KCNK3_RAT
ID KCNK3_RAT Reviewed; 411 AA.
AC O54912;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Potassium channel subfamily K member 3;
DE AltName: Full=Acid-sensitive potassium channel protein TASK-1;
DE AltName: Full=TWIK-related acid-sensitive K(+) channel 1;
DE AltName: Full=Two pore potassium channel KT3.1;
DE Short=Two pore K(+) channel KT3.1;
GN Name=Kcnk3; Synonyms=Task, Task1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RX PubMed=9437008; DOI=10.1523/jneurosci.18-03-00868.1998;
RA Leonoudakis D., Gray A.T., Winegar B.D., Kindler C.H., Harada M.,
RA Taylor D.M., Chavez R.A., Forsayeth J.R., Yost C.S.;
RT "An open rectifier potassium channel with two pore domains in tandem cloned
RT from rat cerebellum.";
RL J. Neurosci. 18:868-877(1998).
CC -!- FUNCTION: pH-dependent, voltage-insensitive, background potassium
CC channel protein. Rectification direction results from potassium ion
CC concentration on either side of the membrane. Acts as an outward
CC rectifier when external potassium concentration is low. When external
CC potassium concentration is high, current is inward.
CC {ECO:0000250|UniProtKB:O14649}.
CC -!- SUBUNIT: Homodimer. Heterodimer with KCNK1.
CC {ECO:0000250|UniProtKB:O14649}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14649};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}.
CC -!- TISSUE SPECIFICITY: Strongest expression in heart. Moderate expression
CC in lung and brain. Low levels in liver, kidney and skeletal muscle.
CC -!- MISCELLANEOUS: Inhibited by extracellular acidification, zinc,
CC bupivacaine and phenytoin. Activated by protein kinase A.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
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DR EMBL; AF031384; AAC39952.1; -; mRNA.
DR RefSeq; NP_203694.1; NM_033376.1.
DR AlphaFoldDB; O54912; -.
DR SMR; O54912; -.
DR DIP; DIP-61121N; -.
DR IntAct; O54912; 2.
DR STRING; 10116.ENSRNOP00000013107; -.
DR BindingDB; O54912; -.
DR ChEMBL; CHEMBL4294; -.
DR GuidetoPHARMACOLOGY; 515; -.
DR GlyGen; O54912; 1 site.
DR PhosphoSitePlus; O54912; -.
DR PaxDb; O54912; -.
DR ABCD; O54912; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000108628; ENSRNOP00000079208; ENSRNOG00000009790.
DR GeneID; 29553; -.
DR KEGG; rno:29553; -.
DR CTD; 3777; -.
DR RGD; 61997; Kcnk3.
DR eggNOG; KOG4404; Eukaryota.
DR GeneTree; ENSGT00940000158248; -.
DR HOGENOM; CLU_022504_4_0_1; -.
DR InParanoid; O54912; -.
DR OMA; TCMEQSH; -.
DR OrthoDB; 1109218at2759; -.
DR PhylomeDB; O54912; -.
DR TreeFam; TF313947; -.
DR Reactome; R-RNO-1299316; TWIK-releated acid-sensitive K+ channel (TASK).
DR Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:O54912; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000009790; Expressed in heart and 17 other tissues.
DR ExpressionAtlas; O54912; baseline and differential.
DR Genevisible; O54912; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005216; F:ion channel activity; ISO:RGD.
DR GO; GO:0005252; F:open rectifier potassium channel activity; IDA:RGD.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0044548; F:S100 protein binding; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:RGD.
DR GO; GO:0071294; P:cellular response to zinc ion; IEP:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IMP:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:0060075; P:regulation of resting membrane potential; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:RGD.
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 InterPro; IPR005406; KCNK3.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR PANTHER; PTHR11003:SF138; PTHR11003:SF138; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01584; TASK1CHANNEL.
DR PRINTS; PR01095; TASKCHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..411
FT /note="Potassium channel subfamily K member 3"
FT /id="PRO_0000101746"
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 78..101
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..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 184..207
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 45276 MW; D2778016E09E2BF5 CRC64;
MKRQNVRTLA LIVCTFTYLL VGAAVFDALE SEPEMIERQR LELRQLELRA RYNLSEGGYE
ELERVVLRLK PHKAGVQWRF AGSFYFAITV ITTIGYGHAA PSTDGGKVFC MFYALLGIPL
TLVMFQSLGE RINTFVRYLL HRAKRGLGMR HAEVSMANMV LIGFVSCIST LCIGAAAFSY
YERWTFFQAY YYCFITLTTI GFGDYVALQK DQALQTQPQY VAFSFVYILT GLTVIGAFLN
LVVLRFMTMN AEDEKRDAEH RALLTHNGQA GGLGGLSCLS GSLGDGVRPR DPVTCAAAAG
GMGVGVGVGG SGFRNVYAEM LHFQSMCSCL WYKSREKLQY SIPMIIPRDL STSDTCVEHS
HSSPGGGGRY SDTPSHPCLC SGTQRSAISS VSTGLHSLAT FRGLMKRRSS V
