ID   KCJ13_CAVPO             Reviewed;         360 AA.
AC   Q9QZ65; Q9QZ64;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Kidney;
RA   Derst C.;
RT   "Cloning and sequencing of guinea pig inwardly rectifying potassium channel
RT   Kir7.1.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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; AF200713; AAF12822.1; -; mRNA.
DR   EMBL; AF200714; AAF12823.1; -; Genomic_DNA.
DR   RefSeq; NP_001166225.1; NM_001172754.1.
DR   AlphaFoldDB; Q9QZ65; -.
DR   SMR; Q9QZ65; -.
DR   STRING; 10141.ENSCPOP00000016497; -.
DR   PRIDE; Q9QZ65; -.
DR   GeneID; 100379277; -.
DR   KEGG; cpoc:100379277; -.
DR   CTD; 3769; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   InParanoid; Q9QZ65; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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_0000154965"
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;  40576 MW;  DCA9FD735C0139FB CRC64;
     MESSNCKVIT PLLSQRHRRM VTKDGHSTLQ TDGAPRGLVY LRDAWGTLID MRWRWVMLVF
     SASFVLHWLV FAVLWYVLAE MNGDLELDHD APPENHTICV KYITSFTAAF SFSLETQLTI
     GYGTMFPSGD CPSAIALLAI QMLLGLMLEA FITGAFVAKI ARPKNRAFSI RFTDLAVVAH
     RDGKPNLIFQ VANIRHSPLT SVRVSAVLYQ ERENGQLHQT SVDFHLDGIS SEECPFFIFP
     LTYYHSITPS SPLVTLLQHE NPPHFELVVF LSAMQEGTGE ICQRRTSYLP SEIMLHHCFA
     SLLTRGSKGE YKVKMENFDK TVPELPTPLV SKSPHRTDLD IRINGQSIDN FQISETGLTE