SUP9_CAEEL
ID SUP9_CAEEL Reviewed; 329 AA.
AC O17185; O76795;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Two pore potassium channel protein sup-9;
DE AltName: Full=Suppressor of unc-93 protein 9;
DE AltName: Full=n2P38;
GN Name=sup-9 {ECO:0000312|WormBase:F34D6.3}; ORFNames=F34D6.3;
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:AAQ84518.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF MET-1; GLY-22; ALA-23;
RP VAL-41; VAL-44; ASP-58; ILE-61; ALA-74; ILE-94; GLY-95; PRO-101; THR-103;
RP GLY-106; PHE-109; PRO-119; GLY-121; LEU-122; TRP-165; GLY-172; GLY-173;
RP ALA-174; GLU-181; TYR-190; THR-195; GLY-200; GLY-202; ASP-203; PHE-226;
RP GLY-230; SER-235; ALA-236 AND VAL-242.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:14534247};
RX PubMed=14534247; DOI=10.1523/jneurosci.23-27-09133.2003;
RA de la Cruz I.P., Levin J.Z., Cummins C., Anderson P., Horvitz H.R.;
RT "sup-9, sup-10, and unc-93 may encode components of a two-pore K+ channel
RT that coordinates muscle contraction in Caenorhabditis elegans.";
RL J. Neurosci. 23:9133-9145(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC32863.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Z.-W., Salkoff L.;
RT "Potassium channels in C. elegans.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=11301195; DOI=10.1016/s0306-4522(01)00079-3;
RA Salkoff L., Butler A., Fawcett G., Kunkel M., McArdle C., Paz-y-Mino G.,
RA Nonet M., Walton N., Wang Z.-W., Yuan A., Wei A.;
RT "Evolution tunes the excitability of individual neurons.";
RL Neuroscience 103:853-859(2001).
RN [5]
RP FUNCTION, REGION, AND MUTAGENESIS OF ASP-27; THR-100; LEU-122; ARG-244;
RP SER-292; SER-294 AND LEU-303.
RX PubMed=24586202; DOI=10.1371/journal.pgen.1004175;
RA de la Cruz I.P., Ma L., Horvitz H.R.;
RT "The Caenorhabditis elegans iodotyrosine deiodinase ortholog SUP-18
RT functions through a conserved channel SC-box to regulate the muscle two-
RT pore domain potassium channel SUP-9.";
RL PLoS Genet. 10:E1004175-E1004175(2014).
CC -!- FUNCTION: Potassium channel involved in coordination of muscle
CC contraction (PubMed:14534247). Activity is regulated by sup-18
CC (PubMed:24586202). {ECO:0000269|PubMed:14534247,
CC ECO:0000269|PubMed:24586202}.
CC -!- SUBUNIT: May form a complex with the regulatory subunits unc-93 and
CC sup-10. {ECO:0000303|PubMed:14534247}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Associated with dense bodies.
CC {ECO:0000269|PubMed:14534247}.
CC -!- TISSUE SPECIFICITY: Low levels along surface of body-wall muscle cells,
CC in vulval and intestinal muscles and, more weakly, in anal depressor
CC and sphincter muscles. Also expressed in a subset of head neurons.
CC {ECO:0000269|PubMed:11301195, ECO:0000269|PubMed:14534247}.
CC -!- DEVELOPMENTAL STAGE: Expressed in body wall muscles from 3.5-fold stage
CC of embryogenesis with highest levels in late embryos and L1 stage
CC larvae. Lower levels persist to adulthood.
CC {ECO:0000269|PubMed:14534247}.
CC -!- MISCELLANEOUS: Uncoordinated rubber band response is phenocopied by
CC exposure to the unc-49 agonist muscimol. {ECO:0000269|PubMed:14534247}.
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; AY357729; AAQ84518.1; -; mRNA.
DR EMBL; AF083652; AAC32863.1; -; mRNA.
DR EMBL; FO081204; CCD69862.1; -; Genomic_DNA.
DR PIR; T32347; T32347.
DR PIR; T43509; T43509.
DR RefSeq; NP_494333.1; NM_061932.3.
DR AlphaFoldDB; O17185; -.
DR SMR; O17185; -.
DR STRING; 6239.F34D6.3; -.
DR TCDB; 1.A.1.9.7; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; O17185; -.
DR EnsemblMetazoa; F34D6.3.1; F34D6.3.1; WBGene00006318.
DR GeneID; 173613; -.
DR KEGG; cel:CELE_F34D6.3; -.
DR UCSC; F34D6.3; c. elegans.
DR CTD; 173613; -.
DR WormBase; F34D6.3; CE28297; WBGene00006318; sup-9.
DR eggNOG; KOG4404; Eukaryota.
DR GeneTree; ENSGT00940000166380; -.
DR HOGENOM; CLU_022504_4_0_1; -.
DR InParanoid; O17185; -.
DR OMA; TAWFGQV; -.
