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Protein

G protein-activated inward rectifier potassium channel 1

Gene

Kcnj3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This potassium channel is controlled by G proteins. 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. This receptor plays a crucial role in regulating the heartbeat.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei173 – 1731Role 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

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_308732. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_339334. Activation of G protein gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
G protein-activated inward rectifier potassium channel 1
Short name:
GIRK-1
Alternative name(s):
Inward rectifier K(+) channel Kir3.1
Potassium channel, inwardly rectifying subfamily J member 3
Gene namesi
Name:Kcnj3
Synonyms:Girk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:104742. Kcnj3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8080CytoplasmicAdd
BLAST
Transmembranei81 – 10525Helical; Name=M1By similarityAdd
BLAST
Topological domaini106 – 12924ExtracellularBy similarityAdd
BLAST
Intramembranei130 – 14112Helical; Pore-forming; Name=H5By similarityAdd
BLAST
Intramembranei142 – 1487Pore-formingBy similarity
Topological domaini149 – 1579ExtracellularBy similarity
Transmembranei158 – 17922Helical; Name=M2By similarityAdd
BLAST
Topological domaini180 – 501322CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501G protein-activated inward rectifier potassium channel 1PRO_0000154939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP63250.
PRIDEiP63250.

Expressioni

Gene expression databases

BgeeiP63250.
ExpressionAtlasiP63250. baseline and differential.
GenevisibleiP63250. MM.

Interactioni

Subunit structurei

Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein activated heteromultimer pore-forming unit. The resulting inward current is much larger (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-48585N.
STRINGi10090.ENSMUSP00000063329.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi55 – 584Combined sources
Helixi69 – 779Combined sources
Helixi178 – 1858Combined sources
Helixi190 – 1923Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi227 – 23711Combined sources
Beta strandi243 – 2519Combined sources
Turni255 – 2573Combined sources
Beta strandi268 – 2736Combined sources
Turni279 – 2824Combined sources
Helixi285 – 2884Combined sources
Beta strandi294 – 3018Combined sources
Turni304 – 3074Combined sources
Beta strandi310 – 3178Combined sources
Helixi318 – 3203Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi335 – 3406Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi348 – 3503Combined sources
Helixi358 – 36710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N9PX-ray1.80A41-371[»]
1U4EX-ray2.09A41-63[»]
2QKSX-ray2.20A/B41-82[»]
A/B178-371[»]
3K6NX-ray2.00A41-371[»]
ProteinModelPortaliP63250.
SMRiP63250. Positions 41-370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63250.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi143 – 1486Selectivity filterBy similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG280776.
GeneTreeiENSGT00760000118842.
HOGENOMiHOG000237325.
HOVERGENiHBG006178.
InParanoidiP63250.
KOiK04997.
OMAiNQPPPEK.
OrthoDBiEOG7XPZ5K.
PhylomeDBiP63250.
TreeFamiTF313676.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003274. K_chnl_inward-rec_Kir3.1.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PRINTSiPR01327. KIR31CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

P63250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALRRKFGD DYQVVTTSSS GSGLQPQGPG QGPQQQLVPK KKRQRFVDKN
60 70 80 90 100
GRCNVQHGNL GSETSRYLSD LFTTLVDLKW RWNLFIFILT YTVAWLFMAS
110 120 130 140 150
MWWVIAYTRG DLNKAHVGNY TPCVANVYNF PSAFLFFIET EATIGYGYRY
160 170 180 190 200
ITDKCPEGII LFLFQSILGS IVDAFLIGCM FIKMSQPKKR AETLMFSEHA
210 220 230 240 250
VISMRDGKLT LMFRVGNLRN SHMVSAQIRC KLLKSRQTPE GEFLPLDQLE
260 270 280 290 300
LDVGFSTGAD QLFLVSPLTI CHVIDAKSPF YDLSQRSMQT EQFEVVVILE
310 320 330 340 350
GIVETTGMTC QARTSYTEDE VLWGHRFFPV ISLEEGFFKV DYSQFHATFE
360 370 380 390 400
VPTPPYSVKE QEEMLLMSSP LIAPAITNSK ERHNSVECLD GLDDISTKLP
410 420 430 440 450
SKLQKITGRE DFPKKLLRMS STTSEKAYSL GDLPMKLQRI SSVPGNSEEK
460 470 480 490 500
LVSKTTKMLS DPMSQSVADL PPKLQKMAGG PTRMEGNLPA KLRKMNSDRF

