
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2620..2684
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3188..3215
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 57..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2138..2174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2175..2194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3219..3237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3290 AA; 374257 MW; B978A4B509138F19 CRC64;
MINGEEEEGA DLHSEQLDSH SVLCYLMNLY LAMISTSKIE NELEAQQIQQ QKAAILAAHK
MQSQPSTSSG LQIPPQSPPA HTMLDRGKSF EQSVESEVRS RKSSSSSQKS GKSKKVRREE
QLAEFKSCIE QVLTWLLEAE DELATLTQMP RVELASVRSQ FADFESFMSS LTDSQDTVGR
VLLRGQMLSN KSENEEEKEA IAAKLHLVNT RWEALREQAM QEQAVLQQQI HLLQQSELDS
ISQWLDATEL EIESFGPLAS DSAQALRQIE LHTKFQQKLN DFQETIDKLE SFVAVVDEEN
DASVATLEDA LSGVSVRWGH VCEWAEKRAA KLDGLADLID RTNEVFENLS DWLTARENEL
MVGLKSAHHL ENEEQVAQQV RRLQRTEEQL EQEHSSFVRL SQLSCELVGR LDESNGAAAN
TVRLSLDSIT QRWDNLVARI EEHGKTLVKS GKADVKQVET KEPQVSSEGL STDTEGEEQK
NQLVDKFLLH ISKLSHELEP LQEWSERFEV SRKRDDVRKM MNTCQEKLIQ IKEQEARVNR
LQLELEHLHV AKLNAKQLKR ANDAFEQFAK GWARIVTKIS EAMNVLTGQE ANGGNGGSEE
AAVAAKIEQW IEAVDKVINE LSQLPVSERL SRIDKLEQQL QVQDKNVGFI EKDLLKKAIL
KKGLEIAGKR LAALKIEEKV EEPEAEKHVT FTQEASNSPI SESSLLEELD GPWSPVGDVI
RIEQDLLRAQ RAVDTARNSN MSNETVEKAE TRKAEMEEKR RVTVAARSKF QIAEETVDEI
ERSLDRLQAS DLEIADLVRG LEQESTKLAD HSSQRKEAER TAEKMLSMDD VEIAPEIVIK
TKDSIEKLAK RWNQLELDLE ENLRKARKDQ DLFIQKRLRE GEEALNEIKS AIESKRESLD
AETAAESLDH LESSLDNISS LFGEIGSLPM DDNSREKLTK LTEAKEEITG RANEALAALS
RTVSECEDFE KQIMLFQNWS ARIGFLLQAR KSADISAFDI PHEFHDDLGN EAELIPKLSR
EFEDWTGKLN EMNSLAMEKE DAVRMREQLN HANDTMSELR RKFNEFKRPK GFEEKLEKVI
TTLSNVEMGL DDTTGIDGSE CGGALMEVRA LVRMLDGAQE KWKDLSENRE QLVKDHILDE
ETSKETLQKL QYAKTKSKEL YERSSTCIER LEDCVEMYQR LRMESDEIER FLEEMETRLD
RYAASDRPEE AEVVDELISE WNRNEAAMNN AAHLQRQLNE RAIKIPEDVL SLKRIRADAL
KNRLNSWCRT IQEMSEDDES ALLEIDELHH NLEKELQEVS DKEPAKIAEK LRFLRADRDR
LSSRTRKLAA KNPHLAATSS DVLASLNQKW KDLEEKATRE KEPEKLLELR DASLSAPEAA
PFDKRVEELC GLFQNLGAHL DFVSSPVSSA KEYQKRVYDL DVYLDEYRPP LDDVIEEGRK
