KCNJ9_RAT
ID KCNJ9_RAT Reviewed; 393 AA.
AC Q63511;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=G protein-activated inward rectifier potassium channel 3;
DE Short=GIRK-3;
DE AltName: Full=Inward rectifier K(+) channel Kir3.3;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 9;
GN Name=Kcnj9; Synonyms=Girk3;
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=Brain;
RX PubMed=8670306; DOI=10.1006/bbrc.1996.0918;
RA Dissmann E., Wischmeyer E., Spauschus A., Pfeil D.V., Karschin C.,
RA Karschin A.;
RT "Functional expression and cellular mRNA localization of a G protein-
RT activated K+ inward rectifier isolated from rat brain.";
RL Biochem. Biophys. Res. Commun. 223:474-479(1996).
RN [2]
RP SEQUENCE REVISION.
RA Dissmann E., Wischmeyer E., Spauschus A., Pfeil D.V., Karschin C.,
RA Karschin A.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH SNX27, AND MUTAGENESIS OF 390-GLU--VAL-393; LYS-392 AND
RP VAL-393.
RX PubMed=17828261; DOI=10.1038/nn1953;
RA Lunn M.L., Nassirpour R., Arrabit C., Tan J., McLeod I., Arias C.M.,
RA Sawchenko P.E., Yates J.R. III, Slesinger P.A.;
RT "A unique sorting nexin regulates trafficking of potassium channels via a
RT PDZ domain interaction.";
RL Nat. Neurosci. 10:1249-1259(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 388-393 IN COMPLEX WITH SNX27,
RP INTERACTION WITH SNX27, AND MUTAGENESIS OF 388-GLU-SER-389.
RX PubMed=21422294; DOI=10.1073/pnas.1018645108;
RA Balana B., Maslennikov I., Kwiatkowski W., Stern K.M., Bahima L., Choe S.,
RA Slesinger P.A.;
RT "Mechanism underlying selective regulation of G protein-gated inwardly
RT rectifying potassium channels by the psychostimulant-sensitive sorting
RT nexin 27.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5831-5836(2011).
CC -!- FUNCTION: This receptor is controlled by G proteins. Inward rectifier
CC potassium channels are characterized by a greater tendency to allow
CC potassium to flow into the cell rather than out of it. Their voltage
CC dependence is regulated by the concentration of extracellular
CC potassium; as external potassium is raised, the voltage range of the
CC channel opening shifts to more positive voltages. The inward
CC rectification is mainly due to the blockage of outward current by
CC internal magnesium (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with GIRK1 to form a G-protein-activated
CC heteromultimer pore-forming unit (By similarity). Interacts (via PDZ-
CC binding motif) with SNX27 (via PDZ domain); the interaction is required
CC when endocytosed to prevent degradation in lysosomes and promote
CC recycling to the plasma membrane. {ECO:0000250,
CC ECO:0000269|PubMed:17828261, ECO:0000269|PubMed:21422294}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The PDZ-binding motif specifically binds the PDZ domain of
CC SNX27: the specificity for SNX27 is provided by the 2 residues located
CC upstream (Glu-388 and Ser-389) of the PDZ-binding motif
CC (PubMed:17828261, PubMed:21422294). {ECO:0000269|PubMed:17828261,
CC ECO:0000269|PubMed:21422294}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ9 subfamily. {ECO:0000305}.
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DR EMBL; L77929; AAB95433.1; -; mRNA.
DR RefSeq; NP_446286.1; NM_053834.1.
DR PDB; 3QDO; X-ray; 1.88 A; A=388-393.
DR PDB; 3QE1; X-ray; 1.68 A; A=388-393.
DR PDB; 3QGL; X-ray; 3.31 A; F/G/H/I/J=388-393.
DR PDBsum; 3QDO; -.
DR PDBsum; 3QE1; -.
DR PDBsum; 3QGL; -.
DR AlphaFoldDB; Q63511; -.
DR SMR; Q63511; -.
DR STRING; 10116.ENSRNOP00000010113; -.
DR iPTMnet; Q63511; -.
DR PhosphoSitePlus; Q63511; -.
DR PaxDb; Q63511; -.
DR ABCD; Q63511; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000010113; ENSRNOP00000010113; ENSRNOG00000007645.
DR GeneID; 116560; -.
DR KEGG; rno:116560; -.
DR CTD; 3765; -.
DR RGD; 621440; Kcnj9.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_11_0_1; -.
DR InParanoid; Q63511; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q63511; -.
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 EvolutionaryTrace; Q63511; -.
DR PRO; PR:Q63511; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000007645; Expressed in frontal cortex and 11 other tissues.
DR ExpressionAtlas; Q63511; baseline and differential.
DR Genevisible; Q63511; RN.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
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; IPR003276; K_chnl_inward-rec_Kir3.3.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF17; PTHR11767:SF17; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01329; KIR33CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..393
FT /note="G protein-activated inward rectifier potassium
FT channel 3"
FT /id="PRO_0000154952"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 58..82
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 83..106
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 107..118
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 119..125
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 126..134
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..156
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 157..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..125
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 390..393
FT /note="PDZ-binding"
FT SITE 150
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT MUTAGEN 388..389
FT /note="ES->RR,RS: Abolishes interaction with SNX27."
FT /evidence="ECO:0000269|PubMed:21422294"
FT MUTAGEN 390..393
FT /note="Missing: Abolishes interaction with SNX27."
FT /evidence="ECO:0000269|PubMed:17828261"
FT MUTAGEN 392
FT /note="K->D: Abolishes interaction with SNX27."
FT /evidence="ECO:0000269|PubMed:17828261"
FT MUTAGEN 392
FT /note="K->E: Does not affect interaction with SNX27."
FT /evidence="ECO:0000269|PubMed:17828261"
FT MUTAGEN 393
FT /note="V->I: Abolishes interaction with SNX27."
FT /evidence="ECO:0000269|PubMed:17828261"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:3QGL"
SQ SEQUENCE 393 AA; 43965 MW; 9CF749672A996608 CRC64;
MAQENAAFSP GSEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS
LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT
IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS
LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF
LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW
GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK
VEEEGAGEGA GAGDGADKEQ NGCLPPPESE SKV