T
Length:501
Mass (Da):56,573
Last modified:October 11, 2004 - v1
Checksum:iAB8910E9CC08FFEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45022 mRNA. Translation: BAA08079.1.
CCDSiCCDS16042.1.
PIRiJC4139.
RefSeqiNP_032452.1. NM_008426.2.
XP_006497792.1. XM_006497729.2.
XP_006497793.1. XM_006497730.2.
UniGeneiMm.418451.
Mm.5127.

Genome annotation databases

EnsembliENSMUST00000067101; ENSMUSP00000063329; ENSMUSG00000026824.
ENSMUST00000112633; ENSMUSP00000108252; ENSMUSG00000026824.
GeneIDi16519.
KEGGimmu:16519.
UCSCiuc008jru.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45022 mRNA. Translation: BAA08079.1.
CCDSiCCDS16042.1.
PIRiJC4139.
RefSeqiNP_032452.1. NM_008426.2.
XP_006497792.1. XM_006497729.2.
XP_006497793.1. XM_006497730.2.
UniGeneiMm.418451.
Mm.5127.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N9PX-ray1.80A41-371[»]
1U4EX-ray2.09A41-63[»]
2QKSX-ray2.20A/B41-82[»]
A/B178-371[»]
3K6NX-ray2.00A41-371[»]
ProteinModelPortaliP63250.
SMRiP63250. Positions 41-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48585N.
STRINGi10090.ENSMUSP00000063329.

Chemistry

BindingDBiP63250.
GuidetoPHARMACOLOGYi434.

Proteomic databases

PaxDbiP63250.
PRIDEiP63250.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067101; ENSMUSP00000063329; ENSMUSG00000026824.
ENSMUST00000112633; ENSMUSP00000108252; ENSMUSG00000026824.
GeneIDi16519.
KEGGimmu:16519.
UCSCiuc008jru.2. mouse.

Organism-specific databases

CTDi3760.
MGIiMGI:104742. Kcnj3.

Phylogenomic databases

eggNOGiNOG280776.
GeneTreeiENSGT00760000118842.
HOGENOMiHOG000237325.
HOVERGENiHBG006178.
InParanoidiP63250.
KOiK04997.
OMAiNQPPPEK.
OrthoDBiEOG7XPZ5K.
PhylomeDBiP63250.
TreeFamiTF313676.

Enzyme and pathway databases

ReactomeiREACT_308732. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_339334. Activation of G protein gated Potassium channels.

Miscellaneous databases

EvolutionaryTraceiP63250.
NextBioi289889.
PROiP63250.
SOURCEiSearch...

Gene expression databases

BgeeiP63250.
ExpressionAtlasiP63250. baseline and differential.
GenevisibleiP63250. MM.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003274. K_chnl_inward-rec_Kir3.1.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PRINTSiPR01327. KIR31CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of a mouse G-protein-activated K+ channel (mGIRK1) and distinct distributions of three GIRK (GIRK1, 2 and 3) mRNAs in mouse brain."
    Kobayashi T., Ikeda K., Ichikawa T., Abe S., Togashi S., Kumanishi T.
    Biochem. Biophys. Res. Commun. 208:1166-1173(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. "Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution."
    Nishida M., MacKinnon R.
    Cell 111:957-965(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 43-63 AND 190-370.

Entry informationi

Entry nameiKCNJ3_MOUSE
AccessioniPrimary (citable) accession number: P63250
Secondary accession number(s): P35562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 22, 2015
This is version 104 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, 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

External Data

Dasty 3

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 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.