ID A0A0V0V4Q8_9BILA Unreviewed; 3535 AA.
AC A0A0V0V4Q8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=H(+)/Cl(-) exchange transporter 4 {ECO:0000313|EMBL:KRX58518.1};
GN ORFNames=T09_11799 {ECO:0000313|EMBL:KRX58518.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX58518.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX58518.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX58518.1};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FAM114 family.
CC {ECO:0000256|ARBA:ARBA00006903}.
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:KRX58518.1}.
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DR EMBL; JYDN01000084; KRX58518.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:InterPro.
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; 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; 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; 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; PS51746; PPM_2; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 1949..1971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2321..2346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2419..2444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2465..2487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2521..2545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2557..2574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2595..2616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2682..2702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2708..2732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2753..2777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..182
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT DOMAIN 394..763
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 836..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2113..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2984..3033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3079..3109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3352..3371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2021..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2120..2139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3352..3367
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 3535 AA; 390944 MW; BD0C99B6A770174B 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
NAEEGFDING GFDPAFIGAN GLSPRYFDSA ADASRLAYQS ASSPTNCLDN GKMLEMDAKP
LSVTASQRHE LMLHRMDDIA RHGCGSQAAS KSATTARQLC ESFVEFTKLL TVAKRKVLQD
PDLYKSTGKN SSNEIKAIRR MVKYKLMELP GKLDHASVVA YRVGFVEVQP EADELLSARD
DQVQLPVRPS VLPFAKTNTE IIGQSKMLSS IAIDDSCETP RAEAQFEFQS CACKLSSSSS
SSSSGSVRPL ANSVLEKRKQ QRADQSSTAS PIRLNSPRPS VEEKLDVMFS VVSRFAQSSS
SNSGERRANA NGVASADGCC NKMVNVGKSK KHGRTSPTRH TIAVDQADLL KRCSTSSQEQ
QQKASAGENE ENVVARLIGN KETIRMTIDR TRLIGSGLPL ARLKDVDDSL CAVVEAAAAL
