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   24-JAN-2024, entry version 144.
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
CC       (TC 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; 10090-ENSMUSP00000071829; -.
DR   ProteomicsDB; 269187; -.
DR   ABCD; Q8JZN3; 1 sequenced antibody.
DR   Antibodypedia; 68399; 21 antibodies from 14 providers.
DR   DNASU; 211480; -.
DR   Ensembl; ENSMUST00000071937.7; ENSMUSP00000071829.6; ENSMUSG00000058743.7.
DR   GeneID; 211480; -.
DR   KEGG; mmu:211480; -.
DR   UCSC; uc009gxi.1; mouse.
DR   AGR; MGI:2384820; -.
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; 4126787at2759; -.
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 77 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 78 other cell types or tissues.
DR   ExpressionAtlas; Q8JZN3; baseline and differential.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0034702; C:monoatomic ion channel complex; 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 monoatomic ion transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 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:SF40; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 14; 1.
DR   PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 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; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   Genevisible; Q8JZN3; MM.
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
//