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Database: UniProt
Entry: KCNJ6_MOUSE
LinkDB: KCNJ6_MOUSE
Original site: KCNJ6_MOUSE 
ID   KCNJ6_MOUSE             Reviewed;         425 AA.
AC   P48542; O70290; P70216; P70306; P70307; P70308; P70309; P70454;
AC   Q9QYH5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-OCT-2019, entry version 164.
DE   RecName: Full=G protein-activated inward rectifier potassium channel 2;
DE            Short=GIRK-2;
DE   AltName: Full=Inward rectifier K(+) channel Kir3.2;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 6;
GN   Name=Kcnj6; Synonyms=Girk2, Kcnj7, W;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2-1).
RC   TISSUE=Brain;
RX   PubMed=7926018; DOI=10.1016/0014-5793(94)01007-2;
RA   Lesage F., Duprat F., Fink M., Guillemare E., Coppola T.,
RA   Lazdunski M., Hugnot J.-P.;
RT   "Cloning provides evidence for a family of inward rectifier and G-
RT   protein coupled K+ channels in the brain.";
RL   FEBS Lett. 353:37-42(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2A).
RC   TISSUE=Brain;
RX   PubMed=7499385; DOI=10.1074/jbc.270.48.28660;
RA   Lesage F., Guillemare E., Fink M., Duprat F., Heurteaux C., Fosset M.,
RA   Romey G., Barhanin J., Lazdunski M.;
RT   "Molecular properties of neuronal G-protein-activated inwardly
RT   rectifying K+ channels.";
RL   J. Biol. Chem. 270:28660-28667(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2B).
RC   TISSUE=Brain;
RX   PubMed=8573147; DOI=10.1006/bbrc.1996.0050;
RA   Isomoto S., Kondo C., Takahashi N., Matsumoto S., Yamada M.,
RA   Takumi T., Horio Y., Kurachi Y.;
RT   "A novel ubiquitously distributed isoform of GIRK2 (GIRK2B) enhances
RT   GIRK1 expression of the G-protein-gated K+ current in Xenopus
RT   oocytes.";
RL   Biochem. Biophys. Res. Commun. 218:286-291(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129/SvJ;
RX   PubMed=9721208; DOI=10.1006/geno.1998.5369;
RA   Wei J., Hodes M.E., Piva R., Feng Y., Wang Y., Ghetti B., Dlouhy S.R.;
RT   "Characterization of murine Girk2 transcript isoforms: structure and
RT   differential expression.";
RL   Genomics 51:379-390(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2D).
RA   Inanobe A., Horio Y., Fujita A., Tanemoto M., Kurachi Y.;
RT   "Molecular cloning and characterization of a novel splicing variant of
RT   Kir3.2/GIRK2 predominantly expressed in mouse testis.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 379-390, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   INVOLVEMENT IN WV PHENOTYPE, AND VARIANT WV SER-156.
RX   PubMed=7550338; DOI=10.1038/ng1095-126;
RA   Patil N., Cox D.R., Bhat D., Faham M., Myers R.M., Peterson A.S.;
RT   "A potassium channel mutation in weaver mice implicates membrane
RT   excitability in granule cell differentiation.";
RL   Nat. Genet. 11:126-129(1995).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-25, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: This potassium channel is controlled by G proteins. It
CC       plays a role in granule cell differentiation, possibly via
CC       membrane hyperpolarization. Inward rectifier potassium channels
CC       are characterized by a greater tendency to allow potassium to flow
CC       into the cell rather than out of it. Their voltage dependence is
CC       regulated by the concentration of extracellular potassium; as
CC       external potassium is raised, the voltage range of the channel
CC       opening shifts to more positive voltages. The inward rectification
CC       is mainly due to the blockage of outward current by internal
CC       magnesium.
