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Protein

ATP-sensitive inward rectifier potassium channel 12

Gene

Kcnj12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei173Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesiumBy similarity1

GO - Molecular functioni

  • inward rectifier potassium channel activity Source: UniProtKB
  • PDZ domain binding Source: RGD

GO - Biological processi

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:
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 namesi
Name:Kcnj12
Synonyms:Irk2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621660. Kcnj12.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 82CytoplasmicBy similarityAdd BLAST82
Transmembranei83 – 107Helical; Name=M1By similarityAdd BLAST25
Topological domaini108 – 123ExtracellularBy similarityAdd BLAST16
Intramembranei124 – 128By similarity5
Intramembranei129 – 141Helical; Pore-forming; Name=H5By similarityAdd BLAST13
Intramembranei142 – 151Pore-formingBy similarity10
Topological domaini152 – 156ExtracellularBy similarity5
Transmembranei157 – 181Helical; Name=M2By similarityAdd BLAST25
Topological domaini182 – 427CytoplasmicBy similarityAdd BLAST246

GO - Cellular componenti

  • dendrite Source: RGD
  • integral component of plasma membrane Source: GO_Central
  • intrinsic component of membrane Source: UniProtKB
  • neuronal cell body Source: RGD
  • T-tubule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi431.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001549641 – 427ATP-sensitive inward rectifier potassium channel 12Add BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei75S-nitrosocysteineBy similarity1
Disulfide bondi155InterchainBy similarity

Keywords - PTMi

Disulfide bond, S-nitrosylation

Proteomic databases

PaxDbiP52188.
PRIDEiP52188.

PTM databases

iPTMnetiP52188.
PhosphoSitePlusiP52188.

Expressioni

Tissue specificityi

Highest level in cerebellum. Moderately found in kidney, forebrain and skeletal muscle. Not detected in uterus, liver and pancreas.1 Publication

Interactioni

Subunit structurei

Homotetramer. Forms heteromer with KCNJ4. Association, via its PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its localization and trafficking.

GO - Molecular functioni

  • PDZ domain binding Source: RGD

Protein-protein interaction databases

IntActiP52188. 8 interactors.
MINTiMINT-158957.
STRINGi10116.ENSRNOP00000054762.

Structurei

3D structure databases

ProteinModelPortaliP52188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi79 – 81Interaction with phosphatidylinositidesBy similarity3
Motifi143 – 148Selectivity filterBy similarity6
Motifi183 – 190Interaction with phosphatidylinositidesBy similarity8
Motifi425 – 427PDZ-bindingSequence analysis3

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3827. Eukaryota.
ENOG410XQ62. LUCA.
HOGENOMiHOG000237325.
HOVERGENiHBG006178.
InParanoidiP52188.
PhylomeDBiP52188.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. 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]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF14. PTHR11767:SF14. 1 hit.
PfamiPF01007. IRK. 1 hit.
PF08466. IRK_N. 1 hit.
[Graphical view]
PRINTSiPR01325. KIR22CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

P52188-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAASRANPY SIVSSEEDGL HLVTMSGANG FGNGKVHTRR RCRNRFVKKN
60 70 80 90 100
GQCNIEFANM DEKSQRYLAD MFTTCVDIRW RYMLLIFSLA FLASWLLFGI
110 120 130 140 150
IFWVIAVAHG DLEPAEGRGR TPCVLQVHGF MAAFLFSIET QTTIGYGLRC
160 170 180 190 200
VTEECPVAVF MVVAQSIVGC IIDSFMIGAI MAKMGRPKKR AQTLLFSHNA
210 220 230 240 250
VVALRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRVTEE GEYIPLDQID
260 270 280 290 300
IDVGFDKGLD RIFLVSPITI LHEIDEASPL FGISRQDLET DDFEIVVILE
310 320 330 340 350
GMVEATAMTT QARSSYLANE ILWGHRFEPV LFEEKNQYKI DYSHFHKTYE
360 370 380 390 400
VPSTPRCSAK DLVENKFLLP SANSFCYENE LAFLSRDEED EVATDRDGRS
410 420
PQPEHDFDRL QASSGALERP YRRESEI
Length:427
Mass (Da):48,399
Last modified:October 1, 1996 - v1
Checksum:i6FA100FEB6066677
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78461 mRNA. Translation: CAA55216.1.
PIRiS43667.
UniGeneiRn.10406.

Genome annotation databases

UCSCiRGD:621660. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78461 mRNA. Translation: CAA55216.1.
PIRiS43667.
UniGeneiRn.10406.

3D structure databases

ProteinModelPortaliP52188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52188. 8 interactors.
MINTiMINT-158957.
STRINGi10116.ENSRNOP00000054762.

Chemistry databases

GuidetoPHARMACOLOGYi431.

PTM databases

iPTMnetiP52188.
PhosphoSitePlusiP52188.

Proteomic databases

PaxDbiP52188.
PRIDEiP52188.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621660. rat.

Organism-specific databases

RGDi621660. Kcnj12.

Phylogenomic databases

eggNOGiKOG3827. Eukaryota.
ENOG410XQ62. LUCA.
HOGENOMiHOG000237325.
HOVERGENiHBG006178.
InParanoidiP52188.
PhylomeDBiP52188.

Miscellaneous databases

PROiP52188.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. 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]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF14. PTHR11767:SF14. 1 hit.
PfamiPF01007. IRK. 1 hit.
PF08466. IRK_N. 1 hit.
[Graphical view]
PRINTSiPR01325. KIR22CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKCJ12_RAT
AccessioniPrimary (citable) accession number: P52188
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.