ID A0A0V0V4W7_9BILA Unreviewed; 3566 AA.
AC A0A0V0V4W7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=T09_11799 {ECO:0000313|EMBL:KRX58524.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX58524.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX58524.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX58524.1};
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: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004337}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361221}.
CC -!- SIMILARITY: Belongs to the FAM114 family.
CC {ECO:0000256|ARBA:ARBA00006903}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000256|RuleBase:RU361221}.
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:KRX58524.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDN01000084; KRX58524.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03684; ClC_3_like; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.580.20; -; 1.
DR Gene3D; 3.90.1280.20; -; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR007998; DUF719.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR031437; TMEM132_M.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF05334; DUF719; 1.
DR Pfam; PF13672; PP2C_2; 1.
DR Pfam; PF16070; TMEM132; 1.
DR Pfam; PF00179; UQ_con; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU361221};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361221};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361221}; Transport {ECO:0000256|RuleBase:RU361221};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 1954..1976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2326..2351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2424..2449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2470..2492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2526..2550
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2562..2579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2600..2621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2687..2707
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2713..2737
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2758..2782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 30..182
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT DOMAIN 394..768
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 2930..2991
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 841..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2019..2063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2118..2144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3012..3064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3108..3138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3383..3402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2026..2058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2125..2144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3383..3398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 3566 AA; 394440 MW; 44F33684E32735BB CRC64;
MLNLQKKLKE QKINESNKQN ATGRKEAASV RDRLLQVEFQ DLGSSLPPGC KLEFPTAELH
NFFVSIKPED GMYVGGEYRF QIEVPMEYNF EPPIVKCLTK IWHPNISENG AVCLSLLRSL
SMDGFGWNPT RGIKDVILGL YALFGDLIDF DDPLNSDAAK MYLRNPTEFK CKVITWACLF
VVDMPCHLNI LGVVGWQCCY YCCCCCCCCL KATRMASIKK RMYCVMRHFS SSVGSPCELE
KKLEDVIPSA GSAVDDVSKN RQKSSTAPSY LKRYFCSQMA KKRTPEIYYG KSGADLPNFN
IITLLETPVI ASYTGPDGGL TEAPPLRVTV PAGIANLDDE LSLSMHASSE SLTVDRCCTD
ASLGGLKTDL LSKKRIVRMC DWISPDDQHS YGKSVSLYER NPITSKLAGN PVADVFAVCT
