TWK12_CAEEL
ID TWK12_CAEEL Reviewed; 713 AA.
AC Q19907;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=TWiK family of potassium channels protein 12;
GN Name=twk-12; ORFNames=F29F11.4;
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:0000312|EMBL:CAA98271.2}
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 [2] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53 AND ASN-77, AND
RP IDENTIFICATION BY MASS 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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; Z73974; CAA98271.2; -; Genomic_DNA.
DR PIR; T21551; T21551.
DR RefSeq; NP_505731.3; NM_073330.4.
DR AlphaFoldDB; Q19907; -.
DR BioGRID; 56566; 1.
DR TCDB; 1.A.1.9.9; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q19907; -.
DR EPD; Q19907; -.
DR PaxDb; Q19907; -.
DR EnsemblMetazoa; F29F11.4.1; F29F11.4.1; WBGene00006667.
DR GeneID; 192074; -.
DR KEGG; cel:CELE_F29F11.4; -.
DR UCSC; F29F11.4; c. elegans.
DR CTD; 192074; -.
DR WormBase; F29F11.4; CE48353; WBGene00006667; twk-12.
DR eggNOG; KOG1418; Eukaryota.
DR InParanoid; Q19907; -.
DR OrthoDB; 1171809at2759; -.
DR Reactome; R-CEL-1299344; TWIK-related spinal cord K+ channel (TRESK).
DR Reactome; R-CEL-1299361; TWIK-related alkaline pH activated K+ channel (TALK).
DR Reactome; R-CEL-1299503; TWIK related potassium channel (TREK).
DR Reactome; R-CEL-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:Q19907; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00006667; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 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..713
FT /note="TWiK family of potassium channels protein 12"
FT /id="PRO_0000390697"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 112..132
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 267..287
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 713 AA; 82068 MW; FC97140E09FC45B0 CRC64;
MTLFKKIQWF CNLIRLRSYY KFLLLIAYTA FGAWLFRTYE LQADIKRRSV FGNTTNLVRR
QLAERWIEMH KDAVLRNDSA LRFRRAAEAV EWLLDELNLS DHIRDLSEET PWTWTGAMFY
AGQLYTTIGY GYPTTKTDEG RICTIFYALF GIPCFLMYLK IENAIEWKKD KQLGKRALKM
HGLINDSFQS IGKTLSKKMK KYYKKLRRSR VGRILLPTRV TAMKDGFEDP EAAEERKKKP
FPIPIAIIML IIWICFSASM FCIWEDTWVF SSAVYFFIVS ISTVGLGDML FRTPDMMVFN
FLLILVGLAL LSMCFELITD RVAKWKQKRF DEHIKKVQKM AFQVFEKDPF IEEAPPLGIR
MAPNLMQIAA THVSEEKRGF FAEFKDWFAG KVTDNVIQSK LEDSDDESDS EEALEEFDSP
QIATVTANDL IVCSNGAATR RVSKQSYALS DISNLSNSKI LPGNNYGQLL DRIKAMEKFK
PKKNDLDSRM FAKFLENKKL AKILEQTELR ELATVSCQTD LSGLVVQRRN PKGRHARIGS
CSSQSTMSTL LPNKMHAPDE DSVMSFTFGD LKFDYKTEPF IDEYYIRESN HSIFDFDEDE
TVRIPQKMLI SRPGMPPPPP SRPLNLASPL RTLLEKEQKY DEDPEIQLTP RRLNSLSDIQ
ARKVKLGVDE NLQHARLVCG LLPQDFDSPS TSTSTSMIDS GYELSKRDAS TMA
