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Protein

ATP-sensitive inward rectifier potassium channel 12

Gene

KCNJ12

Organism
Gallus gallus (Chicken)
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. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification is probably due to the blockage of outward current by cytoplasmic polyamines and/or magnesium ions.2 Publications

GO - Molecular functioni

  • inward rectifier potassium channel activity Source: UniProtKB

GO - Biological processi

  • potassium ion import Source: GO_Central
  • potassium ion transport Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
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

ReactomeiR-GGA-1296041. Activation of G protein gated Potassium channels.
R-GGA-1296053. Classical Kir channels.
R-GGA-5576886. Phase 4 - resting membrane potential.
R-GGA-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-sensitive inward rectifier potassium channel 12
Alternative name(s):
Inward rectifier K(+) channel Kir2.2
Potassium channel, inwardly rectifying subfamily J member 12
Gene namesi
Name:KCNJ12
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8181CytoplasmicAdd
BLAST
Transmembranei82 – 10625Helical; Name=M1Add
BLAST
Topological domaini107 – 12317ExtracellularAdd
BLAST
Intramembranei124 – 1285
Intramembranei129 – 14214Helical; Pore-forming; Name=H5Add
BLAST
Intramembranei143 – 1519Pore-forming
Topological domaini152 – 1565Extracellular
Transmembranei157 – 18125Helical; Name=M2Add
BLAST
Topological domaini182 – 429248CytoplasmicAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: GO_Central
  • intrinsic component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429ATP-sensitive inward rectifier potassium channel 12PRO_0000422544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi155 – 155Interchain1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiF1NHE9.

Expressioni

Gene expression databases

ExpressionAtlasiF1NHE9. baseline.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

DIPiDIP-59161N.
STRINGi9031.ENSGALP00000007506.

Structurei

Secondary structure

1
429
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 574Combined sources
Helixi62 – 687Combined sources
Helixi70 – 767Combined sources
Helixi79 – 10830Combined sources
Helixi110 – 1123Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi123 – 1253Combined sources
Helixi130 – 14112Combined sources
Beta strandi147 – 1515Combined sources
Helixi156 – 18530Combined sources
Helixi187 – 1926Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi208 – 22114Combined sources
Beta strandi223 – 23715Combined sources
Beta strandi243 – 2519Combined sources
Helixi255 – 2573Combined sources
Turni258 – 2603Combined sources
Beta strandi268 – 2736Combined sources
Turni279 – 2824Combined sources
Helixi285 – 2884Combined sources
Beta strandi294 – 30310Combined sources
Turni304 – 3063Combined sources
Beta strandi308 – 31710Combined sources
Helixi318 – 3203Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi331 – 3344Combined sources
Beta strandi337 – 3404Combined sources
Helixi342 – 3443Combined sources
Beta strandi348 – 3503Combined sources
Helixi359 – 36911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JYCX-ray3.11A38-369[»]
3SPCX-ray2.45A38-369[»]
3SPGX-ray2.61A38-369[»]
3SPHX-ray3.00A38-369[»]
3SPIX-ray3.31A38-369[»]
3SPJX-ray3.31A38-369[»]
ProteinModelPortaliF1NHE9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 803Interaction with phosphatidylinositides
Motifi143 – 1486Selectivity filterCurated
Motifi183 – 1908Interaction with phosphatidylinositides

Domaini

Phosphatidylinositol 4,5-bisphosphate binding to the cytoplasmic side of the channel triggers a conformation change leading to channel opening.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3827. Eukaryota.
ENOG410XQ62. LUCA.
HOGENOMiHOG000237325.
InParanoidiF1NHE9.
KOiK05005.
OrthoDBiEOG7XPZ5K.
PhylomeDBiF1NHE9.
TreeFamiTF313676.

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.

F1NHE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAGRVNPYS IVSSEEDGLR LTTMPGINGF GNGKIHTRRK CRNRFVKKNG
60 70 80 90 100
QCNVEFTNMD DKPQRYIADM FTTCVDIRWR YMLLLFSLAF LVSWLLFGLI
110 120 130 140 150
FWLIALIHGD LENPGGDDTF KPCVLQVNGF VAAFLFSIET QTTIGYGFRC
160 170 180 190 200
VTEECPLAVF MVVVQSIVGC IIDSFMIGAI MAKMARPKKR AQTLLFSHNA
210 220 230 240 250
VVAMRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRITEE GEYIPLDQID
260 270 280 290 300
IDVGFDKGLD RIFLVSPITI LHEINEDSPL FGISRQDLET DDFEIVVILE
310 320 330 340 350
GMVEATAMTT QARSSYLASE ILWGHRFEPV LFEEKNQYKV DYSHFHKTYE
360 370 380 390 400
VPSTPRCSAK DLVENKFLLP STNSFCYENE LAFMSRDEDE EDDDSRGLDD
410 420
LSPDNRHEFD RLQATIALDQ RSYRRESEI
Length:429
Mass (Da):49,083
Last modified:May 3, 2011 - v1
Checksum:iE0AF2D60A03D06C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN02023767 Genomic DNA. No translation available.
RefSeqiXP_004945226.1. XM_004945169.2.
XP_004945227.1. XM_004945170.2.
XP_015149865.1. XM_015294379.1.

Genome annotation databases

GeneIDi427662.
KEGGigga:427662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN02023767 Genomic DNA. No translation available.
RefSeqiXP_004945226.1. XM_004945169.2.
XP_004945227.1. XM_004945170.2.
XP_015149865.1. XM_015294379.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JYCX-ray3.11A38-369[»]
3SPCX-ray2.45A38-369[»]
3SPGX-ray2.61A38-369[»]
3SPHX-ray3.00A38-369[»]
3SPIX-ray3.31A38-369[»]
3SPJX-ray3.31A38-369[»]
ProteinModelPortaliF1NHE9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59161N.
STRINGi9031.ENSGALP00000007506.

Proteomic databases

PaxDbiF1NHE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi427662.
KEGGigga:427662.

Organism-specific databases

CTDi3768.

Phylogenomic databases

eggNOGiKOG3827. Eukaryota.
ENOG410XQ62. LUCA.
HOGENOMiHOG000237325.
InParanoidiF1NHE9.
KOiK05005.
OrthoDBiEOG7XPZ5K.
PhylomeDBiF1NHE9.
TreeFamiTF313676.

Enzyme and pathway databases

ReactomeiR-GGA-1296041. Activation of G protein gated Potassium channels.
R-GGA-1296053. Classical Kir channels.
R-GGA-5576886. Phase 4 - resting membrane potential.
R-GGA-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

Miscellaneous databases

PROiF1NHE9.

Gene expression databases

ExpressionAtlasiF1NHE9. baseline.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
    Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
    , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
    Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Red jungle fowl.
  2. "Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution."
    Tao X., Avalos J.L., Chen J., MacKinnon R.
    Science 326:1668-1674(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 38-369, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BOND, SUBUNIT.
  3. "Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2."
    Hansen S.B., Tao X., MacKinnon R.
    Nature 477:495-498(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 38-369, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TOPOLOGY, SUBUNIT.

Entry informationi

Entry nameiKCJ12_CHICK
AccessioniPrimary (citable) accession number: F1NHE9
Secondary accession number(s): D2YW45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: May 3, 2011
Last modified: June 8, 2016
This is version 42 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.