TWK18_CAEEL
ID TWK18_CAEEL Reviewed; 461 AA.
AC Q18120; Q9TZP8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=TWiK family of potassium channels protein 18;
GN Name=twk-18; ORFNames=C24A3.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC32861.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP GLY-140; GLY-165 AND MET-280, AND DISRUPTION PHENOTYPE.
RX PubMed=11027209; DOI=10.1523/jneurosci.20-20-07517.2000;
RA Kunkel M.T., Johnstone D.B., Thomas J.H., Salkoff L.;
RT "Mutants of a temperature-sensitive two-P domain potassium channel.";
RL J. Neurosci. 20:7517-7524(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Outwardly rectifying potassium channel protein; activity is
CC sharply augmented by increase in temperature.
CC {ECO:0000269|PubMed:11027209}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscle.
CC {ECO:0000269|PubMed:11027209}.
CC -!- DISRUPTION PHENOTYPE: Worms display uncoordinated movement and
CC paralysis. {ECO:0000269|PubMed:11027209}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000255}.
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DR EMBL; AF083650; AAC32861.1; -; mRNA.
DR EMBL; FO080639; CCD65384.1; -; Genomic_DNA.
DR PIR; T15585; T15585.
DR PIR; T43394; T43394.
DR RefSeq; NP_509516.1; NM_077115.5.
DR AlphaFoldDB; Q18120; -.
DR SMR; Q18120; -.
DR STRING; 6239.C24A3.6.1; -.
DR TCDB; 1.A.1.9.5; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q18120; -.
DR EPD; Q18120; -.
DR PaxDb; Q18120; -.
DR PeptideAtlas; Q18120; -.
DR EnsemblMetazoa; C24A3.6.1; C24A3.6.1; WBGene00006672.
DR EnsemblMetazoa; C24A3.6.2; C24A3.6.2; WBGene00006672.
DR GeneID; 181139; -.
DR UCSC; C24A3.6.2; c. elegans.
DR CTD; 181139; -.
DR WormBase; C24A3.6; CE24811; WBGene00006672; twk-18.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_597598_0_0_1; -.
DR InParanoid; Q18120; -.
DR OMA; CMTVYTT; -.
DR OrthoDB; 1171809at2759; -.
DR PhylomeDB; Q18120; -.
DR PRO; PR:Q18120; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006672; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IC:WormBase.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:WormBase.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0006936; P:muscle contraction; IMP:WormBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IDA:WormBase.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..461
FT /note="TWiK family of potassium channels protein 18"
FT /id="PRO_0000101773"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 116..136
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 253..273
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT MUTAGEN 140
FT /note="G->E: In sa589; defects in locomotion."
FT /evidence="ECO:0000269|PubMed:11027209"
FT MUTAGEN 165
FT /note="G->D: In e1913; homozygotes are embryonic lethal,
FT heterozygotes exhibit defects in locomotion."
FT /evidence="ECO:0000269|PubMed:11027209"
FT MUTAGEN 280
FT /note="M->I: In cn110; temperature sensitive defects in
FT locomotion."
FT /evidence="ECO:0000269|PubMed:11027209"
SQ SEQUENCE 461 AA; 52746 MW; D436B3654AB9C5DF CRC64;
MAIVAQGVST ILTTFQKTFK GLLPLIILVA YTLLGAWIFW MIEGENEREM LIEQQKERDE
LIRRTVYKIN QLQIKRQRRL MTAEEEYNRT AKVLTTFQET LGIVPADMDK DIHWTFLGSI
FYCMTVYTTI GYGNIVPGTG WGRFATILYA FIGIPLTVLS LYCLGSLFAK GCKMLWRFFL
KSTRVVSKDL SNKISEAADN IEEGTTAITP SAEKTENNDD DLLSFPISGL LLITVIWVIF
CAVLFTFLEE WDFGTSLYFT LISFTTIGFG DILPSDYDFM PIVGVLLLIG LSLVSTVMTL
IQQQIEALAS GMKDNIDQEY ARALNEARED GEVDEHVDPE EDPENNKKSF DAVISRMNWS
KRGLYYLLPD SQKKELAKQS EKKMGRKSIK IQTDNDLLET LIREEILKAE LNNEMHKYTA
PRSSHQPKLV YSDVREKEVP IEVVRVEHFN HGNEDYLEHD I
