KCJ14_MOUSE
ID KCJ14_MOUSE Reviewed; 434 AA.
AC Q8JZN3; Q8BMK3; Q8BXM0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 14;
DE AltName: Full=Inward rectifier K(+) channel Kir2.4;
DE Short=IRK-4;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 14;
GN Name=Kcnj14; Synonyms=Irk4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: 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. Their voltage dependence is regulated by the concentration
CC of extracellular potassium; as external potassium is raised, the
CC voltage range of the channel opening shifts to more positive voltages.
CC The inward rectification is mainly due to the blockage of outward
CC current by internal magnesium. KCNJ14 gives rise to low-conductance
CC channels with a low affinity to the channel blockers Barium and Cesium
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ14 subfamily. {ECO:0000305}.
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DR EMBL; AK030711; BAC27093.1; -; mRNA.
DR EMBL; AK044725; BAC32051.1; -; mRNA.
DR EMBL; AK080732; BAC38000.1; -; mRNA.
DR EMBL; BC029692; AAH29692.1; -; mRNA.
DR EMBL; BC031753; AAH31753.1; -; mRNA.
DR CCDS; CCDS21265.1; -.
DR RefSeq; NP_666075.1; NM_145963.2.
DR RefSeq; XP_017177583.1; XM_017322094.1.
DR AlphaFoldDB; Q8JZN3; -.
DR SMR; Q8JZN3; -.
DR STRING; 10090.ENSMUSP00000071829; -.
DR PaxDb; Q8JZN3; -.
DR PRIDE; Q8JZN3; -.
DR ProteomicsDB; 269187; -.
DR ABCD; Q8JZN3; 1 sequenced antibody.
DR Antibodypedia; 68399; 20 antibodies from 13 providers.
DR DNASU; 211480; -.
DR Ensembl; ENSMUST00000071937; ENSMUSP00000071829; ENSMUSG00000058743.
DR GeneID; 211480; -.
DR KEGG; mmu:211480; -.
DR UCSC; uc009gxi.1; mouse.
DR CTD; 3770; -.
DR MGI; MGI:2384820; Kcnj14.
DR VEuPathDB; HostDB:ENSMUSG00000058743; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_3_0_1; -.
DR InParanoid; Q8JZN3; -.
DR OMA; CHNGWAP; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q8JZN3; -.
DR TreeFam; TF313676; -.
DR Reactome; R-MMU-1296053; Classical Kir channels.
DR Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR BioGRID-ORCS; 211480; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Kcnj14; mouse.
DR PRO; PR:Q8JZN3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8JZN3; protein.
DR Bgee; ENSMUSG00000058743; Expressed in layer of retina and 76 other tissues.
DR ExpressionAtlas; Q8JZN3; baseline and differential.
DR Genevisible; Q8JZN3; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
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; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; S-nitrosylation; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..434
FT /note="ATP-sensitive inward rectifier potassium channel 14"
FT /id="PRO_0000154969"
FT TOPO_DOM 1..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..109
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 110..131
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 132..143
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 144..150
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 151..159
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 160..181
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 182..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 398..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 145..150
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 413..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P63252"
FT CONFLICT 32
FT /note="C -> F (in Ref. 1; BAC32051)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> M (in Ref. 1; BAC27093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 47607 MW; 67DC26097BD75BED CRC64;
MGLARALRRL SGALEPGNSR AGDEEEAGAG LCRNGWAPGP VAGSRRRGRF VKKDGHCNVR
FVNLGGQGAR YLSDLFTTCV DVRWRWMCLL FSCSFLASWL LFGLTFWLIA SLHGDLAAPP
PPAPCFSQVA SFLAAFLFAL ETQTSIGYGV RSVTEECPAA VAAVVLQCIA GCVLDAFVVG
AVMAKMAKPK KRNETLVFSE NAVVALRDHR LCLMWRVGNL RRSHLVEAHV RAQLLQPRVT
PEGEYIPLDH QDVDVGFDGG TDRIFLVSPI TIVHEIDSAS PLYELGRAEL ARADFELVVI
LEGMVEATAM TTQCRSSYLP GELLWGHRFE PVLFQRGSQY EVDYRHFHRT YEVPGTPVCS
AKELDERAEQ ASHSPKSSFP GSLTAFCYEN ELALSCCQEE DEEEDTKEGT SAETPERAAS
PQALTPTLAL TLPP
