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Q92806 (IRK9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. 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.

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 By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Voltage-gated channel
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsynaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionG-protein activated inward rectifier potassium channel activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393G protein-activated inward rectifier potassium channel 3
PRO_0000154950

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

Natural variations

Natural variant3661A → V. Ref.1 Ref.2
Corresponds to variant rs3001040 [ dbSNP | Ensembl ].
VAR_023568

Sequences

Sequence LengthMass (Da)Tools
Q92806 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: C6F79F80A37B01C9

FASTA39344,020
        10         20         30         40         50         60 
MAQENAAFSP GQEEPPRRRG 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 GGEAGADKEQ NGCLPPPESE SKV 

« Hide

References

« Hide 'large scale' references
[1]"Co-expression of human Kir3 subunits can yield channels with different functional properties."
Schoots O., Wilson J.M., Ethier N., Bigras E., Hebert T.E., Van Tol H.H.M.
Cell. Signal. 11:871-883(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-366.
[2]"Genomic structure and expression of human KCNJ9 (Kir3.3/GIRK3)."
Vaughn J., Wolford J.K., Prochazka M., Permana P.A.
Biochem. Biophys. Res. Commun. 274:302-309(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-366.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52152 mRNA. Translation: AAB07043.1.
AF193615 Genomic DNA. Translation: AAF89098.1.
AL121987 Genomic DNA. Translation: CAI15268.1.
RefSeqNP_004974.2. NM_004983.2.
UniGeneHs.66726.

3D structure databases

ProteinModelPortalQ92806.
SMRQ92806. Positions 22-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109967. 2 interactions.
STRING9606.ENSP00000357067.

Chemistry

GuidetoPHARMACOLOGY436.

PTM databases

PhosphoSiteQ92806.

Polymorphism databases

DMDM125987834.

Proteomic databases

PaxDbQ92806.
PRIDEQ92806.

Protocols and materials databases

DNASU3765.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368088; ENSP00000357067; ENSG00000162728.
GeneID3765.
KEGGhsa:3765.
UCSCuc001fuy.1. human.

Organism-specific databases

CTD3765.
GeneCardsGC01P160051.
H-InvDBHIX0028866.
HGNCHGNC:6270. KCNJ9.
MIM600932. gene.
neXtProtNX_Q92806.
PharmGKBPA30051.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72812.
HOGENOMHOG000237325.
HOVERGENHBG006178.
InParanoidQ92806.
KOK05002.
OMAADEVLWG.
OrthoDBEOG7XPZ5K.
PhylomeDBQ92806.
TreeFamTF313676.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

BgeeQ92806.
CleanExHS_KCNJ9.
GenevestigatorQ92806.

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

GeneWikiKCNJ9.
GenomeRNAi3765.
NextBio14763.
PROQ92806.
SOURCESearch...

Entry information

Entry nameIRK9_HUMAN
AccessionPrimary (citable) accession number: Q92806
Secondary accession number(s): Q5JW75
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM