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Q8JZN3 (IRK14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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 14
Alternative name(s):
Inward rectifier K(+) channel Kir2.4
Short name=IRK-4
Potassium channel, inwardly rectifying subfamily J member 14
Gene names
Name:Kcnj14
Synonyms:Irk4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. KCNJ14 gives rise to low-conductance channels with a low affinity to the channel blockers Barium and Cesium By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ14 subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434ATP-sensitive inward rectifier potassium channel 14
PRO_0000154969

Regions

Topological domain1 – 8484Cytoplasmic By similarity
Transmembrane85 – 10925Helical; Name=M1; By similarity
Topological domain110 – 13122Extracellular By similarity
Intramembrane132 – 14312Helical; Pore-forming; Name=H5; By similarity
Intramembrane144 – 1507Pore-forming; By similarity
Topological domain151 – 1599Extracellular By similarity
Transmembrane160 – 18122Helical; Name=M2; By similarity
Topological domain182 – 434253Cytoplasmic By similarity
Motif145 – 1506Selectivity filter By similarity

Experimental info

Sequence conflict321C → F in BAC32051. Ref.1
Sequence conflict2971L → M in BAC27093. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8JZN3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 67DC26097BD75BED

FASTA43447,607
        10         20         30         40         50         60 
MGLARALRRL SGALEPGNSR AGDEEEAGAG LCRNGWAPGP VAGSRRRGRF VKKDGHCNVR 

        70         80         90        100        110        120 
FVNLGGQGAR YLSDLFTTCV DVRWRWMCLL FSCSFLASWL LFGLTFWLIA SLHGDLAAPP 

       130        140        150        160        170        180 
PPAPCFSQVA SFLAAFLFAL ETQTSIGYGV RSVTEECPAA VAAVVLQCIA GCVLDAFVVG 

       190        200        210        220        230        240 
AVMAKMAKPK KRNETLVFSE NAVVALRDHR LCLMWRVGNL RRSHLVEAHV RAQLLQPRVT 

       250        260        270        280        290        300 
PEGEYIPLDH QDVDVGFDGG TDRIFLVSPI TIVHEIDSAS PLYELGRAEL ARADFELVVI 

       310        320        330        340        350        360 
LEGMVEATAM TTQCRSSYLP GELLWGHRFE PVLFQRGSQY EVDYRHFHRT YEVPGTPVCS 

       370        380        390        400        410        420 
AKELDERAEQ ASHSPKSSFP GSLTAFCYEN ELALSCCQEE DEEEDTKEGT SAETPERAAS 

       430 
PQALTPTLAL TLPP 

« Hide

References

[1]"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: Retina.
[2]"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].
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK030711 mRNA. Translation: BAC27093.1.
AK044725 mRNA. Translation: BAC32051.1.
AK080732 mRNA. Translation: BAC38000.1.
BC029692 mRNA. Translation: AAH29692.1.
BC031753 mRNA. Translation: AAH31753.1.
RefSeqNP_666075.1. NM_145963.2.
UniGeneMm.68170.

3D structure databases

ProteinModelPortalQ8JZN3.
SMRQ8JZN3. Positions 47-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000071829.

Proteomic databases

PRIDEQ8JZN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071937; ENSMUSP00000071829; ENSMUSG00000058743.
GeneID211480.
KEGGmmu:211480.
UCSCuc009gxi.1. mouse.

Organism-specific databases

CTD3770.
MGIMGI:2384820. Kcnj14.

Phylogenomic databases

eggNOGNOG251076.
GeneTreeENSGT00650000093228.
HOGENOMHOG000237325.
HOVERGENHBG006178.
InParanoidQ8JZN3.
KOK05007.
OMAPCFSQVA.
OrthoDBEOG7XPZ5K.
PhylomeDBQ8JZN3.
TreeFamTF313676.

Gene expression databases

BgeeQ8JZN3.
GenevestigatorQ8JZN3.

Family and domain databases

Gene3D2.60.40.1400. 1 hit.
InterProIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERPTHR11767. PTHR11767. 1 hit.
PfamPF01007. IRK. 1 hit.
[Graphical view]
PIRSFPIRSF005465. GIRK_kir. 1 hit.
PRINTSPR01320. KIRCHANNEL.
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

NextBio373248.
PROQ8JZN3.
SOURCESearch...

Entry information

Entry nameIRK14_MOUSE
AccessionPrimary (citable) accession number: Q8JZN3
Secondary accession number(s): Q8BMK3, Q8BXM0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 85 of the entry and version 1 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