KCJ15_CAVPO
ID KCJ15_CAVPO Reviewed; 375 AA.
AC O70339;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 15;
DE AltName: Full=Inward rectifier K(+) channel Kir1.3;
DE AltName: Full=Inward rectifier K(+) channel Kir4.2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 15;
GN Name=KCNJ15;
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].
RX PubMed=9727001; DOI=10.1074/jbc.273.37.23884;
RA Derst C., Wischmeyer E., Preisig-Mueller R., Spauschus A., Konrad M.,
RA Hensen P., Jeck N., Seyberth H.W., Daut J., Karschin A.;
RT "A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary
RT potassium) channels reveals a crucial residue for channel function in
RT Kir1.3 channels.";
RL J. Biol. Chem. 273:23884-23891(1998).
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 -!- 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; AF049076; AAC34748.1; -; Genomic_DNA.
DR RefSeq; XP_013001561.1; XM_013146107.1.
DR RefSeq; XP_013001562.1; XM_013146108.1.
DR RefSeq; XP_013001563.1; XM_013146109.1.
DR RefSeq; XP_013001564.1; XM_013146110.1.
DR RefSeq; XP_013001565.1; XM_013146111.1.
DR RefSeq; XP_013001566.1; XM_013146112.1.
DR RefSeq; XP_013001567.1; XM_013146113.1.
DR RefSeq; XP_013001568.1; XM_013146114.1.
DR AlphaFoldDB; O70339; -.
DR SMR; O70339; -.
DR STRING; 10141.ENSCPOP00000020472; -.
DR GeneID; 100713999; -.
DR KEGG; cpoc:100713999; -.
DR CTD; 3772; -.
DR eggNOG; KOG3827; Eukaryota.
DR HOGENOM; CLU_022738_3_3_1; -.
DR InParanoid; O70339; -.
DR OMA; LPMHRST; -.
DR OrthoDB; 956263at2759; -.
DR TreeFam; TF313676; -.
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; 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 3: Inferred from homology;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..375
FT /note="ATP-sensitive inward rectifier potassium channel 15"
FT /id="PRO_0000154971"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 64..88
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..113
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 114..125
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 126..132
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..141
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..163
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 164..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 127..132
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 157
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 42829 MW; 1ACC85D34B77CFC0 CRC64;
MDTIHMSVTR PPPEKHMAGP GLKTHRPRVM SKSGHSNVRI DKVDGIYLLY LQDLWTTVID
MKWRYKLTLF AATFVMTWFL FGVIYYAIAF IHGDLEPSEA ISNHTPCIMK VDSLTGAFLF
SLESQTTIGY GVRSITEECP HAIFLLVAQL VITTLIEIFI TGTFLAKIAR PKKRAETIKF
SHCAVITKQN GKLCLVIQVA NMRKSLLIQC QLSGKLLQTH VTKEGERILL NQATVKFHVD
SSSESPFLIL PMTFYHVLDE TSPLRDLTPQ NLKEKEFELV VLLNATVEST SAVCQSRTSY
IPEEIYWGFE FVPVVSLSKN GKYVADFSQF EQIRKSSDCT FYCADSEKQK LEEKYRQEDQ
RERELRTLLL HQSNV
