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Protein

G protein-activated inward rectifier potassium channel 2

Gene

Kcnj6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This potassium channel is controlled by G proteins. It plays a role in granule cell differentiation, possibly via membrane hyperpolarization. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei184 – 1841Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesiumBy similarity

GO - Molecular functioni

  • G-protein activated inward rectifier potassium channel activity Source: MGI

GO - Biological processi

  • potassium ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Names & Taxonomyi

Protein namesi
Recommended name:
G protein-activated inward rectifier potassium channel 2
Short name:
GIRK-2
Alternative name(s):
Inward rectifier K(+) channel Kir3.2
Potassium channel, inwardly rectifying subfamily J member 6
Gene namesi
Name:Kcnj6
Synonyms:Girk2, Kcnj7, W
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:104781. Kcnj6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9191CytoplasmicBy similarityAdd
BLAST
Transmembranei92 – 11625Helical; Name=M1By similarityAdd
BLAST
Topological domaini117 – 14024ExtracellularBy similarityAdd
BLAST
Intramembranei141 – 15212Helical; Pore-forming; Name=H5By similarityAdd
BLAST
Intramembranei153 – 1597Pore-formingBy similarity
Topological domaini160 – 1689ExtracellularBy similarity
Transmembranei169 – 19022Helical; Name=M2By similarityAdd
BLAST
Topological domaini191 – 425235CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in Kcnj6 are the cause of the weaver (wv) phenotype. Homozygous animals suffer from severe ataxia that is obvious by about the second postnatal week. The cerebellum of these animals is drastically reduced in size due to depletion of the major cell type of cerebellum, the granule cell neuron. Heterozygous animals are not ataxic but have an intermediate number of surviving granule cells. Male homozygotes are sterile, because of complete failure of sperm production. Both hetero- and homozygous animals undergo sporadic tonic-clonic seizures.

Keywords - Diseasei

Disease mutation

Chemistry

GuidetoPHARMACOLOGYi435.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425G protein-activated inward rectifier potassium channel 2PRO_0000154944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei25 – 251PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP48542.
PaxDbiP48542.
PRIDEiP48542.

PTM databases

PhosphoSiteiP48542.

Expressioni

Tissue specificityi

Cerebellum, testes, cortex and substentia nigra.

Gene expression databases

BgeeiP48542.

Interactioni

Subunit structurei

May associate with GIRK1 or GIRK4 to form a G-protein-activated heteromultimer pore-forming unit. The resulting inward current is much larger. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-60215N.
STRINGi10090.ENSMUSP00000097108.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 704Combined sources
Helixi76 – 805Combined sources
Helixi82 – 887Combined sources
Helixi91 – 11929Combined sources
Turni120 – 1245Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi134 – 1363Combined sources
Helixi143 – 15210Combined sources
Beta strandi158 – 1603Combined sources
Helixi167 – 19630Combined sources
Turni198 – 2003Combined sources
Helixi202 – 2043Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi219 – 2268Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 24815Combined sources
Beta strandi254 – 2629Combined sources
Turni266 – 2716Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi279 – 2846Combined sources
Turni290 – 2934Combined sources
Turni296 – 2983Combined sources
Helixi299 – 3013Combined sources
Beta strandi305 – 31410Combined sources
Turni315 – 3173Combined sources
Beta strandi320 – 3289Combined sources
Helixi329 – 3313Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi342 – 3454Combined sources
Beta strandi348 – 3525Combined sources
Helixi353 – 3553Combined sources
Beta strandi359 – 3613Combined sources
Helixi369 – 3779Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E4FX-ray2.30A53-381[»]
3AGWX-ray2.20A53-380[»]
3AT8X-ray3.30A53-380[»]
3AT9X-ray3.30A53-380[»]
3ATAX-ray3.49A53-380[»]
3ATBX-ray3.51A53-380[»]
3ATDX-ray3.01A53-380[»]
3ATEX-ray3.20A53-380[»]
3ATFX-ray2.95A53-380[»]
3AUWX-ray3.56A/C53-74[»]
B/D200-380[»]
3SYAX-ray2.98A52-380[»]
3SYCX-ray3.41A52-380[»]
3SYOX-ray3.54A52-380[»]
3SYPX-ray3.12A52-380[»]
3SYQX-ray3.44A/B52-380[»]
3VSQX-ray2.00A53-380[»]
4KFMX-ray3.45A52-380[»]
ProteinModelPortaliP48542.
SMRiP48542. Positions 55-380.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48542.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi154 – 1596Selectivity filterBy similarity
Motifi422 – 4254PDZ-binding

