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P48545 (IRK5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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:
G protein-activated inward rectifier potassium channel 4

Short name=GIRK-4
Alternative name(s):
Cardiac inward rectifier
Short name=CIR
Heart KATP channel
Inward rectifier K(+) channel Kir3.4
KATP-1
Potassium channel, inwardly rectifying subfamily J member 5
Gene names
Name:Kcnj5
Synonyms:Girk4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This potassium channel is controlled by G proteins. 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. Can be blocked by external barium.

Subunit structure

May associate with GIRK1 and GIRK2 to form a G-protein-activated heteromultimer pore-forming unit. The resulting inward current is much larger By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Predominantly atrial and pancreatic expression.

Sequence similarities

Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ5 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Voltage-gated channel
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionG-protein activated inward rectifier potassium channel activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419G protein-activated inward rectifier potassium channel 4
PRO_0000154935

Regions

Topological domain1 – 8686Cytoplasmic By similarity
Transmembrane87 – 11125Helical; Name=M1; By similarity
Topological domain112 – 13524Extracellular By similarity
Intramembrane136 – 14712Helical; Pore-forming; Name=H5; By similarity
Intramembrane148 – 1547Pore-forming; By similarity
Topological domain155 – 1639Extracellular By similarity
Transmembrane164 – 18522Helical; Name=M2; By similarity
Topological domain186 – 419234Cytoplasmic By similarity
Motif149 – 1546Selectivity filter By similarity

Sites

Site1791Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium By similarity

Experimental info

Sequence conflict1021L → V in AAB01687. Ref.1
Sequence conflict1091W → G in AAB01687. Ref.1
Sequence conflict1721A → P in AAC53116. Ref.2
Sequence conflict1931P → S in AAB01687. Ref.1
Sequence conflict2141K → N in AAC53116. Ref.2
Sequence conflict2321A → V in AAB01687. Ref.1
Sequence conflict2691F → L in AAB01687. Ref.1
Sequence conflict2871W → V in AAB01687. Ref.1
Sequence conflict2961Q → P in AAC53116. Ref.2
Sequence conflict3511F → S in AAC53116. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48545 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 8383373921C7356A

FASTA41947,669
        10         20         30         40         50         60 
MAGDSRNAMN QDMEIGVTSQ DHKKIPKQAR DYIPIATDRT RLLTEGKKPR QRYMEKTGKC 

        70         80         90        100        110        120 
NVHHGNVQET YRYLSDLFTT LVDLKWRFNL LVFTMVYTIT WLFFGFIWWL IAYVRGDLDH 

       130        140        150        160        170        180 
VGDQEWIPCV ENLSGFVSAF LFSIETETTI GYGFRVITEK CPEGIILLLV QAILGSIVNA 

       190        200        210        220        230        240 
FMVGCMFVKI SQPKKRAETL MFSNNAVISM RDEKLCLMFR VGDLRNSHIV EASIRAKLIK 

       250        260        270        280        290        300 
SRQTKEGEFI PLNQTDINVG FDTGDDRLFL VSPLIISHEI NEKSPFWEMS RAQLEQEEFE 

       310        320        330        340        350        360 
VVVILEGMVE ATGMTCQARS SYMDTEVLWG HRFTPVLTLE KGFYEVDYNT FHDTYETNTP 

       370        380        390        400        410 
SCCAKELAEM KRSGRLLQYL PSPPLLGGCA EAGNEAEAEK DEEGEPNGLS VSQATRGSM 

« Hide

References

« Hide 'large scale' references
[1]"Molecular properties of neuronal G-protein-activated inwardly rectifying K+ channels."
Lesage F., Guillemare E., Fink M., Duprat F., Heurteaux C., Fosset M., Romey G., Barhanin J., Lazdunski M.
J. Biol. Chem. 270:28660-28667(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]Wickman K.D., James M.R., Seldin M.F., Gendler S.J., Clapham D.E.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[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. 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: Embryo.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33631 mRNA. Translation: AAB01687.1.
AF403131 Genomic DNA. Translation: AAC53116.1.
AK164058 mRNA. Translation: BAE37606.1.
CH466522 Genomic DNA. Translation: EDL25354.1.
RefSeqNP_034735.3. NM_010605.4.
XP_006510102.1. XM_006510039.1.
XP_006510103.1. XM_006510040.1.
XP_006510104.1. XM_006510041.1.
UniGeneMm.69472.

3D structure databases

ProteinModelPortalP48545.
SMRP48545. Positions 51-370.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY437.

PTM databases

PhosphoSiteP48545.

Proteomic databases

PRIDEP48545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034533; ENSMUSP00000034533; ENSMUSG00000032034.
GeneID16521.
KEGGmmu:16521.
UCSCuc009orw.1. mouse.

Organism-specific databases

CTD3762.
MGIMGI:104755. Kcnj5.

Phylogenomic databases

eggNOGNOG72812.
GeneTreeENSGT00730000110555.
HOGENOMHOG000237325.
HOVERGENHBG006178.
InParanoidQ3TPX9.
KOK04999.
OMAQARSSYM.
OrthoDBEOG7XPZ5K.
TreeFamTF313676.

Gene expression databases

BgeeP48545.
GenevestigatorP48545.

Family and domain databases

Gene3D2.60.40.1400. 1 hit.
InterProIPR014756. Ig_E-set.
IPR016449. K_chnl_inward-rec_Kir.
IPR003277. K_chnl_inward-rec_Kir3.4.
IPR013518. K_chnl_inward-rec_Kir_cyto.
[Graphical view]
PANTHERPTHR11767. PTHR11767. 1 hit.
PfamPF01007. IRK. 1 hit.
[Graphical view]
PIRSFPIRSF005465. GIRK_kir. 1 hit.
PRINTSPR01330. KIR34CHANNEL.
PR01320. KIRCHANNEL.
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

NextBio289897.
PROP48545.
SOURCESearch...

Entry information

Entry nameIRK5_MOUSE
AccessionPrimary (citable) accession number: P48545
Secondary accession number(s): P97508, Q3TPX9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 115 of the entry and version 3 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