ID H2KZ66_CAEEL Unreviewed; 1720 AA.
AC H2KZ66;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Potassium channel domain-containing protein {ECO:0000313|EMBL:CCD66544.1};
GN Name=twk-11 {ECO:0000313|EMBL:CCD66544.1,
GN ECO:0000313|WormBase:F20A1.7b};
GN ORFNames=CELE_F20A1.7 {ECO:0000313|EMBL:CCD66544.1}, F20A1.7
GN {ECO:0000313|WormBase:F20A1.7b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD66544.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD66544.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD66544.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC ECO:0000256|RuleBase:RU003857}.
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DR EMBL; BX284605; CCD66544.1; -; Genomic_DNA.
DR RefSeq; NP_504783.2; NM_072382.6.
DR AlphaFoldDB; H2KZ66; -.
DR STRING; 6239.F20A1.7b.1; -.
DR PaxDb; 6239-F20A1-7b; -.
DR EnsemblMetazoa; F20A1.7b.1; F20A1.7b.1; WBGene00006666.
DR GeneID; 179088; -.
DR AGR; WB:WBGene00006666; -.
DR WormBase; F20A1.7b; CE39245; WBGene00006666; twk-11.
DR eggNOG; KOG1418; Eukaryota.
DR InParanoid; H2KZ66; -.
DR OMA; EMCEQSA; -.
DR OrthoDB; 2882245at2759; -.
DR Reactome; R-CEL-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-CEL-5576886; Phase 4 - resting membrane potential.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006666; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; H2KZ66; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR Gene3D; 1.10.287.70; -; 1.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR PANTHER; PTHR11003:SF61; TWIK FAMILY OF POTASSIUM CHANNELS; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|RuleBase:RU003857, ECO:0000313|EMBL:CCD66544.1};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..215
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 308..380
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 278..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1598..1720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..628
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..763
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1720 AA; 192258 MW; C8BCCCB4217EA6D4 CRC64;
MSNDNLAIEI DPPDDVEYDV EAGFNSSTCH LMHNFEEERP TSLVASIKES AISSKRKLKY
YCSFICTPIK KLLSTFKLLI IIGLYSFIGA HIFMYLEVPT DLEAREDGFH QRKIAREVMV
LNLRAIFYDN REDREERWKH AILKFEEDIG LEEPVIETVW TFWMSFLYAG TIFTTIGYGN
IACKTRAGQI ATMVYAFVGI PIMLVMLTSL NNFLLKWIKL ITNGVSDMTL YIGVRLGITV
IRQDEVQKRL RYTKLAKTMK RWKLSKHGAP SSIAISNSEE NRLNSTPEDD EEEEEIHQDP
PVLSTLIATV AWIILSAAVF CLFEDWTFFT SFYFCFISLT TIGLGDVTPA NPEYMIATFG
VVIVGLSMLT VCIDVLQEKL AQMYMALLQK LLTEYMEAVK SGDPNAASAM MAGFQGRAKF
LMPLISKNEG AKVMDKFKQD CSKKGIDPPP VLTNINPETG MPAFANAPKE DFRDYIEVAD
EKFADEQQRL SQTPLSKSTD FLQSPTPRPT VTVAVTQTAR PQACVSLEVQ AGTTMGKFHD
YGSQTQTESS DEGIQTDYSI DFDDEKNKEP EKVMADIGTQ YEIVLLTSIG IQPEVSSIYI
GAGLSDHSDE ESGCESEDDS DDSDVSSDEE SELKSSAKYK ETPLPFEVED PGMMSLGLQS
PPIEITPFTD DESAASDARS SPVPPTSSKR SKLTPKTIKV GKSLSMDSTD TVIHVKPVGV
NDDEKRSEEK ESKDQETNDD LKTESGQEKK RRKKKKKLRS KKTREHELRF LKNSGNQASP
LLMDCSTQYE IFTVESGSQY DVKGRSRKCQ TKLSSINHEQ LQGIRETVQK LRRRESEMSK
VSNVSESDWD SETGKEPEVA EISLDLSVVA LGVDESGKVV DIPKEVPKAV QRHESFSPTS
ELTTASESLS AEKVHLDSED EELESLEELE LYTTDAGIQT ETKVMLDKQD NATPKLLEII
KNCSTQTTFS TFHIPQKVYE SASTSSDEED HKNDGEDEKQ KKSKQEVFFM TNTGVQTMHT
SFHIDEKPKF VEENLQTQNT HDGIKEQSAV DEEMPLFLKN SDCQTVEVIS FECATSTENV
SFVGDVETSE GSSQTAMQVS ETEVQTMQQE FVVATMQTDE PLLVSDESQT EQTKSSEIDS
QTDPPSTKSF ICQTELITSS EVEVQAVRAV EFSLVECQTD ALNHEEVEVQ TELDISVSQS
QTDNVDVGHI EMQTDMTITN ASESQTDVLS VGDTEMQTDE KEIFTIESQT EQPSTELQET
QTDDVSFAGD VPTTDQITQS ESAQVFDSET QYALSIEEKD VQATPISFET QTQHSIELEV
KSCQTEGVRM KNKKSQVEDD SMLSVLKIDS ESQIEVDVSS INLSPIRLDV SNMFTMTEPG
ASEEKEVQVD EDCFEPEETS RNYYAGPLWS DFDYTPVIGE DGEEVMDGET QTQDGSEPGD
PEFDEQRGQE QEEGEDDKER AHDQTAIGRS SRRKKIRKSQ CISSENLLET PSSVQQSSDS
LASESAVQCS PESYDMKIQT SKFKKKKKVE KNIEAKVEMS TSTVQATTEM CEQSAGSIED
DWLQVYVQEL DEERRMRMSD IGIQTGVLAR VQHIYTRPIS DDVGPSSSAP ITLRKSSDSS
EHISTKTAKS SEESLAPSAS GTALSAAESM DDHLWPERAS PFASRHGSLK RRTRELDPEK
KGDKTNIVQD LRARFEMKSP PKSPPKDDEE GTSTDPKHFF
//
