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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)DescriptionActionsGraphical viewLength
Sitei184Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesiumBy similarity1

GO - Molecular functioni

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

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 91CytoplasmicBy similarityAdd BLAST91
Transmembranei92 – 116Helical; Name=M1By similarityAdd BLAST25
Topological domaini117 – 140ExtracellularBy similarityAdd BLAST24
Intramembranei141 – 152Helical; Pore-forming; Name=H5By similarityAdd BLAST12
Intramembranei153 – 159Pore-formingBy similarity7
Topological domaini160 – 168ExtracellularBy similarity9
Transmembranei169 – 190Helical; Name=M2By similarityAdd BLAST22
Topological domaini191 – 425CytoplasmicBy similarityAdd BLAST235

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 databases

GuidetoPHARMACOLOGYi435.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001549441 – 425G protein-activated inward rectifier potassium channel 2Add BLAST425

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18PhosphoserineCombined sources1
Modified residuei25PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP48542.
PeptideAtlasiP48542.
PRIDEiP48542.

PTM databases

iPTMnetiP48542.

Expressioni

Tissue specificityi

Cerebellum, testes, cortex and substentia nigra.

Gene expression databases

BgeeiENSMUSG00000043301.

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

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi67 – 70Combined sources4
Helixi76 – 80Combined sources5
Helixi82 – 88Combined sources7
Helixi91 – 119Combined sources29
Turni120 – 124Combined sources5
Beta strandi129 – 131Combined sources3
Beta strandi134 – 136Combined sources3
Helixi143 – 152Combined sources10
Beta strandi158 – 160Combined sources3
Helixi167 – 196Combined sources30
Turni198 – 200Combined sources3
Helixi202 – 204Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi211 – 216Combined sources6
Beta strandi219 – 226Combined sources8
Beta strandi230 – 232Combined sources3
Beta strandi234 – 248Combined sources15
Beta strandi254 – 262Combined sources9
Turni266 – 271Combined sources6
Beta strandi272 – 274Combined sources3
Beta strandi279 – 284Combined sources6
Turni290 – 293Combined sources4
Turni296 – 298Combined sources3
Helixi299 – 301Combined sources3
Beta strandi305 – 314Combined sources10
Turni315 – 317Combined sources3
Beta strandi320 – 328Combined sources9
Helixi329 – 331Combined sources3
Beta strandi332 – 334Combined sources3
Beta strandi336 – 338Combined sources3
Beta strandi342 – 345Combined sources4
Beta strandi348 – 352Combined sources5
Helixi353 – 355Combined sources3
Beta strandi359 – 361Combined sources3
Helixi369 – 377Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48542.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi154 – 159Selectivity filterBy similarity6
Motifi422 – 425PDZ-binding4

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)DescriptionActionsGraphical viewLength
Sequence conflicti67V → C (PubMed:8573147).Curated1
Sequence conflicti67V → C (PubMed:9721208).Curated1
Sequence conflicti260S → T in BAA12972 (PubMed:8573147).Curated1
Sequence conflicti260S → T in AAC34145 (PubMed:9721208).Curated1
Sequence conflicti260S → T in BAA88430 (Ref. 5) Curated1
Sequence conflicti381V → L in BAA88430 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti156G → S in wv. 1 Publication1
Natural varianti313I → M.1
Natural varianti344M → L.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0028061 – 18Missing in isoform GIRK2C. CuratedAdd BLAST18
Alternative sequenceiVSP_002804319 – 327MTCQARSSY → KMGFALGFL in isoform GIRK2B. 1 Publication9
Alternative sequenceiVSP_002807319 – 320MT → QF in isoform GIRK2C. Curated2
Alternative sequenceiVSP_002808321 – 425Missing in isoform GIRK2C. CuratedAdd BLAST105
Alternative sequenceiVSP_002805328 – 425Missing in isoform GIRK2B. 1 PublicationAdd BLAST98
Alternative sequenceiVSP_002803415 – 425Missing in isoform GIRK2-1. 1 PublicationAdd BLAST11

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60215N.
STRINGi10090.ENSMUSP00000097108.

Chemistry databases

GuidetoPHARMACOLOGYi435.

PTM databases

iPTMnetiP48542.

Proteomic databases

PaxDbiP48542.
PeptideAtlasiP48542.
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.
PROiP48542.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000043301.

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...

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: November 2, 2016
This is version 146 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.