DR OrthoDB; 1109218at2759; -.
DR PhylomeDB; O17185; -.
DR Reactome; R-CEL-1299316; TWIK-releated acid-sensitive K+ channel (TASK).
DR Reactome; R-CEL-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:O17185; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006318; Expressed in embryo and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0036195; C:muscle cell projection membrane; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; TAS:UniProtKB.
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:0006813; P:potassium ion transport; TAS:UniProtKB.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01095; TASKCHANNEL.
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..329
FT /note="Two pore potassium channel protein sup-9"
FT /id="PRO_0000101770"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 80..100
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 186..206
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 289..296
FT /note="May be important for regulation by and/or
FT interaction with sup-10"
FT /evidence="ECO:0000303|PubMed:24586202"
FT REGION 307..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 93..98
FT /note="Selectivity filter"
FT /evidence="ECO:0000255"
FT MOTIF 198..203
FT /note="Selectivity filter"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1
FT /note="M->I: In n2282; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 22
FT /note="G->E: In n213; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 23
FT /note="A->V: In lr129; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 27
FT /note="D->N: In n4265 and n3975; loss of function. Not
FT required for sup-18 mediated regulation."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 41
FT /note="V->A: In n1472; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 44
FT /note="V->E: In n233; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 58
FT /note="D->V: In n2291; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 61
FT /note="I->S: In lr35; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 74
FT /note="A->V: In n1025; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 94
FT /note="I->N: In n1016; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 95
FT /note="G->D: In n1020 and n2354; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 100
FT /note="T->I: In n3976; loss of function. Not required for
FT sup-18 mediated regulation."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 101
FT /note="P->S: In n190, n598, n2353 and n2356; loss of
FT function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 103
FT /note="T->I: In n2347; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 106
FT /note="G->E: In n1009; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 106
FT /note="G->R: In n2351; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 109
FT /note="F->S: In lr45; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 119
FT /note="P->S: In n2281 and n2345; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 121
FT /note="G->R: In lr100; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 122
FT /note="L->F: In n264 and n3977; loss of function. Not
FT required for sup-18 mediated regulation."
FT /evidence="ECO:0000269|PubMed:14534247,
FT ECO:0000269|PubMed:24586202"
FT MUTAGEN 165
FT /note="W->R: In lr38; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 172
FT /note="G->E: In n219; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 172
FT /note="G->R: In n223 and n2355; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 173
FT /note="G->E: In n2288; partial loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 173
FT /note="G->R: In n2294 and n2296; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 174
FT /note="A->T: In n2359; partial loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 181
FT /note="E->K: In n2350; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 190
FT /note="Y->F: In n2352; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 195
FT /note="T->I: In n2278 and n2343; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 200
FT /note="G->E: In n191, n2283 and n2286; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 202
FT /note="G->D: In n2344; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 202
FT /note="G->S: In n1469; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 203
FT /note="D->A: In lr1; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 203
FT /note="D->N: In n2346 and n2349; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 226
FT /note="F->S: In n1557; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 230
FT /note="G->E: In n2176; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 230
FT /note="G->R: In n2348; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 235
FT /note="S->F: In n189 and n2358; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 236
FT /note="A->M: In n2360 and n2361; partial loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 236
FT /note="A->T: In n1550, n3310, e2655 and 2661; gain of
FT function, uncoordinated rubber band response in
FT heterozygous mutants, inviable in homozygous mutants."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 242
FT /note="V->M: In lr142; loss of function."
FT /evidence="ECO:0000269|PubMed:14534247"
FT MUTAGEN 244
FT /note="R->W: In n3935; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 292
FT /note="S->A: In n4259; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 292
FT /note="S->F: In n1435, n3942, n4253 and n4254; loss of
FT function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 293
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 294
FT /note="S->A: In n4262; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 295
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 296
FT /note="Y->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
FT MUTAGEN 303
FT /note="L->P: In n4269; loss of function."
FT /evidence="ECO:0000269|PubMed:24586202"
SQ SEQUENCE 329 AA; 36992 MW; 338A6D9A577464CD CRC64;
MKRQNIRTLS LIVCTLTYLL VGAAVFDALE TENEILQRKL VQRVREKLKT KYNMSNADYE
ILEATIVKSV PHKAGYQWKF SGAFYFATTV ITTIGYGHST PMTDAGKVFC MLYALAGIPL
GLIMFQSIGE RMNTFAAKLL RFIRRAAGKQ PIVTSSDLII FCTGWGGLLI FGGAFMFSSY
ENWTYFDAVY YCFVTLTTIG FGDYVALQKR GSLQTQPEYV FFSLVFILFG LTVISAAMNL
LVLRFLTMNT EDERRDEQEA ILAAQGLVRV GDPTADDDFG RLPLSDNVSL ASCSCYQLPD
EKLRHRHRKH TEPHGGPPTF SGMTTRPKY
