P52187 (IRK12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.
Tissue specificity	Highest level in cerebellum.
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]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Voltage-gated channel
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	inward rectifier potassium channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 427	427	ATP-sensitive inward rectifier potassium channel 12		PRO_0000154963
Regions
	Topological domain	1 – 82	82	Cytoplasmic By similarity
	Transmembrane	83 – 107	25	Helical; Name=M1; By similarity
	Topological domain	108 – 123	16	Extracellular By similarity
	Intramembrane	124 – 128	5	By similarity
	Intramembrane	129 – 141	13	Helical; Pore-forming; Name=H5; By similarity
	Intramembrane	142 – 151	10	Pore-forming; By similarity
	Topological domain	152 – 156	5	Extracellular By similarity
	Transmembrane	157 – 181	25	Helical; Name=M2; By similarity
	Topological domain	182 – 427	246	Cytoplasmic By similarity
	Motif	79 – 81	3	Interaction with phosphatidylinositides By similarity
	Motif	143 – 148	6	Selectivity filter By similarity
	Motif	183 – 190	8	Interaction with phosphatidylinositides By similarity
	Motif	425 – 427	3	PDZ-binding Potential
Sites
	Site	173	1	Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium By similarity
Amino acid modifications
	Disulfide bond	155		Interchain By similarity
Experimental info
	Sequence conflict	177	1	I → N in CAA56622. Ref.1
	Sequence conflict	255	1	F → L in BAA88471. Ref.5
	Sequence conflict	385	1	S → I in CAA56622. Ref.1
	Sequence conflict	393	1	A → S in CAA56622. Ref.1
	Sequence conflict	398 – 400	3	GRS → VRT in CAA56622. Ref.1
	Sequence conflict	418	1	E → V in CAA56622. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P52187 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 3FA101CCF8BCF6AC	FASTA	427	48,427
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00123670. IPI00649845.
RefSeq	NP_001254522.1. NM_001267593.1.
UniGene	Mm.4970.
3D structure databases
ProteinModelPortal	P52187.
SMR	P52187. Positions 42-372.
ModBase	Search...
Proteomic databases
PRIDE	P52187.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000089184; ENSMUSP00000086588; ENSMUSG00000042529. ENSMUST00000108717; ENSMUSP00000104357; ENSMUSG00000042529.
GeneID	16515.
KEGG	mmu:16515.
UCSC	uc007jgy.2. mouse.
Organism-specific databases
CTD	3768.
MGI	MGI:108495. Kcnj12.
Phylogenomic databases
eggNOG	NOG72812.
GeneTree	ENSGT00650000093228.
HOGENOM	HOG000237325.
HOVERGEN	HBG006178.
InParanoid	P52187.
KO	K05005.
OrthoDB	EOG4N04DV.
Gene expression databases
Genevestigator	P52187.
GermOnline	ENSMUSG00000042529. Mus musculus.
Family and domain databases
Gene3D	2.60.40.1400. 1 hit.
InterPro	IPR014756. 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]
PANTHER	PTHR11767. PTHR11767. 1 hit. PTHR11767:SF14. PTHR11767:SF14. 1 hit.
Pfam	PF01007. IRK. 1 hit. PF08466. IRK_N. 1 hit. [Graphical view]
PIRSF	PIRSF005465. GIRK_kir. 1 hit.
PRINTS	PR01325. KIR22CHANNEL. PR01320. KIRCHANNEL.
SUPFAM	SSF81296. Ig_E-set. 1 hit.
ProtoNet	Search...
Other
NextBio	289869.
SOURCE	Search...

Entry information

Entry name

IRK12_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program