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Q63511

- KCNJ9_RAT

UniProt

Q63511 - KCNJ9_RAT

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Protein

G protein-activated inward rectifier potassium channel 3

Gene
Kcnj9, Girk3
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Sites

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

GO - Molecular functioni

  1. G-protein activated inward rectifier potassium channel activity Source: InterPro
  2. PDZ domain binding Source: UniProtKB
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 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: Chromosome 13

Organism-specific databases

RGDi621440. Kcnj9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757Cytoplasmic By similarityAdd
BLAST
Transmembranei58 – 8225Helical; Name=M1; By similarityAdd
BLAST
Topological domaini83 – 10624Extracellular By similarityAdd
BLAST
Intramembranei107 – 11812Helical; Pore-forming; Name=H5; By similarityAdd
BLAST
Intramembranei119 – 1257Pore-forming; By similarity
Topological domaini126 – 1349Extracellular By similarity
Transmembranei135 – 15622Helical; Name=M2; By similarityAdd
BLAST
Topological domaini157 – 393237Cytoplasmic By similarityAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  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. 2 Publications
Mutagenesisi392 – 3921K → D: Abolishes interaction with SNX27. 2 Publications
Mutagenesisi392 – 3921K → E: Does not affect interaction with SNX27. 2 Publications
Mutagenesisi393 – 3931V → I: Abolishes interaction with SNX27. 2 Publications

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.2 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 – 3924

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ63511.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi120 – 1256Selectivity filter By 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 (1 Publication, 1 Publication).

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG72812.
GeneTreeiENSGT00730000110555.
HOGENOMiHOG000237325.
HOVERGENiHBG006178.
InParanoidiQ63511.
KOiK05002.
OMAiDYASFHQ.
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

MAQENAAFSP GSEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT    50
TLVDLQWRLS LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC 100
VNNLNGFVAA FLFSIETETT IGYGHRVITD QCPEGIVLLL LQAILGSMVN 150
AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS LRDGRLCLMF RVGDLRSSHI 200
VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF LVSPLVISHE 250
IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW 300
GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY 350
WSIPSRLDEK VEEEGAGEGA GAGDGADKEQ NGCLPPPESE SKV 393
Length:393
Mass (Da):43,965
Last modified:July 15, 1999 - v2
Checksum:i9CF749672A996608
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L77929 mRNA. Translation: AAB95433.1 .
RefSeqi NP_446286.1. NM_053834.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QDO X-ray 1.88 A 388-393 [» ]
3QE1 X-ray 1.68 A 388-393 [» ]
3QGL X-ray 3.31 F/G/H/I/J 388-393 [» ]
ProteinModelPortali Q63511.
SMRi Q63511. Positions 168-346.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000010113.

PTM databases

PhosphoSitei Q63511.

Proteomic databases

PRIDEi Q63511.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000010113 ; ENSRNOP00000010113 ; ENSRNOG00000007645 .
GeneIDi 116560.
KEGGi rno:116560.

Organism-specific databases

CTDi 3765.
RGDi 621440. Kcnj9.

Phylogenomic databases

eggNOGi NOG72812.
GeneTreei ENSGT00730000110555.
HOGENOMi HOG000237325.
HOVERGENi HBG006178.
InParanoidi Q63511.
KOi K05002.
OMAi DYASFHQ.
OrthoDBi EOG7XPZ5K.
PhylomeDBi Q63511.
TreeFami TF313676.

Miscellaneous databases

EvolutionaryTracei Q63511.
NextBioi 619225.
PROi Q63511.

Gene expression databases

Genevestigatori Q63511.

Family and domain databases

Gene3Di 2.60.40.1400. 1 hit.
InterProi IPR014756. 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 ]
PANTHERi PTHR11767. PTHR11767. 1 hit.
PTHR11767:SF17. PTHR11767:SF17. 1 hit.
Pfami PF01007. IRK. 1 hit.
[Graphical view ]
PIRSFi PIRSF005465. GIRK_kir. 1 hit.
PRINTSi PR01329. KIR33CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMi SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

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: May 14, 2014
This is version 108 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

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