位置:首页 > 蛋白库 > IRK1_CAEEL
IRK1_CAEEL
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   03-AUG-2022, entry version 144.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; -.
DR   EPD; P52192; -.
DR   PaxDb; P52192; -.
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   CTD; 180944; -.
DR   WormBase; R03E9.4; CE47227; WBGene00002149; irk-1.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT01040000240379; -.
DR   HOGENOM; CLU_022738_10_0_1; -.
DR   InParanoid; P52192; -.
DR   OMA; SKDGHCN; -.
DR   OrthoDB; 956263at2759; -.
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 tissues.
DR   GO; GO:0016021; C:integral component of membrane; 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:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0046662; P:regulation of oviposition; IMP:UniProtKB.
DR   Gene3D; 2.60.40.1400; -; 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; PTHR11767; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024