ID A0A0V0ZFX0_9BILA Unreviewed; 3075 AA.
AC A0A0V0ZFX0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN Name=CLCN4 {ECO:0000313|EMBL:KRY11327.1};
GN ORFNames=T12_1613 {ECO:0000313|EMBL:KRY11327.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY11327.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY11327.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY11327.1};
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 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:KRY11327.1}.
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DR EMBL; JYDQ01000198; KRY11327.1; -; Genomic_DNA.
DR SMR; A0A0V0ZFX0; -.
DR STRING; 990121.A0A0V0ZFX0; -.
DR Proteomes; UP000054783; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000054783};
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 2373..2401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2421..2440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2502..2524
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2544..2564
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2604..2628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2640..2661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2681..2705
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2765..2784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2791..2814
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 2838..2860
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 435..809
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 3008..3069
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 906..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1951..1979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2065..2121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2165..2191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..1972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2072..2105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2172..2191
FT /note="Polar 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 3075 AA; 340300 MW; 9AE2E8DBC8FAFA32 CRC64;
MLNLQKKLKE QKINESNKQN ATVRKEAASV RDRLLQVEFQ DLGSSLPPGC KLEFPTAELH
NFFVSIKPED GMYVGGEYRF QIEVPMEYNF EPPIVKCLTK IWHPNISENG AVCLSLLRSL
SMDGFGWNPT RGIKDVILGL YALFGDLIDF DDPLNSDAAK MYLRNPTEFK CKVITGQVAT
ANSKGIKMQF ICNQLQFIIS VLKRGFAYLW SICMSHGNNY NAFGVPCHLN ILGVVGWQCC
YYCCCCCCCC LKATRMASIK KRMYCVMRHF SSSVGSPCEL EKKLEDVIPS AGSTVDDVSK
NRQKSSTAPS YLKRYFCSQM AKKRTPEIYY GKSGADLPNF NVITLLETPV IASYTGPDGG
LTEAPPLRVT VPAGIANLDD ELSLSMHASS ESLTVDRCCT DASLGGLKTD LLSKKRIVRL
CDWISPDDQH SYGKSVSLYE RNPITSKLAG NPVADVFAVC TRRNCSILIL ADGVNWGEKA
RLAARCAVRG SMDFLNAELF DRSQPITSTS EIFQSLLRAF HCGHRLILQE EGSFTTLCVV
VVCPLENSEH WVACACNVGD SLAFIFSEQH GVRELTSGSH DIRQIRNMRD AGGALGPVYG
