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Protein

ATP-sensitive inward rectifier potassium channel 15

Gene

Kcnj15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei157 – 1571Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesiumBy similarity

GO - Molecular functioni

  1. inward rectifier potassium channel activity Source: GO_Central
  2. potassium channel activity Source: MGI

GO - Biological processi

  1. potassium ion import Source: GO_Central
  2. potassium ion transport Source: MGI
  3. regulation of ion transmembrane transport Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_208837. Activation of G protein gated Potassium channels.
REACT_226457. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-sensitive inward rectifier potassium channel 15
Alternative name(s):
Inward rectifier K(+) channel Kir4.2
Potassium channel, inwardly rectifying subfamily J member 15
Gene namesi
Name:Kcnj15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1310000. Kcnj15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6363CytoplasmicBy similarityAdd
BLAST
Transmembranei64 – 8825Helical; Name=M1By similarityAdd
BLAST
Topological domaini89 – 11325ExtracellularBy similarityAdd
BLAST
Intramembranei114 – 12512Helical; Pore-forming; Name=H5By similarityAdd
BLAST
Intramembranei126 – 1327Pore-formingBy similarity
Topological domaini133 – 1419ExtracellularBy similarity
Transmembranei142 – 16322Helical; Name=M2By similarityAdd
BLAST
Topological domaini164 – 375212CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: MGI
  2. integral component of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375ATP-sensitive inward rectifier potassium channel 15PRO_0000154973Add
BLAST

Proteomic databases

PRIDEiO88932.

PTM databases

PhosphoSiteiO88932.

Expressioni

Gene expression databases

BgeeiO88932.
ExpressionAtlasiO88932. baseline and differential.
GenevestigatoriO88932.

Interactioni

Subunit structurei

Interacts with INADL.By similarity

Protein-protein interaction databases

BioGridi200898. 1 interaction.
IntActiO88932. 1 interaction.
MINTiMINT-1890790.

Structurei

3D structure databases

ProteinModelPortaliO88932.
SMRiO88932. Positions 26-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi127 – 1326Selectivity filterBy similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG289501.
HOGENOMiHOG000237326.
HOVERGENiHBG006178.
InParanoidiO88932.
KOiK05008.
OrthoDBiEOG7GFB4Z.
PhylomeDBiO88932.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003270. K_chnl_inward-rec_Kir1.3.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF20. PTHR11767:SF20. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PIRSFiPIRSF005465. GIRK_kir. 1 hit.
PRINTSiPR01323. KIR13CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

O88932-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDAIHLGMSS APLVKHTNGV GLKAHRPRVM SKSGHSNVRI DKVDGIYLLY
60 70 80 90 100
LQDLWTTVID MKWRYKLTLF AATFVMTWFL FGVVYYAIAF IHGDLQLGES
110 120 130 140 150
NSNHTPCIMK VDSLTGAFLF SLESQTTIGY GVRSITEECP HAIFLLVAQL
160 170 180 190 200
VITTLIEIFI TGTFLAKIAR PKKRAETIKF SHCAVISKQN GKLCLVIQVA
210 220 230 240 250
NMRKSLLIQC QLSGKLLQTH VTKEGERILL NQATVKFHVD SSSESPFLIL
260 270 280 290 300
PMTFYHVLDE TSPLRDLTPQ NLKEKEFELV VLLNATVEST SAVCQSRTSY
310 320 330 340 350
IPEEIYWGFE FVPVVSLSKN GKYVADFSQF EQIRKSPDCT FYCADSEKQK
360 370
LEEQYRQEDQ RERELRSLLL QQSNV
Length:375
Mass (Da):42,605
Last modified:November 1, 1998 - v1
Checksum:i163277597D4B2C8E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141V → W in CAB89666. (PubMed:10906485)Curated
Sequence conflicti99 – 991E → G in CAB89666. (PubMed:10906485)Curated
Sequence conflicti262 – 2621S → K in CAB89666. (PubMed:10906485)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085696 mRNA. Translation: AAC68685.1.
AJ012368 mRNA. Translation: CAB89666.1.
AK085689 mRNA. Translation: BAC39507.1.
BC010794 mRNA. Translation: AAH10794.1.
BC057915 mRNA. Translation: AAH57915.1.
CCDSiCCDS37410.1.
RefSeqiNP_001034145.1. NM_001039056.2.
NP_001258618.1. NM_001271689.1.
NP_001258620.1. NM_001271691.1.
NP_001258622.1. NM_001271693.1.
NP_001258624.1. NM_001271695.1.
NP_062638.1. NM_019664.5.
XP_006523014.1. XM_006522951.1.
XP_006523015.1. XM_006522952.1.
XP_006523249.1. XM_006523186.1.
XP_006523250.1. XM_006523187.1.
XP_006523251.1. XM_006523188.1.
XP_006523252.1. XM_006523189.1.
XP_006523253.1. XM_006523190.1.
XP_006523254.1. XM_006523191.1.
XP_006523255.1. XM_006523192.1.
XP_006523256.1. XM_006523193.1.
UniGeneiMm.272239.
Mm.491313.

