KCNJ1_RAT
ID KCNJ1_RAT Reviewed; 391 AA.
AC P35560; O88639; O88640; Q9QUR5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 1;
DE AltName: Full=ATP-regulated potassium channel ROM-K;
DE AltName: Full=Inward rectifier K(+) channel Kir1.1;
DE AltName: Full=KAB-1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 1;
GN Name=Kcnj1; Synonyms=Romk1;
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=Kidney;
RX PubMed=7680431; DOI=10.1038/362031a0;
RA Ho K., Nichols C.G., Lederer W.J., Lytton J., Vassilev P.M.,
RA Kanazirska M.V., Hebert S.C.;
RT "Cloning and expression of an inwardly rectifying ATP-regulated potassium
RT channel.";
RL Nature 362:31-38(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8166245; DOI=10.1152/ajpcell.1994.266.3.c809;
RA Zhou H., Tate S.S., Palmer L.G.;
RT "Primary structure and functional properties of an epithelial K channel.";
RL Am. J. Physiol. 266:C809-C824(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; E AND F).
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=10069985; DOI=10.1152/ajpcell.1999.276.3.c585;
RA Beesley A.H., Ortega B., White S.J.;
RT "Splicing of a retained intron within ROMK K+ channel RNA generates a novel
RT set of isoforms in rat kidney.";
RL Am. J. Physiol. 276:C585-C592(1999).
RN [4]
RP FUNCTION.
RX PubMed=9015377; DOI=10.1006/bbrc.1996.6024;
RA Derst C., Konrad M., Koeckerling A., Karolyi L., Deschenes G., Daut J.,
RA Karschin A., Seyberth H.W.;
RT "Mutations in the ROMK gene in antenatal Bartter syndrome are associated
RT with impaired K+ channel function.";
RL Biochem. Biophys. Res. Commun. 230:641-645(1997).
CC -!- FUNCTION: In the kidney, probably plays a major role in potassium
CC homeostasis. 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. Their voltage dependence is regulated by the concentration
CC of extracellular potassium; as external potassium is raised, the
CC voltage range of the channel opening shifts to more positive voltages.
CC The inward rectification is mainly due to the blockage of outward
CC current by internal magnesium. This channel is activated by internal
CC ATP and can be blocked by external barium.
CC {ECO:0000269|PubMed:9015377}.
CC -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000250|UniProtKB:P48048}.
CC -!- SUBUNIT: Interacts with SGK1 and SLC9A3R2/NHERF2.
CC {ECO:0000250|UniProtKB:P48048}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48048};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P48048}.
CC Note=Phosphorylation at Ser-44 by SGK1 is necessary for its expression
CC at the cell membrane. {ECO:0000250|UniProtKB:P48048}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=A;
CC IsoId=P35560-1; Sequence=Displayed;
CC Name=B; Synonyms=ROMK2;
CC IsoId=P35560-2; Sequence=VSP_002799;
CC Name=C; Synonyms=ROMK3;
CC IsoId=P35560-3; Sequence=VSP_002800;
CC Name=D; Synonyms=1.1, ROMK1.1;
CC IsoId=P35560-4; Sequence=VSP_002801, VSP_002802;
CC Name=E; Synonyms=3.1, ROMK3.1;
CC IsoId=P35560-5; Sequence=VSP_002800, VSP_002801, VSP_002802;
CC Name=F; Synonyms=6.1, ROMK6.1;
CC IsoId=P35560-6; Sequence=VSP_002799, VSP_002801, VSP_002802;
CC -!- TISSUE SPECIFICITY: Mainly in kidney (renal cortex, medulla and
CC papilla). In the brain, found in the cortex and the hippocampus.
CC {ECO:0000269|PubMed:8166245}.
CC -!- PTM: Phosphorylation at Ser-44 by SGK1 is necessary for its expression
CC at the cell membrane. {ECO:0000250|UniProtKB:P48048}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ1 subfamily. {ECO:0000305}.
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DR EMBL; X72341; CAA51068.1; -; mRNA.
DR EMBL; L29403; AAA50378.1; -; mRNA.
DR EMBL; S69385; AAB30553.1; -; mRNA.
DR EMBL; AF081365; AAC34443.1; -; mRNA.
DR EMBL; AF081366; AAC34444.1; -; mRNA.
DR EMBL; AF081367; AAC34445.1; -; mRNA.
DR EMBL; AF081368; AAC34446.1; -; mRNA.
DR PIR; S30046; S30046.
DR AlphaFoldDB; P35560; -.
DR SMR; P35560; -.
DR BioGRID; 246676; 1.
DR STRING; 10116.ENSRNOP00000047576; -.
DR BindingDB; P35560; -.
DR ChEMBL; CHEMBL2146350; -.
DR GuidetoPHARMACOLOGY; 429; -.
DR GlyGen; P35560; 1 site.
DR iPTMnet; P35560; -.
DR PhosphoSitePlus; P35560; -.
DR PaxDb; P35560; -.
DR PRIDE; P35560; -.
DR RGD; 2957; Kcnj1.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; P35560; -.
DR OrthoDB; 520651at2759; -.
DR PhylomeDB; P35560; -.
DR Reactome; R-RNO-1296067; Potassium transport channels.
DR PRO; PR:P35560; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:ARUK-UCL.
DR GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IDA:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IMP:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0030955; F:potassium ion binding; IMP:RGD.
DR GO; GO:0071286; P:cellular response to magnesium ion; IDA:RGD.
DR GO; GO:0072359; P:circulatory system development; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:1900128; P:regulation of G-protein activated inward rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0070294; P:renal sodium ion absorption; ISO:RGD.
DR GO; GO:0035864; P:response to potassium ion; IEP:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
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; IPR003268; K_chnl_inward-rec_Kir1.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF6; PTHR11767:SF6; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..391
FT /note="ATP-sensitive inward rectifier potassium channel 1"
FT /id="PRO_0000154919"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 78..102
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 103..127
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT INTRAMEM 128..139
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 140..146
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 147..155
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT TRANSMEM 156..177
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 178..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00180"
FT MOTIF 141..146
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 171
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:P48048"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform B and isoform F)"
FT /evidence="ECO:0000303|PubMed:10069985,
FT ECO:0000303|PubMed:8166245"
FT /id="VSP_002799"
FT VAR_SEQ 1..12
FT /note="MGASERSVFRVL -> MVSELSIPSIPTGVAGLSK (in isoform C
FT and isoform E)"
FT /evidence="ECO:0000303|PubMed:10069985"
FT /id="VSP_002800"
FT VAR_SEQ 79..124
FT /note="YKMTVFITAFLGSWFLFGLLWYVVAYVHKDLPEFYPPDNRTPCVEN -> DS
FT SDHRLRIQVCDRTVRHCHFPAYLPVYSWSDHQFLHVWCHFSQDL (in isoform D,
FT isoform E and isoform F)"
FT /evidence="ECO:0000303|PubMed:10069985"
FT /id="VSP_002801"
FT VAR_SEQ 125..391
FT /note="Missing (in isoform D, isoform E and isoform F)"
FT /evidence="ECO:0000303|PubMed:10069985"
FT /id="VSP_002802"
SQ SEQUENCE 391 AA; 44963 MW; 896FD0FD128F85D0 CRC64;
MGASERSVFR VLIRALTERM FKHLRRWFIT HIFGRSRQRA RLVSKEGRCN IEFGNVDAQS
RFIFFVDIWT TVLDLKWRYK MTVFITAFLG SWFLFGLLWY VVAYVHKDLP EFYPPDNRTP
CVENINGMTS AFLFSLETQV TIGYGFRFVT EQCATAIFLL IFQSILGVII NSFMCGAILA
KISRPKKRAK TITFSKNAVI SKRGGKLCLL IRVANLRKSL LIGSHIYGKL LKTTITPEGE
TIILDQTNIN FVVDAGNENL FFISPLTIYH IIDHNSPFFH MAAETLSQQD FELVVFLDGT
VESTSATCQV RTSYVPEEVL WGYRFVPIVS KTKEGKYRVD FHNFGKTVEV ETPHCAMCLY
NEKDARARMK RGYDNPNFVL SEVDETDDTQ M