ISPDLQNFTC SLSIVDPGDI VFITSDGVSD NFDPVVGKFC INAEVECFVE GFDINGGFDP
AFIGANGLSP RYFDSAADAP RLAYQSASSP TNCLDNGKML EMDAKPLSVT ASQRHELMLH
RMDDIARHGC GGQAASKSAT TARQLCESFV EFTKLLTVAK RKVLQDPDLY KSTGKNSSNE
IKAIRRMVKY KLMELPGKLD HASVVAYRVG FVEVQPEADE LLSGRDDQVQ LPVRPSVLPF
AKTNTEIIGQ IKMLSSIAID DSCETPRAEA QFEFQSCACK LSSSSSSSSS WSSSSGSVRP
LANSVLEKRK QQRADQSSTA SPIRLNSPRP SVEEKLDVMF SVVSRFAQSS SSNSGERRAS
DANDVASADG CCNKMVNVGK LKKHGRTSPT RHTIAVDQAD LLKRCSTSSQ EQQQKASAGE
NEENVVARLI GNKETLRMTI DRTRLIGSGL PLARLKDVDD SLCAVVEAAA ALWRPSGDRS
TFLGCLKFSV KPRHTKMPLV LRRCRDLPAW IVLFPFCCTF LFEITNTLQV RFLKNENAFS
VRGQDSLDWD AVDADEPTAV DFWLLDDSLE ETDVVVEDGA GAFLRQSVGR LVNKTDAVAR
VRPLSRTVSR EQPNVRLVVE RVSGRRWSSG RPAPPPSGRR HFDHQTATKG SSSSSPLCVT
VFVGTADEQI SASCAPSTVD GLCTVDVLVP LSWWPEADLR STVTPDKPKR PRRTLRIAHI
SRRLSGDDIS NCPTMATGQT VAVWPSTPTP TAGDRALIRL ADQLQLHHRS SEYTMLPIDH
TLGLLVPNIQ FYPGSVFTIS LHFQRRPQQQ QQQRPVRAFR LRCSPSSNLR ILLAQPIPDG
AWAIKSTLIS TVDSNQPILI DATFKQTFLN DTSAASNEVL IFVISVLSEQ RNSNGLAELL
WTVEYFYDDD GDVRELSDIG ILSEKTSEEE LARQRNLNTR FTIQKDTLMG LFTVGKTALV
NTAVMTGKQI AIPMKVFGVS YAGVIREVTL SANCISKETS VLKVTPSCTA VYVDGSEVRG
SANAIIQVEF SEIKSTVRYT VWFPELPVNI YLKDPVLHAI KNWHVPVMDS TLLNSNKQSI
SNFTSHLINK RLFDKPNCRK RYQETEVKIF ARFRVDDMLS GWHSYLGRRG RQLLFDLTFL
TKNYLKVTDS EIASIRFSAN GAVYLQGLQS GRTEIQVLLP FLRSPYGVSE VTVVNELVNI
RSVQLQSVCF LNVTAANTDG SDNIHRLYVS RVKTFSKRLQ ECFLDITLEY SDSTKSSVQN
LPEADYEAIV QSDERSLLIL ESDLGFPALF RYLNLDEEKA GHIRASLYGA ATCGRPLLGT
GMVLVSPQYS STKPHFFANS GRVRFYDSYQ NHDSDSSSTR YFSKKDKHAK VDGPSSPVQT
QRKLITTTDA GSDSMKTPEI VMYCLIGVCG IAGAVLSLNC LVRSPTPKLV LNSAIAQAAC
FLRRPQVLPA GQEFIWVQAE HAEHRRQSSH LQEESVPSST TASTTNNSSS SSNNTSRNSI
GSSIQHLKRH TDEDEEVEIE EDYDDEPHTL NGRHYHHQPQ VANSYLGSEI SVHISDRPAI
EVHEDGRRAS SWNISRSRSR SQHGLVDSSS ERNISQYSFT KPKATIGDLH WNSQSLGMSE
LQLRDYINSL RETNRLPSRK SHPIVTQSPP RIASTMPPFF LGLLMSETDL LLYKGVKKYS
TPSSRIMATE IQENGSFGSS GTRAIGLKNM KEDDADTSVS YDVPANLDCE EPLPIVLSQY
EDFHTIDWQR DLARDRLRHK FIKKKNRESM TSCITGLVDA GSGWICVLFV GLTAVNIVRF
IGGNGVKQEA YTVLLFNDST FLFVLKCLHF HGVVAGLVDI STRWMSDLKE GVCPDAFWFD
REHCCWSAND TLFYGDKCNA WHTWPELFGH YSEDGLAYFV EYVFYTCWAL GLAGLAAIFV
RVFAPYACGS GIPEIKCMLS GFVIHGYLGK WTLIIKTIGL VLAAASGLSL GKEGPMVHLT
CCIGNILSYL FPKYGKNEAK KREILSASAA AGVSVAFGAP IGGVLFSLEE ASYYFPLKTL
WRSFFCALIA GLILKFINPF GTDQTSLFAV DYPMRWSYIE LIPFISLGIF GGVIGTIFIK
CNICWCRFRK SSTLGDYPIA EVLSITFITA LLSFPNEYTS KYREVIGVTN STSDISFGSL
MNGTIWKLVL SLIFKIVITI FTFGMKVPSG LFVPSLAIGA IGGRLVGITM EWLALDYRDA
WWWGIYCEPG KVCVQPGLYA MVGAAAVLGG VTLSLVVIMF ELTGSLEFIV PTMAAVMFAK
WIGDAFDRRG IYDAHIALNG YPFLDNKEEF TLNSVAADVM RPRPGDLPLR VISQEGMTVG
DIEELLRLTD HNGFPIVVSE DSPNLIGYVT RPTARKNQEG IVTDSLVYFS SNAPVDPEGP
GRPVPLRLRK LLDLAPISIT DQTPMETVID IFRKLGLRQL LVTHMGKLLG IVTKKDVLVH
IKELENEDTS TILSV
//