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3827. Eukaryota.
ENOG410XQ62. LUCA.
HOVERGENiHBG006178.
InParanoidiP48542.
KOiK05000.
PhylomeDBiP48542.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003275. K_chnl_inward-rec_Kir3.2.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF19. PTHR11767:SF19. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PIRSFiPIRSF005465. GIRK_kir. 1 hit.
PRINTSiPR01328. KIR32CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform GIRK2A (identifier: P48542-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR
60 70 80 90 100
TKRKIQRYVR KDGKCNVHHG NVRETYRYLT DIFTTLVDLK WRFNLLIFVM
110 120 130 140 150
VYTVTWLFFG MIWWLIAYIR GDMDHIEDPS WTPCVTNLNG FVSAFLFSIE
160 170 180 190 200
TETTIGYGYR VITDKCPEGI ILLLIQSVLG SIVNAFMVGC MFVKISQPKK
210 220 230 240 250
RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR AKLIKSKQTS
260 270 280 290 300
EGEFIPLNQS DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP
310 320 330 340 350
KEELEIVVIL EGIVEATGMT CQARSSYITS EILWGYRFTP VLTMEDGFYE
360 370 380 390 400
VDYNSFHETY ETSTPSLSAK ELAELANRAE VPLSWSVSSK LNQHAELETE
410 420
EEEKNPEELT ERNGDVANLE NESKV
Length:425
Mass (Da):48,652
Last modified:February 1, 1996 - v1
Checksum:i2E5153DCB1B60331
GO
Isoform GIRK2-1 (identifier: P48542-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     415-425: Missing.

Show »
Length:414
Mass (Da):47,452
Checksum:iF83E86C01A9D644B
GO
Isoform GIRK2B (identifier: P48542-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     319-327: MTCQARSSY → KMGFALGFL
     328-425: Missing.

Show »
Length:327
Mass (Da):37,392
Checksum:i8215CE889186C931
GO
Isoform GIRK2C (identifier: P48542-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.
     319-320: MT → QF
     321-425: Missing.

Show »
Length:302
Mass (Da):34,761
Checksum:i432A521BAA03AD02
GO
Isoform GIRK2D (identifier: P48542-5)

Also known as: KIR3.2D

Sequence is not available
Length:
Mass (Da):

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671V → C (PubMed:8573147).Curated
Sequence conflicti67 – 671V → C (PubMed:9721208).Curated
Sequence conflicti260 – 2601S → T in BAA12972 (PubMed:8573147).Curated
Sequence conflicti260 – 2601S → T in AAC34145 (PubMed:9721208).Curated
Sequence conflicti260 – 2601S → T in BAA88430 (Ref. 5) Curated
Sequence conflicti381 – 3811V → L in BAA88430 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti156 – 1561G → S in wv. 1 Publication
Natural varianti313 – 3131I → M.
Natural varianti344 – 3441M → L.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1818Missing in isoform GIRK2C. CuratedVSP_002806Add
BLAST
Alternative sequencei319 – 3279MTCQARSSY → KMGFALGFL in isoform GIRK2B. 1 PublicationVSP_002804
Alternative sequencei319 – 3202MT → QF in isoform GIRK2C. CuratedVSP_002807
Alternative sequencei321 – 425105Missing in isoform GIRK2C. CuratedVSP_002808Add
BLAST
Alternative sequencei328 – 42598Missing in isoform GIRK2B. 1 PublicationVSP_002805Add
BLAST
Alternative sequencei415 – 42511Missing in isoform GIRK2-1. 1 PublicationVSP_002803Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37253 mRNA. Translation: AAA91457.1.
U11859 mRNA. Translation: AAA53245.1.
U51122 mRNA. Translation: AAC34141.1.
U51123 mRNA. Translation: AAC34142.1.
U51124 mRNA. Translation: AAC34143.1.
U51125 mRNA. Translation: AAC34144.1.
U51126 mRNA. Translation: AAC34145.1.
AF040049, AF040047 Genomic DNA. Translation: AAC34286.1.
AF040050, AF040049 Genomic DNA. Translation: AAC34287.1.
AF040051, AF040047, AF040049 Genomic DNA. Translation: AAC34285.1.
AF040052
, AF040047, AF040049, AF040051 Genomic DNA. Translation: AAC34284.1.
D86040 mRNA. Translation: BAA12972.1.
AB029502 mRNA. Translation: BAA88430.1.
CCDSiCCDS37408.1. [P48542-2]
CCDS49921.1. [P48542-4]
PIRiJC4586.
S48738.
RefSeqiNP_001020756.1. NM_001025585.2.
NP_001020761.1. NM_001025590.1.
NP_034736.2. NM_010606.2.
XP_011244406.1. XM_011246104.1.
UniGeneiMm.328720.

