ID IRK1_CAEEL Reviewed; 544 AA.
AC P52192;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Inward rectifier potassium channel irk-1;
GN Name=irk-1; Synonyms=irk-4; ORFNames=R03E9.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23152612; DOI=10.1523/jneurosci.2667-12.2012;
RA Emtage L., Aziz-Zaman S., Padovan-Merhar O., Horvitz H.R., Fang-Yen C.,
RA Ringstad N.;
RT "IRK-1 potassium channels mediate peptidergic inhibition of Caenorhabditis
RT elegans serotonin neurons via a G(o) signaling pathway.";
RL J. Neurosci. 32:16285-16295(2012).
CC -!- FUNCTION: Inward rectifier potassium channels are characterized by a
CC greater tendency to allow potassium to flow into the cell rather than
CC out of it. Required for modulation of the activity of the
CC hermaphrodite-specific neurons (HSNs) by the G-protein coupled
CC neuropeptide receptor egl-6 which in turn controls egg-laying behavior.
CC {ECO:0000269|PubMed:23152612}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Perikaryon {ECO:0000269|PubMed:23152612}. Cell
CC projection {ECO:0000269|PubMed:23152612}. Note=Detected in perikarya
CC and neurites of HSNs.
CC -!- TISSUE SPECIFICITY: Expressed in neurons in the head and tail with no
CC expression detected in non-neuronal cells in these regions. Also
CC detected in the egg-laying system of adult hermaphordites with strong
CC expression in the HSN motor neurons and weak expression in vulval
CC muscles. {ECO:0000269|PubMed:23152612}.
CC -!- DISRUPTION PHENOTYPE: Strongly suppresses the egg-laying defect caused
CC by a mutant form of egl-6. Very mild defect in egg-laying behavior when
CC deleted in a wild-type background. {ECO:0000269|PubMed:23152612}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. {ECO:0000305}.
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DR EMBL; FO081560; CCD72424.2; -; Genomic_DNA.
DR EMBL; FO081559; CCD72424.2; JOINED; Genomic_DNA.
DR PIR; T28859; T28859.
DR RefSeq; NP_509138.2; NM_076737.2.
DR AlphaFoldDB; P52192; -.
DR SMR; P52192; -.
DR STRING; 6239.R03E9.4.1; -.
DR EPD; P52192; -.
DR PaxDb; 6239-R03E9-4; -.
DR EnsemblMetazoa; R03E9.4.1; R03E9.4.1; WBGene00002149.
DR EnsemblMetazoa; R03E9.4.2; R03E9.4.2; WBGene00002149.
DR GeneID; 180944; -.
DR KEGG; cel:CELE_R03E9.4; -.
DR UCSC; R03E9.4; c. elegans.
DR AGR; WB:WBGene00002149; -.
DR WormBase; R03E9.4; CE47227; WBGene00002149; irk-1.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01080000257365; -.
DR HOGENOM; CLU_022738_10_0_1; -.
DR InParanoid; P52192; -.
DR OMA; EVAFMDK; -.
DR OrthoDB; 4126787at2759; -.
DR PhylomeDB; P52192; -.
DR Reactome; R-CEL-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-CEL-1296053; Classical Kir channels.
DR Reactome; R-CEL-1296067; Potassium transport channels.
DR Reactome; R-CEL-5576886; Phase 4 - resting membrane potential.
DR Reactome; R-CEL-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P52192; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002149; Expressed in larva and 3 other cell types or tissues.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IMP:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0046662; P:regulation of egg-laying behavior; IMP:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR041647; IRK_C.
DR InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR PANTHER; PTHR11767:SF51; INWARD RECTIFIER POTASSIUM CHANNEL IRK-1; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..544
FT /note="Inward rectifier potassium channel irk-1"
FT /id="PRO_0000154979"
FT TOPO_DOM 1..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..134
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 135..158
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 159..170
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 171..177
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 178..186
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 187..208
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 209..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 411..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..177
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 433..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 61338 MW; 37177B7FB4ED37D6 CRC64;
MTLSVPDCAE MNRIRMSNHR KMSLGSAPLI ANGRPSPPPR RTSLAESIRT LAFTARRNSS
PLYRKSTKKL KKSRLVGKNG ICNVYNTNVP KKDRQYLRDI FTTMIDVKWR WMLMLFASAF
VLSWSIFGTT YYLIALVHGD LSLPTPVNHT ACVMNLDSVY SSFLFAVETH HTIGYGHRYI
TTECYLAGAI VCLQAICALL LQSFMVGIVF AKMARPKKRA ETIIFSDKAV ICLRDGQLCF
LCRVGDMRNT HLVEAHVRLQ FITDRETNEG EIEPLHQFEM KVGPSIADDD RLFLVWPTTL
CHVIDSRSPL YNYNQQTLMS AQFEIIVLLE GIVESTGMTA QAKTSYLPSE VLWGHRFRKL
VTYQRSNGSY QIDYDLFHST YPVRTPAMSP AEFYSSKPNL KDYYCHDSHE HKLEDNRSSD
STPLPSPSPY SYPSTPLNHF QSSSNSPVFS NNHSKFNTEA VTCEAGMLCP PTIVVQCPST
CASPNHMRRT RNQMDKSRTS SSCDLTRPST ALSDLEEECS DSGSPTKCQS PPVVPIHIEI
VSET
//
