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   24-JAN-2024, entry version 157.
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
CC       (TC 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.ENSRNOP00000071010; -.
DR   iPTMnet; Q63511; -.
DR   PhosphoSitePlus; Q63511; -.
DR   PaxDb; 10116-ENSRNOP00000010113; -.
DR   ABCD; Q63511; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000010113.5; ENSRNOP00000010113.2; ENSRNOG00000007645.6.
DR   Ensembl; ENSRNOT00055037575; ENSRNOP00055030648; ENSRNOG00055021892.
DR   Ensembl; ENSRNOT00060039489; ENSRNOP00060032675; ENSRNOG00060022766.
DR   GeneID; 116560; -.
DR   KEGG; rno:116560; -.
DR   AGR; RGD:621440; -.
DR   CTD; 3765; -.
DR   RGD; 621440; Kcnj9.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT01080000257365; -.
DR   HOGENOM; CLU_022738_11_0_1; -.
DR   InParanoid; Q63511; -.
DR   OMA; RFSPMML; -.
DR   OrthoDB; 4126787at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q63511; baseline and differential.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; ISO: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 monoatomic ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0099505; P:regulation of presynaptic membrane potential; ISO:RGD.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 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:SF17; G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 3; 1.
DR   PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 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; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   Genevisible; Q63511; RN.
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
//