KCJ12_CHICK
ID KCJ12_CHICK Reviewed; 429 AA.
AC F1NHE9; D2YW45;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 12;
DE AltName: Full=Inward rectifier K(+) channel Kir2.2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 12;
GN Name=KCNJ12;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 38-369, FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=20019282; DOI=10.1126/science.1180310;
RA Tao X., Avalos J.L., Chen J., MacKinnon R.;
RT "Crystal structure of the eukaryotic strong inward-rectifier K+ channel
RT Kir2.2 at 3.1 A resolution.";
RL Science 326:1668-1674(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 38-369, FUNCTION, SUBCELLULAR
RP LOCATION, DOMAIN, TOPOLOGY, AND SUBUNIT.
RX PubMed=21874019; DOI=10.1038/nature10370;
RA Hansen S.B., Tao X., MacKinnon R.;
RT "Structural basis of PIP2 activation of the classical inward rectifier K+
RT channel Kir2.2.";
RL Nature 477:495-498(2011).
CC -!- FUNCTION: Inward rectifying potassium channel that is activated by
CC phosphatidylinositol 4,5-bisphosphate and that probably participates in
CC controlling the resting membrane potential in electrically excitable
CC cells. Inward rectifier potassium channels are characterized by a
CC greater tendency to allow potassium to flow into the cell rather than
CC out of it. The inward rectification is probably due to the blockage of
CC outward current by cytoplasmic polyamines and/or magnesium ions.
CC {ECO:0000269|PubMed:20019282, ECO:0000269|PubMed:21874019}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20019282,
CC ECO:0000269|PubMed:21874019}.
CC -!- INTERACTION:
CC F1NHE9; F1NHE9: KCNJ12; NbExp=2; IntAct=EBI-15942324, EBI-15942324;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane; Multi-pass membrane protein.
CC -!- DOMAIN: Phosphatidylinositol 4,5-bisphosphate binding to the
CC cytoplasmic side of the channel triggers a conformation change leading
CC to channel opening. {ECO:0000269|PubMed:21874019}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC family. {ECO:0000305}.
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DR EMBL; AADN02023767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004945226.1; XM_004945169.2.
DR RefSeq; XP_004945227.1; XM_004945170.2.
DR RefSeq; XP_015149865.1; XM_015294379.1.
DR PDB; 3JYC; X-ray; 3.11 A; A=38-369.
DR PDB; 3SPC; X-ray; 2.45 A; A=38-369.
DR PDB; 3SPG; X-ray; 2.61 A; A=38-369.
DR PDB; 3SPH; X-ray; 3.00 A; A=38-369.
DR PDB; 3SPI; X-ray; 3.31 A; A=38-369.
DR PDB; 3SPJ; X-ray; 3.31 A; A=38-369.
DR PDB; 5KUK; X-ray; 2.00 A; A=38-369.
DR PDB; 5KUM; X-ray; 2.80 A; A=38-369.
DR PDB; 6M84; X-ray; 2.81 A; A=38-369.
DR PDB; 6M85; X-ray; 2.71 A; A=38-369.
DR PDB; 6M86; X-ray; 3.60 A; A=38-366.
DR PDBsum; 3JYC; -.
DR PDBsum; 3SPC; -.
DR PDBsum; 3SPG; -.
DR PDBsum; 3SPH; -.
DR PDBsum; 3SPI; -.
DR PDBsum; 3SPJ; -.
DR PDBsum; 5KUK; -.
DR PDBsum; 5KUM; -.
DR PDBsum; 6M84; -.
DR PDBsum; 6M85; -.
DR PDBsum; 6M86; -.
DR AlphaFoldDB; F1NHE9; -.
DR SMR; F1NHE9; -.
DR DIP; DIP-59161N; -.
DR STRING; 9031.ENSGALP00000007506; -.
DR PaxDb; F1NHE9; -.
DR Ensembl; ENSGALT00000007518; ENSGALP00000007506; ENSGALG00000004721.
DR GeneID; 427662; -.
DR KEGG; gga:427662; -.
DR CTD; 3768; -.
DR VEuPathDB; HostDB:geneid_427662; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_3_0_1; -.
DR InParanoid; F1NHE9; -.
DR OMA; MHGMNGF; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; F1NHE9; -.
DR TreeFam; TF313676; -.
DR PRO; PR:F1NHE9; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000004721; Expressed in heart and 4 other tissues.
DR ExpressionAtlas; F1NHE9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 2.60.40.1400; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR041647; IRK_C.
DR InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR InterPro; IPR003272; K_chnl_inward-rec_Kir2.2.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF14; PTHR11767:SF14; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR Pfam; PF08466; IRK_N; 1.
DR PRINTS; PR01325; KIR22CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Ion channel; Ion transport;
KW Membrane; Potassium; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..429
FT /note="ATP-sensitive inward rectifier potassium channel 12"
FT /id="PRO_0000422544"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT TRANSMEM 82..106
FT /note="Helical; Name=M1"
FT TOPO_DOM 107..123
FT /note="Extracellular"
FT INTRAMEM 124..128
FT INTRAMEM 129..142
FT /note="Helical; Pore-forming; Name=H5"
FT INTRAMEM 143..151
FT /note="Pore-forming"
FT TOPO_DOM 152..156
FT /note="Extracellular"
FT TRANSMEM 157..181
FT /note="Helical; Name=M2"
FT TOPO_DOM 182..429
FT /note="Cytoplasmic"
FT REGION 386..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 78..80
FT /note="Interaction with phosphatidylinositides"
FT MOTIF 143..148
FT /note="Selectivity filter"
FT /evidence="ECO:0000305"
FT MOTIF 183..190
FT /note="Interaction with phosphatidylinositides"
FT DISULFID 155
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:20019282"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3JYC"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 79..108
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6M85"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 156..184
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 223..237
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5KUK"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:5KUK"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:5KUK"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 309..317
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5KUK"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:5KUK"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:5KUK"
SQ SEQUENCE 429 AA; 49083 MW; E0AF2D60A03D06C1 CRC64;
MTAGRVNPYS IVSSEEDGLR LTTMPGINGF GNGKIHTRRK CRNRFVKKNG QCNVEFTNMD
DKPQRYIADM FTTCVDIRWR YMLLLFSLAF LVSWLLFGLI FWLIALIHGD LENPGGDDTF
KPCVLQVNGF VAAFLFSIET QTTIGYGFRC VTEECPLAVF MVVVQSIVGC IIDSFMIGAI
MAKMARPKKR AQTLLFSHNA VVAMRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRITEE
GEYIPLDQID IDVGFDKGLD RIFLVSPITI LHEINEDSPL FGISRQDLET DDFEIVVILE
GMVEATAMTT QARSSYLASE ILWGHRFEPV LFEEKNQYKV DYSHFHKTYE VPSTPRCSAK
DLVENKFLLP STNSFCYENE LAFMSRDEDE EDDDSRGLDD LSPDNRHEFD RLQATIALDQ
RSYRRESEI
