ID   KCJ13_RAT               Reviewed;         360 AA.
AC   O70617;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Inward rectifier potassium channel 13;
DE   AltName: Full=Inward rectifier K(+) channel Kir7.1;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 13;
GN   Name=Kcnj13;
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.
RC   TISSUE=Brain;
RA   Doering F., Derst C., Wischmeyer E., Karschin C., Daut J., Karschin A.;
RT   "Unique epithelial Kir7.1 subunit defines a new subfamily of inwardly
RT   rectifying potassium channels.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Hirose S., Suzuki Y., Nakamura N.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=10871613; DOI=10.1074/jbc.m003734200;
RA   Nakamura N., Suzuki Y., Ikeda Y., Notoya M., Hirose S.;
RT   "Complex structure and regulation of expression of the rat gene for inward
RT   rectifier potassium channel Kir7.1.";
RL   J. Biol. Chem. 275:28276-28284(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=11042260; DOI=10.1016/s0014-5793(00)02092-5;
RA   Doering F., Karschin A.;
RT   "Genomic structure and promoter analysis of the rat Kir7.1 potassium
RT   channel gene (Kcnj13).";
RL   FEBS Lett. 483:93-98(2000).
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. KCNJ13 has a very low single channel
CC       conductance, low sensitivity to block by external barium and cesium,
CC       and no dependence of its inward rectification properties on the
CC       internal blocking particle magnesium.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylation at Ser-201 by PKC strongly inhibits ionic
CC       currents, while phosphorylation at Ser-287 by PKA increases them.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC       1.A.2.1) family. KCNJ13 subfamily. {ECO:0000305}.
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DR   EMBL; AJ006129; CAA06879.1; -; mRNA.
DR   EMBL; AB013890; BAA28272.1; -; mRNA.
DR   EMBL; AB034241; BAA97255.1; -; Genomic_DNA.
DR   EMBL; AJ292748; CAC17469.1; -; Genomic_DNA.
DR   RefSeq; NP_446060.1; NM_053608.2.
DR   RefSeq; XP_008765523.1; XM_008767301.2.
DR   AlphaFoldDB; O70617; -.
DR   SMR; O70617; -.
DR   STRING; 10116.ENSRNOP00000021507; -.
DR   PaxDb; O70617; -.
DR   Ensembl; ENSRNOT00000021507; ENSRNOP00000021507; ENSRNOG00000016057.
DR   GeneID; 94341; -.
DR   KEGG; rno:94341; -.
DR   UCSC; RGD:621661; rat.
DR   CTD; 3769; -.
DR   RGD; 621661; Kcnj13.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT00990000203615; -.
DR   HOGENOM; CLU_022738_3_3_1; -.
DR   InParanoid; O70617; -.
DR   OMA; QGQTCLM; -.
DR   OrthoDB; 956263at2759; -.
DR   PhylomeDB; O70617; -.
DR   TreeFam; TF313676; -.
DR   PRO; PR:O70617; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000016057; Expressed in duodenum and 14 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
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; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR008062; KCNJ13.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF3; PTHR11767:SF3; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01679; KIR7CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..360
FT                   /note="Inward rectifier potassium channel 13"
FT                   /id="PRO_0000154967"
FT   TOPO_DOM        1..53
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        54..78
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        79..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        106..117
FT                   /note="Helical; Pore-forming; Name=H5"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        118..124
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        125..133
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        134..155
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        156..360
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOTIF           119..124
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   SITE            149
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         201
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:O60928"
FT   MOD_RES         287
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:O60928"
SQ   SEQUENCE   360 AA;  40637 MW;  B3D2F6CB8F99FD16 CRC64;
     MDSRNCKVNA PLLSQRYRRM VTKDGHSTLQ MDGAQRGLVY LRDAWGILMD MRWRWMMLVF
     SASFVVHWLV FAVLWYAVAE MNGDLEIDHD VPPENHTICV KHITSFTAAF SFSLETQLTI
     GYGTMFPSGD CPSAIALLAI QMLLGLMLEA FITGAFVAKI ARPKNRAFSI RFTDLAVVAH
     KDGKPNLIFQ VANTRPSPLT SVRVSAVLYQ ERENGELYQT SVDFHLDGIS SEECPFFIFP
     LTYYHTITPS SPLATLLQHE TPSHFELVVF LSAMQEGTGE ICQRRTSYLP SEIMLHHRFA
     ALMTRGSKGE YQVKMENFDK TVPEHPTPVV SKSPHRTDLD IHINGQSIDN FQIAETGLTE