RRNCSILILA DGVNWGEKAR LAARCAVRGS MDFLNAELFD RSQPITSTSE IFQSLLRAFH
CGHRLILQEE GSFTTLCVVV VCPLENSEHW VACACNVGDS LAFIFSEQHG VRELTSGSHD
IRQIRNMRDA GGALGPVYGI SPDLQNFTCS LSIVDPGDIV FITSDGVSDN FDPVVGKFCI
NAEVECFVEG FDINGGFDPA FIGANGLSPR YFDSAADASR LAYQSASSPT NCLDNGKMLE
MDAKPLSVTA SQRHELMLHR MDDIARHGCG SQAASKSATT ARQLCESFVE FTKLLTVAKR
KVLQDPDLYK STGKNSSNEI KAIRRMVKYK LMELPGKLDH ASVVAYRVGF VEVQPEADEL
LSARDDQVQL PVRPSVLPFA KTNTEIIGQS KMLSSIAIDD SCETPRAEAQ FEFQSCACKL
SSSSSSSSSG SVRPLANSVL EKRKQQRADQ SSTASPIRLN SPRPSVEEKL DVMFSVVSRF
AQSSSSNSGE RRANANGVAS ADGCCNKMVN VGKSKKHGRT SPTRHTIAVD QADLLKRCST
SSQEQQQKAS AGENEENVVA RLIGNKETIR MTIDRTRLIG SGLPLARLKD VDDSLCAVVE
AAAALWRPSG DRSTFLGCLK FSVKPRHTKM PLVLRRCRDL PAWIVLFPFC CTFLFEITNT
LQVRFLKNEN AFSVRGQDSL DWDAVDADEP TAVDFWLLDD SLEETDVVVE DGAGAFLRQS
VGRLVNKTDA VARVRPLSRT VSREQPNVRL VVERVSGRRW SSGRPAPPPS GRRHFDHQTA
TKGSSSSSPL CVTVFVGTAD EQISASCAPS TVDGLCTVDV LVPLSWWPEA DLRSTVTPDK
PKRPRRTLRI AHISRRLSGD DISNCPTMAT GQTAAVWPST PTPTASDRAL IRLADQLQLH
HRSSEYTMLP IDHTLGLLVP NIQFHPGSVF TISLHFQRRP QQQQQQQRPV RAFRLRCSPS
SNLRILLAQP IPDGAWAIKS TLISTVDSNQ PILIDATFKQ TFLNDTSAAS NEVLIFVISV
LSEQRSSNGL AELLWTVEYF YDDDGDVREL SDIGILSEKT SEEELARQRN LNTRFTIQKD
TLMGLFTVGK TALVNTAVMT GKQIAVPMKV FGVSYAGVIR EVTLSANCIS KETSVLKVTP
SCTAVYVDGS EVRGSANAII QVEFSEIKST VRYTVWFPEL PVNIYLKDPV LHAIKNWHVP
VMDSTLLNSN KQSISNFTSH LINKRLFDKP NCRKRYQETE VKIFARFRVD DMLSGWHSYL
GKRGRQLLFD LTFLTKNYLK VTDSEIASIR FSANGAVYLQ GLQSGRTEIQ VLLPFLRSPY
GVSEVTVVNE LVNIRSVQLQ SVCFLNVTAA NTDGSDNIHR LYVSRIKTFS KRLQECFLDI
TLEYSDSTKS SVQNLPEADY EAIVQSDERS LLILESDLGF PALFRYLNLD EEKAGHIRAS
LYGAATCGRP LLGTGMVLVS PQYSSTKPHF FANSGRVRFY DSYQNHDSDS SSTRYFSKKD
KHAKVDGPSS TVQTQRKLVT TTDAGSDSMK TPEIVMYCLI GVCGIAGAVL SLNCLVRSPT
PKLVLNSAIA QAACFLRRPQ VLPAGQEFIW VQAEHAEHRR QSSHLQEESV PSSTTASTTN
NSSSSNNTSR NSIGSSIQHL KRHIDEDEEV EVEEDYDDEP HTLNGRHYHQ QPQVANSYLG
SEISVHISDR PAIEVHEDGR RASSWNISRS RSRSQHGLVD SSSERNISQY SFTKPKATIG
DLHWNSQSLG MSELQLRDYI NSLRETNRLP SRKSHPIVTQ SPPRIASTMP PFFLGLLMSE
TDLLLYKGVK KYSTPSSRIM ATEIQENGSF GSSGTRAIGL KNMKEDDADT SVSYDVPANL
DCEEPLPIVL SQYEDFHTID WQRDLARDRL RHKFIKKKNR ESMTSCITGL VDAGSGWICV
LFVGLTAVNI VRFRVVAGLV DISTRWMSDL KEGVCPDAFW FDREHCCWSA NDTLFYGDKC
NAWHTWPELF GHYSEDGLAY FVEYVFYTCW ALGLAGLAAI FVRVFAPYAC GSGIPEIKCM
LSGFVIHGYL GKWTLIIKTI GLVLAAASGL SLGKEGPMVH LTCCIGNILS YLFPKYGKNE
AKKREILSAS AAAGVSVAFG APIGGVLFSL EEASYYFPLK TLWRSFFCAL IAGLILKFIN
PFGTDQTSLF AVDYPMRWSY IELIPFISLG IFGGVIGTIF IKCNICWCRF RKSSTLGDYP
IAEVLSITFI TALLSFPNEY TSKYREVIGV TNSTSDISFG SLMNGTIWKL VLSLIFKIVI
TIFTFGMKVP SGLFVPSLAI GAIGGRLVGI TMEWLALDYR DAWWWGIYCE PGKVCVQPGL
YAMVGAAAVL GGVTLSLVVI MFELTGSLEF IVPTMAAVMF AKWIGDAFDR RGIYDAHIAL
NGYPFLDNKE EFTLNSVAAD VMRPRPGDMP LRVISQEGMT VGDIEELLRL TDHNGFPIVV
SEDSPNLIGY VTRPTARKNQ EGIVTDSLVY FSSNAPVDPE GPGRPVPLRL RKLLDLAPIS
ITDQTPMETV IDIFRKLGLR QLLVTHMGKL LGIVTKKDVL VHIKELENED TSTIMDDDDA
YLSATEGSKF SEMYESDDDY DESSGDEISV NKGGSGIKNV ENLKERSDSN EGSSTKASSV
EQQDGLDIFA AVEDRSDSEG TVAGGDWDWN SELDVEGKQP TYVEEVADGD KKSECKSDEG
EEIVESKQTP DTSEKGVTEE KVAAVKDEEP NQSDEGLFGG WGSLVFKAGH SLQSLGQIIG
DSVVTAVETV ESSLGVVSPE EMARRNIELE NHSVSREEEK QENPTGADIC QSGGVVGDLF
KNLKSTSMNL VDSSLGALEI LGQKTYEVLT ECDSATGRRK LKFERSEPTL SEMLQELRDA
GDKEAPLQQP PPVEEFTFDG LKFFTAKLDE KRISHVMKKL EILKMNSLRK IDSMKKTLPP
QRLSSVTKLL AKYEKEFLAT EESLSDGMRE KQADETQEDS SDSEFAITPF EMNIELPITY
TTNLKIDSLK NSHRQCSDLI TSLKNGNSAE LGEVVQMAES GLEALADFTF QCANCWLELI
ESLNTMKAPL CASKLANIVS GMCMEVQTFV SDLNIEILMC TTKEVEAQVC ATEVFLQANK
SCSLIHQAYN YLLPYMQWLH LKDVLN
//