CC   -!- SUBUNIT: May associate with GIRK1 or GIRK4 to form a G-protein-
CC       activated heteromultimer pore-forming unit. The resulting inward
CC       current is much larger. Interacts (via PDZ-binding motif) with
CC       SNX27 (via PDZ domain); the interaction is required when
CC       endocytosed to prevent degradation in lysosomes and promote
CC       recycling to the plasma membrane (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=GIRK2A;
CC         IsoId=P48542-1; Sequence=Displayed;
CC       Name=GIRK2-1;
CC         IsoId=P48542-2; Sequence=VSP_002803;
CC       Name=GIRK2B;
CC         IsoId=P48542-3; Sequence=VSP_002804, VSP_002805;
CC       Name=GIRK2C;
CC         IsoId=P48542-4; Sequence=VSP_002806, VSP_002807, VSP_002808;
CC       Name=GIRK2D; Synonyms=KIR3.2D;
CC         IsoId=P48542-5; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Cerebellum, testes, cortex and substentia
CC       nigra.
CC   -!- DISEASE: Note=Defects in Kcnj6 are the cause of the weaver (wv)
CC       phenotype. Homozygous animals suffer from severe ataxia that is
CC       obvious by about the second postnatal week. The cerebellum of
CC       these animals is drastically reduced in size due to depletion of
CC       the major cell type of cerebellum, the granule cell neuron.
CC       Heterozygous animals are not ataxic but have an intermediate
CC       number of surviving granule cells. Male homozygotes are sterile,
CC       because of complete failure of sperm production. Both hetero- and
CC       homozygous animals undergo sporadic tonic-clonic seizures.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ6 subfamily. {ECO:0000305}.
DR   EMBL; U37253; AAA91457.1; -; mRNA.
DR   EMBL; U11859; AAA53245.1; -; mRNA.
DR   EMBL; U51122; AAC34141.1; -; mRNA.
DR   EMBL; U51123; AAC34142.1; -; mRNA.
DR   EMBL; U51124; AAC34143.1; -; mRNA.
DR   EMBL; U51125; AAC34144.1; -; mRNA.
DR   EMBL; U51126; AAC34145.1; -; mRNA.
DR   EMBL; AF040049; AAC34286.1; -; Genomic_DNA.
DR   EMBL; AF040047; AAC34286.1; JOINED; Genomic_DNA.
DR   EMBL; AF040050; AAC34287.1; -; Genomic_DNA.
DR   EMBL; AF040049; AAC34287.1; JOINED; Genomic_DNA.
DR   EMBL; AF040051; AAC34285.1; -; Genomic_DNA.
DR   EMBL; AF040047; AAC34285.1; JOINED; Genomic_DNA.
DR   EMBL; AF040049; AAC34285.1; JOINED; Genomic_DNA.
DR   EMBL; AF040052; AAC34284.1; -; Genomic_DNA.
DR   EMBL; AF040047; AAC34284.1; JOINED; Genomic_DNA.
DR   EMBL; AF040049; AAC34284.1; JOINED; Genomic_DNA.
DR   EMBL; AF040051; AAC34284.1; JOINED; Genomic_DNA.
DR   EMBL; D86040; BAA12972.1; -; mRNA.
DR   EMBL; AB029502; BAA88430.1; -; mRNA.
DR   CCDS; CCDS37408.1; -. [P48542-2]
DR   CCDS; CCDS49921.1; -. [P48542-4]
DR   PIR; JC4586; JC4586.
DR   PIR; S48738; S48738.
DR   RefSeq; NP_001020756.1; NM_001025585.2.
DR   RefSeq; NP_001020761.1; NM_001025590.1.
DR   RefSeq; NP_034736.2; NM_010606.2.
DR   RefSeq; XP_011244406.1; XM_011246104.1.
DR   PDB; 2E4F; X-ray; 2.30 A; A=53-74, A=200-381.
DR   PDB; 3AGW; X-ray; 2.20 A; A=53-380.
DR   PDB; 3AT8; X-ray; 3.30 A; A=53-380.
DR   PDB; 3AT9; X-ray; 3.30 A; A=53-380.
DR   PDB; 3ATA; X-ray; 3.49 A; A=53-380.
