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Protein

G protein-activated inward rectifier potassium channel 3

Gene

Kcnj9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This receptor 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei150 – 1501Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesiumBy similarity

GO - Molecular functioni

  1. G-protein activated inward rectifier potassium channel activity Source: GO_Central
  2. PDZ domain binding Source: UniProtKB

GO - Biological processi

  1. potassium ion import Source: GO_Central
  2. regulation of ion transmembrane transport Source: GO_Central
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_278318. Activation of G protein gated Potassium channels.
REACT_287906. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

Names & Taxonomyi

Protein namesi
Recommended name:
G protein-activated inward rectifier potassium channel 3
Short name:
GIRK-3
Alternative name(s):
Inward rectifier K(+) channel Kir3.3
Potassium channel, inwardly rectifying subfamily J member 9
Gene namesi
Name:Kcnj9
Synonyms:Girk3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi621440. Kcnj9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757CytoplasmicBy similarityAdd
BLAST
Transmembranei58 – 8225Helical; Name=M1By similarityAdd
BLAST
Topological domaini83 – 10624ExtracellularBy similarityAdd
BLAST
Intramembranei107 – 11812Helical; Pore-forming; Name=H5By similarityAdd
BLAST
Intramembranei119 – 1257Pore-formingBy similarity
Topological domaini126 – 1349ExtracellularBy similarity
Transmembranei135 – 15622Helical; Name=M2By similarityAdd
BLAST
Topological domaini157 – 393237CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: GO_Central
  2. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi388 – 3892ES → RR or RS: Abolishes interaction with SNX27. 1 Publication
Mutagenesisi390 – 3934Missing : Abolishes interaction with SNX27. 1 Publication
Mutagenesisi392 – 3921K → D: Abolishes interaction with SNX27. 1 Publication
Mutagenesisi392 – 3921K → E: Does not affect interaction with SNX27. 1 Publication
Mutagenesisi393 – 3931V → I: Abolishes interaction with SNX27. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393G protein-activated inward rectifier potassium channel 3PRO_0000154952Add
BLAST

Proteomic databases

PRIDEiQ63511.

PTM databases

PhosphoSiteiQ63511.

Expressioni

Gene expression databases

GenevestigatoriQ63511.

Interactioni

Subunit structurei

Associates with GIRK1 to form a G-protein-activated heteromultimer pore-forming unit (By similarity). 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 similarity2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010113.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi389 – 3924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QDOX-ray1.88A388-393[»]
3QE1X-ray1.68A388-393[»]
3QGLX-ray3.31F/G/H/I/J388-393[»]
ProteinModelPortaliQ63511.
SMRiQ63511. Positions 168-346.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63511.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi120 – 1256Selectivity filterBy similarity
Motifi390 – 3934PDZ-binding

Domaini

The PDZ-binding motif specifically binds the PDZ domain of SNX27: the specificity for SNX27 is provided by the 2 residues located upstream (Glu-388 and Ser-389) of the PDZ-binding motif (PubMed:17828261, PubMed:21422294).2 Publications

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG72812.
GeneTreeiENSGT00760000118842.
HOGENOMiHOG000237325.
HOVERGENiHBG006178.
InParanoidiQ63511.
KOiK05002.
OMAiYVEKNGR.
OrthoDBiEOG7XPZ5K.
PhylomeDBiQ63511.
TreeFamiTF313676.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003276. K_chnl_inward-rec_Kir3.3.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF17. PTHR11767:SF17. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PIRSFiPIRSF005465. GIRK_kir. 1 hit.
PRINTSiPR01329. KIR33CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Q63511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQENAAFSP GSEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT
60 70 80 90 100
TLVDLQWRLS LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC
110 120 130 140 150
VNNLNGFVAA FLFSIETETT IGYGHRVITD QCPEGIVLLL LQAILGSMVN
160 170 180 190 200
AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS LRDGRLCLMF RVGDLRSSHI
210 220 230 240 250
VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF LVSPLVISHE
260 270 280 290 300
IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW
310 320 330 340 350
GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY
360 370 380 390
WSIPSRLDEK VEEEGAGEGA GAGDGADKEQ NGCLPPPESE SKV
Length:393
Mass (Da):43,965
Last modified:July 15, 1999 - v2
Checksum:i9CF749672A996608
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77929 mRNA. Translation: AAB95433.1.
RefSeqiNP_446286.1. NM_053834.1.

Genome annotation databases

EnsembliENSRNOT00000010113; ENSRNOP00000010113; ENSRNOG00000007645.
GeneIDi116560.
KEGGirno:116560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77929 mRNA. Translation: AAB95433.1.
RefSeqiNP_446286.1. NM_053834.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QDOX-ray1.88A388-393[»]
3QE1X-ray1.68A388-393[»]
3QGLX-ray3.31F/G/H/I/J388-393[»]
ProteinModelPortaliQ63511.
SMRiQ63511. Positions 168-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010113.

PTM databases

PhosphoSiteiQ63511.

Proteomic databases

PRIDEiQ63511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010113; ENSRNOP00000010113; ENSRNOG00000007645.
GeneIDi116560.
KEGGirno:116560.

Organism-specific databases

CTDi3765.
RGDi621440. Kcnj9.

Phylogenomic databases

eggNOGiNOG72812.
GeneTreeiENSGT00760000118842.
HOGENOMiHOG000237325.
HOVERGENiHBG006178.
InParanoidiQ63511.
KOiK05002.
OMAiYVEKNGR.
OrthoDBiEOG7XPZ5K.
PhylomeDBiQ63511.
TreeFamiTF313676.

Enzyme and pathway databases

ReactomeiREACT_278318. Activation of G protein gated Potassium channels.
REACT_287906. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

Miscellaneous databases

EvolutionaryTraceiQ63511.
NextBioi619225.
PROiQ63511.

Gene expression databases

GenevestigatoriQ63511.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003276. K_chnl_inward-rec_Kir3.3.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF17. PTHR11767:SF17. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PIRSFiPIRSF005465. GIRK_kir. 1 hit.
PRINTSiPR01329. KIR33CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Functional expression and cellular mRNA localization of a G protein-activated K+ inward rectifier isolated from rat brain."
    Dissmann E., Wischmeyer E., Spauschus A., Pfeil D.V., Karschin C., Karschin A.
    Biochem. Biophys. Res. Commun. 223:474-479(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Dissmann E., Wischmeyer E., Spauschus A., Pfeil D.V., Karschin C., Karschin A.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "A unique sorting nexin regulates trafficking of potassium channels via a PDZ domain interaction."
    Lunn M.L., Nassirpour R., Arrabit C., Tan J., McLeod I., Arias C.M., Sawchenko P.E., Yates J.R. III, Slesinger P.A.
    Nat. Neurosci. 10:1249-1259(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX27, MUTAGENESIS OF 390-GLU--VAL-393; LYS-392 AND VAL-393.
  4. "Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant-sensitive sorting nexin 27."
    Balana B., Maslennikov I., Kwiatkowski W., Stern K.M., Bahima L., Choe S., Slesinger P.A.
    Proc. Natl. Acad. Sci. U.S.A. 108:5831-5836(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 388-393 IN COMPLEX WITH SNX27, INTERACTION WITH SNX27, MUTAGENESIS OF 388-GLU-SER-389.

Entry informationi

Entry nameiKCNJ9_RAT
AccessioniPrimary (citable) accession number: Q63511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: April 1, 2015
This is version 114 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.