Genome annotation databases

EnsembliENSMUST00000113854; ENSMUSP00000109485; ENSMUSG00000062609.
ENSMUST00000113855; ENSMUSP00000109486; ENSMUSG00000062609.
ENSMUST00000113856; ENSMUSP00000109487; ENSMUSG00000062609.
GeneIDi16516.
KEGGimmu:16516.
UCSCiuc008abs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085696 mRNA. Translation: AAC68685.1.
AJ012368 mRNA. Translation: CAB89666.1.
AK085689 mRNA. Translation: BAC39507.1.
BC010794 mRNA. Translation: AAH10794.1.
BC057915 mRNA. Translation: AAH57915.1.
CCDSiCCDS37410.1.
RefSeqiNP_001034145.1. NM_001039056.2.
NP_001258618.1. NM_001271689.1.
NP_001258620.1. NM_001271691.1.
NP_001258622.1. NM_001271693.1.
NP_001258624.1. NM_001271695.1.
NP_062638.1. NM_019664.5.
XP_006523014.1. XM_006522951.1.
XP_006523015.1. XM_006522952.1.
XP_006523249.1. XM_006523186.1.
XP_006523250.1. XM_006523187.1.
XP_006523251.1. XM_006523188.1.
XP_006523252.1. XM_006523189.1.
XP_006523253.1. XM_006523190.1.
XP_006523254.1. XM_006523191.1.
XP_006523255.1. XM_006523192.1.
XP_006523256.1. XM_006523193.1.
UniGeneiMm.272239.
Mm.491313.

3D structure databases

ProteinModelPortaliO88932.
SMRiO88932. Positions 26-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200898. 1 interaction.
IntActiO88932. 1 interaction.
MINTiMINT-1890790.

Chemistry

GuidetoPHARMACOLOGYi439.

PTM databases

PhosphoSiteiO88932.

Proteomic databases

PRIDEiO88932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113854; ENSMUSP00000109485; ENSMUSG00000062609.
ENSMUST00000113855; ENSMUSP00000109486; ENSMUSG00000062609.
ENSMUST00000113856; ENSMUSP00000109487; ENSMUSG00000062609.
GeneIDi16516.
KEGGimmu:16516.
UCSCiuc008abs.1. mouse.

Organism-specific databases

CTDi3772.
MGIiMGI:1310000. Kcnj15.

Phylogenomic databases

eggNOGiNOG289501.
HOGENOMiHOG000237326.
HOVERGENiHBG006178.
InParanoidiO88932.
KOiK05008.
OrthoDBiEOG7GFB4Z.
PhylomeDBiO88932.

Enzyme and pathway databases

ReactomeiREACT_208837. Activation of G protein gated Potassium channels.
REACT_226457. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

Miscellaneous databases

ChiTaRSiKcnj15. mouse.
NextBioi289873.
PROiO88932.
SOURCEiSearch...

Gene expression databases

BgeeiO88932.
ExpressionAtlasiO88932. baseline and differential.
GenevestigatoriO88932.

Family and domain databases

Gene3Di2.60.40.1400. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003270. K_chnl_inward-rec_Kir1.3.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERiPTHR11767. PTHR11767. 1 hit.
PTHR11767:SF20. PTHR11767:SF20. 1 hit.
PfamiPF01007. IRK. 1 hit.
[Graphical view]
PIRSFiPIRSF005465. GIRK_kir. 1 hit.
PRINTSiPR01323. KIR13CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of an inward rectifier current from a Kir 4 family K+ channel gene cloned from mouse liver."
    Pearson W.L., Dourado M., Schreiber M., Nichols C.G., Salkoff L.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Developmentally regulated expression of the murine ortholog of the potassium channel KIR4.2 (KCNJ15)."
    Thiery E., Gosset P., Damotte D., Delezoide A.-L., de Saint-Sauveur N., Vayssettes C., Creau N.
    Mech. Dev. 95:313-316(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  3. "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: Mammary gland.
  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].
    Strain: FVB/N.
    Tissue: Kidney.

Entry informationi

Entry nameiKCJ15_MOUSE
AccessioniPrimary (citable) accession number: O88932
Secondary accession number(s): Q9JK34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: February 4, 2015
This is version 125 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.