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Q63511 (KCNJ9_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Kcnj9
Synonyms:Girk3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.3 Ref.4

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

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 (Ref.3, Ref.4).

Sequence similarities

Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ9 subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393G protein-activated inward rectifier potassium channel 3
PRO_0000154952

Regions

Topological domain1 – 5757Cytoplasmic By similarity
Transmembrane58 – 8225Helical; Name=M1; By similarity
Topological domain83 – 10624Extracellular By similarity
Intramembrane107 – 11812Helical; Pore-forming; Name=H5; By similarity
Intramembrane119 – 1257Pore-forming; By similarity
Topological domain126 – 1349Extracellular By similarity
Transmembrane135 – 15622Helical; Name=M2; By similarity
Topological domain157 – 393237Cytoplasmic By similarity
Motif120 – 1256Selectivity filter By similarity
Motif390 – 3934PDZ-binding

Sites

Site1501Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium By similarity

Experimental info

Mutagenesis388 – 3892ES → RR or RS: Abolishes interaction with SNX27. Ref.4
Mutagenesis390 – 3934Missing: Abolishes interaction with SNX27. Ref.3 Ref.4
Mutagenesis3921K → D: Abolishes interaction with SNX27. Ref.3 Ref.4
Mutagenesis3921K → E: Does not affect interaction with SNX27. Ref.3 Ref.4
Mutagenesis3931V → I: Abolishes interaction with SNX27. Ref.3 Ref.4

Secondary structure

... 393
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q63511 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 9CF749672A996608

FASTA39343,965
        10         20         30         40         50         60 
MAQENAAFSP GSEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS 

        70         80         90        100        110        120 
LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT 

       130        140        150        160        170        180 
IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS 

       190        200        210        220        230        240 
LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF 

       250        260        270        280        290        300 
LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW 

       310        320        330        340        350        360 
GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK 

       370        380        390 
VEEEGAGEGA GAGDGADKEQ NGCLPPPESE SKV 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77929 mRNA. Translation: AAB95433.1.
RefSeqNP_446286.1. NM_053834.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QDOX-ray1.88A388-393[»]
3QE1X-ray1.68A388-393[»]
3QGLX-ray3.31F/G/H/I/J388-393[»]
ProteinModelPortalQ63511.
SMRQ63511. Positions 168-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010113.

PTM databases

PhosphoSiteQ63511.

Proteomic databases

PRIDEQ63511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010113; ENSRNOP00000010113; ENSRNOG00000007645.
GeneID116560.
KEGGrno:116560.

Organism-specific databases

CTD3765.
RGD621440. Kcnj9.

Phylogenomic databases

eggNOGNOG72812.
GeneTreeENSGT00730000110555.
HOGENOMHOG000237325.
HOVERGENHBG006178.
InParanoidQ63511.
KOK05002.
OMADYASFHQ.
OrthoDBEOG7XPZ5K.
PhylomeDBQ63511.
TreeFamTF313676.

Gene expression databases

GenevestigatorQ63511.

Family and domain databases

Gene3D2.60.40.1400. 1 hit.
InterProIPR014756. 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]
PANTHERPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF17. PTHR11767:SF17. 1 hit.
PfamPF01007. IRK. 1 hit.
[Graphical view]
PIRSFPIRSF005465. GIRK_kir. 1 hit.
PRINTSPR01329. KIR33CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ63511.
NextBio619225.
PROQ63511.

Entry information

Entry nameKCNJ9_RAT
AccessionPrimary (citable) accession number: Q63511
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: May 14, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references