WRPSGDRSTF LGCLKFSVKP RHTKMPLVLR RCRDLPAWIV LFPFCCTFLF EITNTLQVRF
LKNENAFSVR GQDSLDWDAV DADEPTAVDF WLLDDSLEET DVVVEDGAGA FLRQSVGRLV
NKTDAVARVR PLSRTVSREQ PNVRLVVERV SGRRWSSGRP APPPSGRRHF DHQTATKGSS
SSSPLCVTVF VGTADEQISA SCAPSTVDGL CTVDVLVPLS WWPEADLRST VTPDKPKRPR
RTLRIAHISR RLSGDDISNC PTMATGQTAA VWPSTPTPTA SDRALIRLAD QLQLHHRSSE
YTMLPIDHTL GLLVPNIQFH PGSVFTISLH FQRRPQQQQQ QQRPVRAFRL RCSPSSNLRI
LLAQPIPDGA WAIKSTLIST VDSNQPILID ATFKQTFLND TSAASNEVLI FVISVLSEQR
SSNGLAELLW TVEYFYDDDG DVRELSDIGI LSEKTSEEEL ARQRNLNTRF TIQKDTLMGL
FTVGKTALVN TAVMTGKQIA VPMKVFGVSY AGVIREVTLS ANCISKETSV LKVTPSCTAV
YVDGSEVRGS ANAIIQVEFS EIKSTVRYTV WFPELPVNIY LKDPVLHAIK NWHVPVMDST
LLNSNKQSIS NFTSHLINKR LFDKPNCRKR YQETEVKIFA RFRVDDMLSG WHSYLGKRGR
QLLFDLTFLT KNYLKVTDSE IASIRFSANG AVYLQGLQSG RTEIQVLLPF LRSPYGVSEV
TVVNELVNIR SVQLQSVCFL NVTAANTDGS DNIHRLYVSR IKTFSKRLQE CFLDITLEYS
DSTKSSVQNL PEADYEAIVQ SDERSLLILE SDLGFPALFR YLNLDEEKAG HIRASLYGAA
TCGRPLLGTG MVLVSPQYSS TKPHFFANSG RVRFYDSYQN HDSDSSSTRY FSKKDKHAKV
DGPSSTVQTQ RKLVTTTDAG SDSMKTPEIV MYCLIGVCGI AGAVLSLNCL VRSPTPKLVL
NSAIAQAACF LRRPQVLPAG QEFIWVQAEH AEHRRQSSHL QEESVPSSTT ASTTNNSSSS
NNTSRNSIGS SIQHLKRHID EDEEVEVEED YDDEPHTLNG RHYHQQPQVA NSYLGSEISV
HISDRPAIEV HEDGRRASSW NISRSRSRSQ HGLVDSSSER NISQYSFTKP KATIGDLHWN
SQSLGMSELQ LRDYINSLRE TNRLPSRKSH PIVTQSPPRI ASTMPPFFLG LLMSETDLLL
YKGVKKYSTP SSRIMATEIQ ENGSFGSSGT RAIGLKNMKE DDADTSVSYD VPANLDCEEP
LPIVLSQYED FHTIDWQRDL ARDRLRHKFI KKKNRESMTS CITGLVDAGS GWICVLFVGL
TAVNIVRFRV VAGLVDISTR WMSDLKEGVC PDAFWFDREH CCWSANDTLF YGDKCNAWHT
WPELFGHYSE DGLAYFVEYV FYTCWALGLA GLAAIFVRVF APYACGSGIP EIKCMLSGFV
IHGYLGKWTL IIKTIGLVLA AASGLSLGKE GPMVHLTCCI GNILSYLFPK YGKNEAKKRE
ILSASAAAGV SVAFGAPIGG VLFSLEEASY YFPLKTLWRS FFCALIAGLI LKFINPFGTD
QTSLFAVDYP MRWSYIELIP FISLGIFGGV IGTIFIKCNI CWCRFRKSST LGDYPIAEVL
SITFITALLS FPNEYTSKYR EVIGVTNSTS DISFGSLMNG TIWKLVLSLI FKIVITIFTF
GMKVPSGLFV PSLAIGAIGG RLVGITMEWL ALDYRDAWWW GIYCEPGKVC VQPGLYAMVG
AAAVLGGVTL SLVVIMFELT GSLEFIVPTM AAVMFAKWIG DAFDRRGIYD AHIALNGYPF
LDNKEEFTLN SVAADVMRPR PGDMPLRVIS QEGMTVGDIE ELLRLTDHNG FPIVVSEDSP
NLIGYVTRPT ARKNQEGIVT DSLVYFSSNA PVDPEGPGRP VPLRLRKLLD LAPISITDQT
PMETVIDIFR KLGLRQLLVT HMGMDDDDAY LSATEGSKFS EMYESDDDYD ESSGDEISVN
KGGSGIKNVE NLKERSDSNE GSSTKASSVE QQDGLDIFAA VEDRSDSEGT VAGGDWDWNS
ELDVEGKQPT YVEEVADGDK KSECKSDEGE EIVESKQTPD TSEKGVTEEK VAAVKDEEPN
QSDEGLFGGW GSLVFKAGHS LQSLGQIIGD SVVTAVETVE SSLGVVSPEE MARRNIELEN
HSVSREEEKQ ENPTGADICQ SGGVVGDLFK NLKSTSMNLV DSSLGALEIL GQKTYEVLTE
CDSATGRRKL KFERSEPTLS EMLQELRDAG DKEAPLQQPP PVEEFTFDGL KFFTAKLDEK
RISHVMKKLE ILKMNSLRKI DSMKKTLPPQ RLSSVTKLLA KYEKEFLATE ESLSDGMREK
QADETQEDSS DSEFAITPFE MNIELPITYT TNLKIDSLKN SHRQCSDLIT SLKNGNSAEL
GEVVQMAESG LEALADFTFQ CANCWLELIE SLNTMKAPLC ASKLANIVSG MCMEVQTFVS
DLNIEILMCT TKEVEAQVCA TEVFLQANKS CSLIHQAYNY LLPYMQWLHL KDVLN
//