DR   PDB; 3ATB; X-ray; 3.51 A; A=53-380.
DR   PDB; 3ATD; X-ray; 3.01 A; A=53-380.
DR   PDB; 3ATE; X-ray; 3.20 A; A=53-380.
DR   PDB; 3ATF; X-ray; 2.95 A; A=53-380.
DR   PDB; 3AUW; X-ray; 3.56 A; A/C=53-74, B/D=200-380.
DR   PDB; 3SYA; X-ray; 2.98 A; A=52-380.
DR   PDB; 3SYC; X-ray; 3.41 A; A=52-380.
DR   PDB; 3SYO; X-ray; 3.54 A; A=52-380.
DR   PDB; 3SYP; X-ray; 3.12 A; A=52-380.
DR   PDB; 3SYQ; X-ray; 3.44 A; A/B=52-380.
DR   PDB; 3VSQ; X-ray; 2.00 A; A=53-380.
DR   PDB; 4KFM; X-ray; 3.45 A; A=52-380.
DR   PDBsum; 2E4F; -.
DR   PDBsum; 3AGW; -.
DR   PDBsum; 3AT8; -.
DR   PDBsum; 3AT9; -.
DR   PDBsum; 3ATA; -.
DR   PDBsum; 3ATB; -.
DR   PDBsum; 3ATD; -.
DR   PDBsum; 3ATE; -.
DR   PDBsum; 3ATF; -.
DR   PDBsum; 3AUW; -.
DR   PDBsum; 3SYA; -.
DR   PDBsum; 3SYC; -.
DR   PDBsum; 3SYO; -.
DR   PDBsum; 3SYP; -.
DR   PDBsum; 3SYQ; -.
DR   PDBsum; 3VSQ; -.
DR   PDBsum; 4KFM; -.
DR   SMR; P48542; -.
DR   CORUM; P48542; -.
DR   DIP; DIP-60215N; -.
DR   IntAct; P48542; 1.
DR   STRING; 10090.ENSMUSP00000097108; -.
DR   DrugCentral; P48542; -.
DR   GuidetoPHARMACOLOGY; 435; -.
DR   iPTMnet; P48542; -.
DR   PaxDb; P48542; -.
DR   PeptideAtlas; P48542; -.
DR   PRIDE; P48542; -.
DR   GeneID; 16522; -.
DR   KEGG; mmu:16522; -.
DR   CTD; 3763; -.
DR   MGI; MGI:104781; Kcnj6.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   InParanoid; P48542; -.
DR   KO; K05000; -.
DR   OrthoDB; 956263at2759; -.
DR   PhylomeDB; P48542; -.
DR   Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   ChiTaRS; Kcnj6; mouse.
DR   EvolutionaryTrace; P48542; -.
DR   PRO; PR:P48542; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IDA:MGI.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
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; 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; IPR003275; K_chnl_inward-rec_Kir3.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF19; PTHR11767:SF19; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01328; KIR32CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    425       G protein-activated inward rectifier
FT                                potassium channel 2.
FT                                /FTId=PRO_0000154944.
FT   TOPO_DOM      1     91       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     92    116       Helical; Name=M1. {ECO:0000250}.
FT   TOPO_DOM    117    140       Extracellular. {ECO:0000250}.
FT   INTRAMEM    141    152       Helical; Pore-forming; Name=H5.
FT                                {ECO:0000250}.
FT   INTRAMEM    153    159       Pore-forming. {ECO:0000250}.
FT   TOPO_DOM    160    168       Extracellular. {ECO:0000250}.
FT   TRANSMEM    169    190       Helical; Name=M2. {ECO:0000250}.
FT   TOPO_DOM    191    425       Cytoplasmic. {ECO:0000250}.
FT   MOTIF       154    159       Selectivity filter. {ECO:0000250}.
FT   MOTIF       422    425       PDZ-binding.
FT   SITE        184    184       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium. {ECO:0000250}.
FT   MOD_RES      18     18       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES      25     25       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ       1     18       Missing (in isoform GIRK2C).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_002806.
