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1.A.2.1.2
G-protein enhanced inward rectifier K channel 2, IRK2 (Kir2.1) (Andersen-Tawil Syndrome (ATS-1) protein; the V302M mutation causing the syndrome, alters the G-loop cytoplasmic K conduction pathway) (Bendahhou et al., 2003; Ma et al., 2007). (Blocked by chloroquine which binds in the cytoplasmic pore domain (Rodriguez-Menchaca et al., 2008)). Forms heteromultimers with Kir3.1 and Kir3.4 (Ishihara et al., 2009). A C-terminal domain is critical for the sensitivity of Kir2.1 to cholesterol (Epshtein et al., 2009). Flecainide increases Kir2.1 currents by interacting with cysteine 311, decreasing the polyamine-induced rectification (Caballero et al., 2010).  The inhibitory cholesterol binding site has been identified (Fürst et al. 2014).  Polyamines and Mg2+ block ion flux synergistically (Huang and Kuo 2016).

Accession Number:P63252
Protein Name:Inward rectifier potassium channel 2 aka IRK2
Length:427
Molecular Weight:48288.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:4
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate K+

Cross database links:

Genevestigator: P63252
eggNOG: prNOG10748
HEGENOM: HBG716702
RefSeq: NP_000882.1   
Entrez Gene ID: 3759   
Pfam: PF01007    PF08466   
OMIM: 170390  phenotype
600681  gene
609622  phenotype
KEGG: hsa:3759   

Gene Ontology

GO:0005887 C:integral to plasma membrane
GO:0005242 F:inward rectifier potassium channel activity
GO:0005515 F:protein binding
GO:0006813 P:potassium ion transport

References (10)

[1] “Molecular cloning and expression of a human heart inward rectifier potassium channel.”  Raab-Graham K.F.et.al.   7696590
[2] “Cloning and functional expression of a human gene, hIRK1, encoding the heart inward rectifier K+-channel.”  Wood L.S.et.al.   7590287
[3] “Inwardly rectifying whole cell potassium current in human blood eosinophils.”  Tare M.et.al.   9490857
[4] “Genetic and functional linkage of Kir5.1 and Kir2.1 channel subunits.”  Derst C.et.al.   11240146
[5] “Inward rectifier K+ channel from human heart and brain: cloning and stable expression in a human cell line.”  Ashen M.D.et.al.   7840300
[6] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[7] “Mutations in Kir2.1 cause the developmental and episodic electrical phenotypes of Andersen's syndrome.”  Plaster N.M.et.al.   11371347
[8] “KCNJ2 mutation results in Andersen syndrome with sex-specific cardiac and skeletal muscle phenotypes.”  Andelfinger G.et.al.   12148092
[9] “Functional and clinical characterization of KCNJ2 mutations associated with LQT7 (Andersen syndrome).”  Tristani-Firouzi M.et.al.   12163457
[10] “A novel form of short QT syndrome (SQT3) is caused by a mutation in the KCNJ2 gene.”  Priori S.G.et.al.   15761194

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN 
61:	VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDASKEGK 
121:	ACVSEVNSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM 
181:	AKMAKPKKRN ETLVFSHNAV IAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG 
241:	EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDIDNA DFEIVVILEG 
301:	MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD 
361:	LAEKKYILSN ANSFCYENEV ALTSKEEDDS ENGVPESTST DTPPDIDLHN QASVPLEPRP 
421:	LRRESEI