KCJ15_RAT
ID KCJ15_RAT Reviewed; 405 AA.
AC Q91ZF1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 15;
DE AltName: Full=Inward rectifier K(+) channel Kir4.2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 15;
GN Name=Kcnj15;
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] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley;
RX PubMed=11804844; DOI=10.1152/ajpgi.00256.2001;
RA Hill C.E., Briggs M.M., Liu J., Magtanong L.;
RT "Cloning, expression, and localization of a rat hepatocyte inwardly
RT rectifying potassium channel.";
RL Am. J. Physiol. 282:G233-G240(2002).
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. 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PATJ. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Kir4.2a;
CC IsoId=Q91ZF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZF1-2; Sequence=VSP_011687;
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ15 subfamily. {ECO:0000305}.
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DR EMBL; AY028455; AAK20928.1; -; mRNA.
DR RefSeq; NP_579855.1; NM_133321.2. [Q91ZF1-1]
DR RefSeq; XP_006248190.1; XM_006248128.3. [Q91ZF1-1]
DR RefSeq; XP_006248191.1; XM_006248129.3. [Q91ZF1-1]
DR RefSeq; XP_006248193.1; XM_006248131.3. [Q91ZF1-1]
DR RefSeq; XP_006248194.1; XM_006248132.3. [Q91ZF1-1]
DR RefSeq; XP_006248195.1; XM_006248133.3. [Q91ZF1-1]
DR RefSeq; XP_006248197.1; XM_006248135.2. [Q91ZF1-1]
DR RefSeq; XP_006248201.1; XM_006248139.3. [Q91ZF1-2]
DR RefSeq; XP_006248203.1; XM_006248141.3. [Q91ZF1-2]
DR RefSeq; XP_008766772.1; XM_008768550.2. [Q91ZF1-1]
DR RefSeq; XP_008766773.1; XM_008768551.2. [Q91ZF1-1]
DR RefSeq; XP_008766774.1; XM_008768552.2. [Q91ZF1-1]
DR RefSeq; XP_008766775.1; XM_008768553.2. [Q91ZF1-1]
DR RefSeq; XP_017453350.1; XM_017597861.1. [Q91ZF1-1]
DR RefSeq; XP_017453351.1; XM_017597862.1. [Q91ZF1-1]
DR RefSeq; XP_017453352.1; XM_017597863.1. [Q91ZF1-1]
DR AlphaFoldDB; Q91ZF1; -.
DR SMR; Q91ZF1; -.
DR STRING; 10116.ENSRNOP00000002259; -.
DR GuidetoPHARMACOLOGY; 439; -.
DR TCDB; 1.A.2.1.4; the inward rectifier k(+) channel (irk-c) family.
DR PaxDb; Q91ZF1; -.
DR Ensembl; ENSRNOT00000094937; ENSRNOP00000092361; ENSRNOG00000062944. [Q91ZF1-2]
DR Ensembl; ENSRNOT00000099760; ENSRNOP00000091174; ENSRNOG00000062944. [Q91ZF1-2]
DR Ensembl; ENSRNOT00000104151; ENSRNOP00000089124; ENSRNOG00000062944. [Q91ZF1-2]
DR Ensembl; ENSRNOT00000108557; ENSRNOP00000078466; ENSRNOG00000062944. [Q91ZF1-2]
DR Ensembl; ENSRNOT00000111269; ENSRNOP00000087933; ENSRNOG00000062944. [Q91ZF1-2]
DR Ensembl; ENSRNOT00000111664; ENSRNOP00000093558; ENSRNOG00000062944. [Q91ZF1-2]
DR Ensembl; ENSRNOT00000113883; ENSRNOP00000097650; ENSRNOG00000062944. [Q91ZF1-2]
DR Ensembl; ENSRNOT00000118577; ENSRNOP00000077685; ENSRNOG00000062944. [Q91ZF1-2]
DR GeneID; 170847; -.
DR KEGG; rno:170847; -.
DR UCSC; RGD:621662; rat. [Q91ZF1-1]
DR CTD; 3772; -.
DR RGD; 621662; Kcnj15.
DR VEuPathDB; HostDB:ENSRNOG00000062944; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_3_3_1; -.
DR InParanoid; Q91ZF1; -.
DR OMA; LPMHRST; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q91ZF1; -.
DR TreeFam; TF313676; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:Q91ZF1; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001656; Expressed in adult mammalian kidney and 12 other tissues.
DR Genevisible; Q91ZF1; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:RGD.
DR GO; GO:0005267; F:potassium channel activity; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
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; IPR003270; K_chnl_inward-rec_Kir1.3.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF20; PTHR11767:SF20; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01323; KIR13CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..405
FT /note="ATP-sensitive inward rectifier potassium channel 15"
FT /id="PRO_0000154974"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 94..118
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..143
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 144..155
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 156..162
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 163..171
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 172..193
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 194..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 157..162
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 187
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11804844"
FT /id="VSP_011687"
SQ SEQUENCE 405 AA; 45908 MW; 77C0BEB7C6785E5D CRC64;
MVARWVKGSE DAPLALQKIP DLQSGPRSLR MEAIHIGMSS APLVKHSNGV GLKAHRPRVM
SKSGHSNVRI DKVDGIYLLY LQDLWTTVID MKWRYKLTLF AATFVMTWFL FGVVYYAIAF
IHGDLELGES NSNHTPCIMK VDSLTGAFLF SLESQTTIGY GVRSITEECP HAIFLLVAQL
VITTLIEIFI TGTFLAKIAR PKKRAETIKF SHCAVISKQN GKLCLVIQVA NMRKSLLIQC
QLSGKLLQTH VTKEGERILL NQATVKFHVD SSSESPFLIL PMTFYHVLDE TSPLRDLTPQ
NLKEKEFELV VLLNATVEST SAVCQSRTSY IPEEIYWGFE FVPVVSLSKN GKYVADFSQF
EQIRKSPDCT FYCADSEKQK LEEQYRQEDQ RERELRSLLL QQSNV