FT   VAR_SEQ     319    327       MTCQARSSY -> KMGFALGFL (in isoform
FT                                GIRK2B). {ECO:0000303|PubMed:8573147}.
FT                                /FTId=VSP_002804.
FT   VAR_SEQ     319    320       MT -> QF (in isoform GIRK2C).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_002807.
FT   VAR_SEQ     321    425       Missing (in isoform GIRK2C).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_002808.
FT   VAR_SEQ     328    425       Missing (in isoform GIRK2B).
FT                                {ECO:0000303|PubMed:8573147}.
FT                                /FTId=VSP_002805.
FT   VAR_SEQ     415    425       Missing (in isoform GIRK2-1).
FT                                {ECO:0000303|PubMed:7926018}.
FT                                /FTId=VSP_002803.
FT   VARIANT     156    156       G -> S (in wv).
FT                                {ECO:0000269|PubMed:7550338}.
FT   VARIANT     313    313       I -> M.
FT   VARIANT     344    344       M -> L.
FT   CONFLICT     67     67       V -> C (in Ref. 3 and 4). {ECO:0000305}.
FT   CONFLICT    260    260       S -> T (in Ref. 3; BAA12972, 4; AAC34145
FT                                and 5; BAA88430). {ECO:0000305}.
FT   CONFLICT    381    381       V -> L (in Ref. 5; BAA88430).
FT                                {ECO:0000305}.
FT   HELIX        76     80       {ECO:0000244|PDB:3SYA}.
FT   HELIX        82     88       {ECO:0000244|PDB:3SYA}.
FT   HELIX        91    119       {ECO:0000244|PDB:3SYA}.
FT   TURN        120    124       {ECO:0000244|PDB:3SYA}.
FT   STRAND      129    131       {ECO:0000244|PDB:4KFM}.
FT   STRAND      134    136       {ECO:0000244|PDB:3SYA}.
FT   HELIX       143    152       {ECO:0000244|PDB:3SYA}.
FT   STRAND      158    160       {ECO:0000244|PDB:3SYA}.
FT   HELIX       167    196       {ECO:0000244|PDB:3SYA}.
FT   TURN        198    200       {ECO:0000244|PDB:3SYP}.
FT   HELIX       202    204       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      205    207       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      211    216       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      219    226       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      230    232       {ECO:0000244|PDB:3SYA}.
FT   STRAND      234    248       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      254    262       {ECO:0000244|PDB:3VSQ}.
FT   TURN        266    271       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      272    274       {ECO:0000244|PDB:3SYP}.
FT   STRAND      279    284       {ECO:0000244|PDB:3VSQ}.
FT   TURN        290    293       {ECO:0000244|PDB:3VSQ}.
FT   TURN        296    298       {ECO:0000244|PDB:3VSQ}.
FT   HELIX       299    301       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      305    314       {ECO:0000244|PDB:3VSQ}.
FT   TURN        315    317       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      320    328       {ECO:0000244|PDB:3VSQ}.
FT   HELIX       329    331       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      332    334       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      336    338       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      342    345       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      348    352       {ECO:0000244|PDB:3VSQ}.
FT   HELIX       353    355       {ECO:0000244|PDB:3VSQ}.
FT   STRAND      359    361       {ECO:0000244|PDB:3VSQ}.
FT   HELIX       369    377       {ECO:0000244|PDB:3VSQ}.
SQ   SEQUENCE   425 AA;  48652 MW;  2E5153DCB1B60331 CRC64;
     MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR
     KDGKCNVHHG NVRETYRYLT DIFTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR
     GDMDHIEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG
     SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR
     AKLIKSKQTS EGEFIPLNQS DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP
     KEELEIVVIL EGIVEATGMT CQARSSYITS EILWGYRFTP VLTMEDGFYE VDYNSFHETY
     ETSTPSLSAK ELAELANRAE VPLSWSVSSK LNQHAELETE EEEKNPEELT ERNGDVANLE
     NESKV
//
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