IAQTGRLELQ THAAIEKLDE LANQIEQVET DLDKHREKVP PLVEQHEQLK KDIDSFLLVL
DVFTDRNLDD VDIAKATRKE LAERDSHITS LTSRATAIHC ALPGKSPQLK DSTLDRLRSR
VEALESRLSE TEKRAEPREE PKAPEPSKLD PEAEKLSPDR TSRSSLQLAM EAYGTGTEDD
SVISEAVTVA NKEAPGTPKL EPKIIVPPEE SKKSIEEEEV KESKATTLQA AEEEKIAEVS
TSEVLQGKPA QESIERTVRE VPVDVYEETA NISSGDELQD TKLSPPIPDS DSEVATMFET
LDTIEDAHTN FEEFPFDYLD NAEHDLKKTL ARLESCEKTL EKNEMTINIA QAENARERIT
MLRQMALQRK DKLPKFNEEW NAIQELILNA DQLVEEAERY ESDQIPTMDR KSAPNVLGEL
RKRVSSAEGP VIDLVKKLSQ LVPRMQDDSP KSQNIRKTVY GIEDRFRKVS QAETAAVSKA
LSSALTEPEL KFELAEMVKW CEMAEKEAAQ NVNSLDSDGL EKLDGRLAQF TKELQEKKTD
MVQLEMAKNM IIPSLKGDAH HELRRHFSET AKRVAMVRDE LSDAHKWVST SRDTCDAFWT
DIDQLEGLAR DVVRRANGIR MAVIYTPSRE NVEGVLRDVA RLKISIGDIK KRVQTANLPP
AIKLAGKNAK RVVQVLTETA TTIADCHDLP TYLIDEMNDS GGDTTESRST VVEMTPVHAK
QSSSSSSNRT AESESEPTPH ADDEQSEEDQ KVYSRESSST LPRGGTLDPV AVQLTHTRHW
LHDVERDASV TVDLAQWQPA RELWQSIQGI IDEIRLRSVQ VTGAHDASPN RQVRQQAAQL
LTEMRRTIEN CEKRCVILNQ ISDIARQNES SRNEMELWLK SATDVIGERR VEELAEEVVR
QELGVLERVV GQLGERKEKM AEINTQAHKI VDTFTKDEAH NLSHLLSRLN MTWTKFNDNI
RIRRAVLEAS LRSRRDFHSA LAEFEMWLGR QEENCSKLAH ETSNHQAIKD TSKRKNWTQG
FKTLNAELNA HEDVMRSVES MGKMLAESLE SGGEKAELLK RVGETTRRWA ALRKTTNDIG
ERLEKAEQEW EKLSDGLADL LSWIETKKQK IVEEQPIAGS LSAVMQQSAF VKTIQREMES
KNGVFKTTVA DAHSFLMQHD LRPKLHSPHV LDDDYEEEEL ADLEQRRRGL EINANCEKLK
KNWAELGVEV ESWDKLVQHA MQRLQELERN LAECQLHLTS SENEIETMKA VEKIHLEDLK
IAREETDQIS KRIDEVRLFV DDVNDAAARL LAEDLKLDEH AKGQIEHVNK RYSTLKRAIR
IRQAAVRNAA SDFGPTSEHF LNQSVTLPWQ RAISKSNLLP YYIEQTTEKT QWEHPVWVEI
VKELSAFNRV KFLAYRTAMK LRALQKRLCL DLVDLPLLEK AFVRLKGLSA EECPGLEGMV
CALLPMYEAL HAKHPNQVQS VSLAVDIAIN FLLNLFDQSR DGIMRVLSFK IAMIVFCNIP
LEEKYRYLFK LVSQDGHATQ KQIALLLYDL IHIPRLVGES AAFGGTNVEP SVRSCFESVR
LAPTISEGAF IDWVKKEPQS IVWLAVMHRL VISENTKHAS KCNVCKMFPI IGIRYRCLTC
FNCDLCQNCF FSQRTAKNHK MNHPMQEYCE KTTSSDDARD FAKMIRNKFR ASKRQKGYLP
IDNAEEGIPL TCPPAKVTNQ STEQMNTDTA QMTAHLAKLS AEHGGGAEHM EPVQSPLQII
NQVEQLQRDE MDQMLHRLQI ENKQLRKELE WKRGAASTME IDRSSKRPTD RRSESRGGTL
PLRNGRSVVS LKSTQSQNDV SLSLSXXXXX XXTNPYLFLL IMNPIRQKSI
//