Genome annotation databases

GeneIDi16522.
KEGGimmu:16522.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37253 mRNA. Translation: AAA91457.1.
U11859 mRNA. Translation: AAA53245.1.
U51122 mRNA. Translation: AAC34141.1.
U51123 mRNA. Translation: AAC34142.1.
U51124 mRNA. Translation: AAC34143.1.
U51125 mRNA. Translation: AAC34144.1.
U51126 mRNA. Translation: AAC34145.1.
AF040049, AF040047 Genomic DNA. Translation: AAC34286.1.
AF040050, AF040049 Genomic DNA. Translation: AAC34287.1.
AF040051, AF040047, AF040049 Genomic DNA. Translation: AAC34285.1.
AF040052
, AF040047, AF040049, AF040051 Genomic DNA. Translation: AAC34284.1.
D86040 mRNA. Translation: BAA12972.1.
AB029502 mRNA. Translation: BAA88430.1.
CCDSiCCDS37408.1. [P48542-2]
CCDS49921.1. [P48542-4]
PIRiJC4586.
S48738.
RefSeqiNP_001020756.1. NM_001025585.2.
NP_001020761.1. NM_001025590.1.
NP_034736.2. NM_010606.2.
XP_011244406.1. XM_011246104.1.
UniGeneiMm.328720.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E4FX-ray2.30A53-381[»]
3AGWX-ray2.20A53-380[»]
3AT8X-ray3.30A53-380[»]
3AT9X-ray3.30A53-380[»]
3ATAX-ray3.49A53-380[»]
3ATBX-ray3.51A53-380[»]
3ATDX-ray3.01A53-380[»]
3ATEX-ray3.20A53-380[»]
3ATFX-ray2.95A53-380[»]
3AUWX-ray3.56A/C53-74[»]
B/D200-380[»]
3SYAX-ray2.98A52-380[»]
3SYCX-ray3.41A52-380[»]
3SYOX-ray3.54A52-380[»]
3SYPX-ray3.12A52-380[»]
3SYQX-ray3.44A/B52-380[»]
3VSQX-ray2.00A53-380[»]
4KFMX-ray3.45A52-380[»]
ProteinModelPortaliP48542.
SMRiP48542. Positions 55-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60215N.
STRINGi10090.ENSMUSP00000097108.

Chemistry

GuidetoPHARMACOLOGYi435.

PTM databases

PhosphoSiteiP48542.

Proteomic databases

MaxQBiP48542.
PaxDbiP48542.
PRIDEiP48542.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16522.
KEGGimmu:16522.

Organism-specific databases

CTDi3763.
MGIiMGI:104781. Kcnj6.

Phylogenomic databases

eggNOGiKOG3827. Eukaryota.
ENOG410XQ62. LUCA.
HOVERGENiHBG006178.
InParanoidiP48542.
KOiK05000.
PhylomeDBiP48542.

Miscellaneous databases

EvolutionaryTraceiP48542.
NextBioi289901.
PROiP48542.
SOURCEiSearch...

Gene expression databases

BgeeiP48542.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003275. K_chnl_inward-rec_Kir3.2.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF19. PTHR11767:SF19. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PIRSFiPIRSF005465. GIRK_kir. 1 hit.
PRINTSiPR01328. KIR32CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning provides evidence for a family of inward rectifier and G-protein coupled K+ channels in the brain."
    Lesage F., Duprat F., Fink M., Guillemare E., Coppola T., Lazdunski M., Hugnot J.-P.
    FEBS Lett. 353:37-42(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2-1).
    Tissue: Brain.
  2. "Molecular properties of neuronal G-protein-activated inwardly rectifying K+ channels."
    Lesage F., Guillemare E., Fink M., Duprat F., Heurteaux C., Fosset M., Romey G., Barhanin J., Lazdunski M.
    J. Biol. Chem. 270:28660-28667(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2A).
    Tissue: Brain.
  3. "A novel ubiquitously distributed isoform of GIRK2 (GIRK2B) enhances GIRK1 expression of the G-protein-gated K+ current in Xenopus oocytes."
    Isomoto S., Kondo C., Takahashi N., Matsumoto S., Yamada M., Takumi T., Horio Y., Kurachi Y.
    Biochem. Biophys. Res. Commun. 218:286-291(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2B).
    Tissue: Brain.
  4. "Characterization of murine Girk2 transcript isoforms: structure and differential expression."
    Wei J., Hodes M.E., Piva R., Feng Y., Wang Y., Ghetti B., Dlouhy S.R.
    Genomics 51:379-390(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
    Strain: 129/SvJ.
  5. "Molecular cloning and characterization of a novel splicing variant of Kir3.2/GIRK2 predominantly expressed in mouse testis."
    Inanobe A., Horio Y., Fujita A., Tanemoto M., Kurachi Y.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2D).
  6. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 379-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. "A potassium channel mutation in weaver mice implicates membrane excitability in granule cell differentiation."
    Patil N., Cox D.R., Bhat D., Faham M., Myers R.M., Peterson A.S.
    Nat. Genet. 11:126-129(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN WV PHENOTYPE, VARIANT WV SER-156.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKCNJ6_MOUSE
AccessioniPrimary (citable) accession number: P48542
Secondary accession number(s): O70290
, P70216, P70306, P70307, P70308, P70309, P70454, Q9QYH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.