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P52187 (IRK12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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:
ATP-sensitive inward rectifier potassium channel 12
Alternative name(s):
Inward rectifier K(+) channel Kir2.2
Short name=IRK-2
Potassium channel, inwardly rectifying subfamily J member 12
Gene names
Name:Kcnj12
Synonyms:Irk2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. 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. Ref.1

Subunit structure

Homotetramer. Association, via its PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its localization and trafficking By similarity.

Subcellular location

Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein By similarity Ref.1.

Tissue specificity

Highest level in cerebellum. Ref.1

Domain

Phosphatidylinositol 4,5-bisphosphate binding to the cytoplasmic side of the channel triggers a conformation change leading to channel opening By similarity.

Sequence similarities

Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ12 subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427ATP-sensitive inward rectifier potassium channel 12
PRO_0000154963

Regions

Topological domain1 – 8282Cytoplasmic By similarity
Transmembrane83 – 10725Helical; Name=M1; By similarity
Topological domain108 – 12316Extracellular By similarity
Intramembrane124 – 1285 By similarity
Intramembrane129 – 14113Helical; Pore-forming; Name=H5; By similarity
Intramembrane142 – 15110Pore-forming; By similarity
Topological domain152 – 1565Extracellular By similarity
Transmembrane157 – 18125Helical; Name=M2; By similarity
Topological domain182 – 427246Cytoplasmic By similarity
Motif79 – 813Interaction with phosphatidylinositides By similarity
Motif143 – 1486Selectivity filter By similarity
Motif183 – 1908Interaction with phosphatidylinositides By similarity
Motif425 – 4273PDZ-binding Potential

Sites

Site1731Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium By similarity

Amino acid modifications

Disulfide bond155Interchain By similarity

Experimental info

Sequence conflict1771I → N in CAA56622. Ref.1
Sequence conflict2551F → L in BAA88471. Ref.5
Sequence conflict3851S → I in CAA56622. Ref.1
Sequence conflict3931A → S in CAA56622. Ref.1
Sequence conflict398 – 4003GRS → VRT in CAA56622. Ref.1
Sequence conflict4181E → V in CAA56622. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52187 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 3FA101CCF8BCF6AC

FASTA42748,427
        10         20         30         40         50         60 
MTAASRANPY SIVSSEEDGL HLVTMSGANG FGNGKVHTRR RCRNRFVKKN GQCNIEFANM 

        70         80         90        100        110        120 
DEKSQRYLAD MFTTCVDIRW RYMLLIFSLA FLASWLLFGI IFWVIAVAHG DLEPAEGRGR 

       130        140        150        160        170        180 
TPCVLQVHGF MAAFLFSIET QTTIGYGLRC VTEECPVAVF MVVAQSIVGC IIDSFMIGAI 

       190        200        210        220        230        240 
MAKMARPKKR AQTLLFSHNA VVALRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRVTEE 

       250        260        270        280        290        300 
GEYIPLDQID IDVGFDKGLD RIFLVSPITI LHEIDEASPL FGISRQDLET DDFEIVVILE 

       310        320        330        340        350        360 
GMVEATAMTT QARSSYLANE ILWGHRFEPV LFEEKNQYKI DYSHFHKTYE VPSTPRCSAK 

       370        380        390        400        410        420 
DLVENKFLLP SANSFCYENE LAFLSRDEED EVATDRDGRS PQPEHDFDRL QASSAALERP 


YRRESEI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional expression of cDNA encoding a second class of inward rectifier potassium channels in the mouse brain."
Takahashi N., Morishige K., Jahangir A., Yamada M., Findlay I., Koyama H., Kurachi Y.
J. Biol. Chem. 269:23274-23279(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Olfactory bulb.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Inward recifier potassium channel IRK2."
Ikeda K., Kobayashi T.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-420.
Strain: C57BL/6NJcl.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X80417 mRNA. Translation: CAA56622.1.
AK032271 mRNA. Translation: BAC27788.1.
AL646093 Genomic DNA. Translation: CAI25892.1.
BC115970 mRNA. Translation: AAI15971.1.
BC116677 mRNA. Translation: AAI16678.1.
AB035889 mRNA. Translation: BAA88471.1.
RefSeqNP_001254522.1. NM_001267593.1.
XP_006532381.1. XM_006532318.1.
UniGeneMm.4970.

3D structure databases

ProteinModelPortalP52187.
SMRP52187. Positions 42-372.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY431.

Proteomic databases

PRIDEP52187.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089184; ENSMUSP00000086588; ENSMUSG00000042529.
ENSMUST00000108717; ENSMUSP00000104357; ENSMUSG00000042529.
GeneID16515.
KEGGmmu:16515.
UCSCuc007jgy.2. mouse.

Organism-specific databases

CTD3768.
MGIMGI:108495. Kcnj12.

Phylogenomic databases

eggNOGNOG72812.
GeneTreeENSGT00650000093228.
HOGENOMHOG000237325.
HOVERGENHBG006178.
InParanoidP52187.
KOK05005.
OrthoDBEOG7XPZ5K.
TreeFamTF313676.

Gene expression databases

GenevestigatorP52187.

Family and domain databases

Gene3D2.60.40.1400. 1 hit.
InterProIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003272. K_chnl_inward-rec_Kir2.2.
IPR013518. K_chnl_inward-rec_Kir_cyto.
IPR013673. K_chnl_inward-rec_Kir_N.
[Graphical view]
PANTHERPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF14. PTHR11767:SF14. 1 hit.
PfamPF01007. IRK. 1 hit.
PF08466. IRK_N. 1 hit.
[Graphical view]
PIRSFPIRSF005465. GIRK_kir. 1 hit.
PRINTSPR01325. KIR22CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

NextBio289869.
PROP52187.
SOURCESearch...

Entry information

Entry nameIRK12_MOUSE
AccessionPrimary (citable) accession number: P52187
Secondary accession number(s): Q8CCR0, Q9QYF2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 112 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot