KCJ16_MOUSE
ID KCJ16_MOUSE Reviewed; 419 AA.
AC Q9Z307; Q8BH37;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Inward rectifier potassium channel 16;
DE AltName: Full=Inward rectifier K(+) channel Kir5.1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 16;
GN Name=Kcnj16;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9806850; DOI=10.1006/geno.1998.5572;
RA Mouri T., Kittaka N., Horio Y., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Kurachi Y.;
RT "Assignment of mouse inwardly rectifying potassium channel Kcnj16 to the
RT distal region of mouse chromosome 11.";
RL Genomics 54:181-182(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cochlea;
RA Nie L., Feng W.H., Vazquez A.E., Yamoah E.N.;
RT "Interaction of inner ear-specific Kir channels.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, Corpora quadrigemina, and Olfactory bulb;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-374 AND SER-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=33811157; DOI=10.1681/asn.2020111587;
RA Schlingmann K.P., Renigunta A., Hoorn E.J., Forst A.L., Renigunta V.,
RA Atanasov V., Mahendran S., Barakat T.S., Gillion V., Godefroid N.,
RA Brooks A.S., Lugtenberg D., Lake J., Debaix H., Rudin C., Knebelmann B.,
RA Tellier S., Rousset-Rouviere C., Viering D., de Baaij J.H.F., Weber S.,
RA Palygin O., Staruschenko A., Kleta R., Houillier P., Bockenhauer D.,
RA Devuyst O., Vargas-Poussou R., Warth R., Zdebik A.A., Konrad M.;
RT "Defects in KCNJ16 cause a novel tubulopathy with hypokalemia, salt
RT wasting, disturbed acid-base homeostasis, and sensorineural deafness.";
RL J. Am. Soc. Nephrol. 32:1498-1512(2021).
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. KCNJ16 may be involved in the regulation
CC of fluid and pH balance. In the kidney, together with KCNJ10, mediates
CC basolateral K(+) recycling in distal tubules; this process is critical
CC for Na(+) reabsorption at the tubules. {ECO:0000250|UniProtKB:Q9NPI9}.
CC -!- SUBUNIT: Heterodimer with Kir4.1/KCNJ10; this interaction is required
CC for KCNJ16 localization to the basolateral membrane in kidney cells. As
CC a heterodimer with KCNJ10, may interact with MAGI1; this interaction
CC may facilitate KCNJ10/KCNJ16 potassium channel expression at the
CC basolateral membrane in kidney cells. May form heterodimers with
CC Kir2.1/KCNJ2. {ECO:0000250|UniProtKB:Q9NPI9}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NPI9}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q9NPI9}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:Q9NPI9}. Note=In kidney distal
CC convoluted tubules, located in the basolateral membrane in the presence
CC of KCNJ10. {ECO:0000250|UniProtKB:Q9NPI9}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the proximal and distal
CC segments of the nephron. {ECO:0000269|PubMed:33811157}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ16 subfamily. {ECO:0000305}.
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DR EMBL; AB016197; BAA34723.1; -; mRNA.
DR EMBL; AY377989; AAQ88167.1; -; mRNA.
DR EMBL; AK032192; BAC27749.1; -; mRNA.
DR EMBL; AK045447; BAC32374.1; -; mRNA.
DR EMBL; AK078905; BAC37450.1; -; mRNA.
DR EMBL; AK140249; BAE24297.1; -; mRNA.
DR EMBL; AL592422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34389.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34390.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34391.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34392.1; -; Genomic_DNA.
DR CCDS; CCDS25593.1; -.
DR RefSeq; NP_001239136.1; NM_001252207.1.
DR RefSeq; NP_001239137.1; NM_001252208.1.
DR RefSeq; NP_001239138.1; NM_001252209.2.
DR RefSeq; NP_001239139.1; NM_001252210.2.
DR RefSeq; NP_034734.3; NM_010604.3.
DR AlphaFoldDB; Q9Z307; -.
DR SMR; Q9Z307; -.
DR BioGRID; 200899; 1.
DR IntAct; Q9Z307; 2.
DR STRING; 10090.ENSMUSP00000102246; -.
DR iPTMnet; Q9Z307; -.
DR PhosphoSitePlus; Q9Z307; -.
DR jPOST; Q9Z307; -.
DR MaxQB; Q9Z307; -.
DR PaxDb; Q9Z307; -.
DR PRIDE; Q9Z307; -.
DR ProteomicsDB; 269189; -.
DR Antibodypedia; 31886; 174 antibodies from 29 providers.
DR DNASU; 16517; -.
DR Ensembl; ENSMUST00000106635; ENSMUSP00000102246; ENSMUSG00000051497.
DR Ensembl; ENSMUST00000106636; ENSMUSP00000102247; ENSMUSG00000051497.
DR Ensembl; ENSMUST00000178798; ENSMUSP00000137414; ENSMUSG00000051497.
DR Ensembl; ENSMUST00000180023; ENSMUSP00000136382; ENSMUSG00000051497.
DR GeneID; 16517; -.
DR KEGG; mmu:16517; -.
DR UCSC; uc007mdu.1; mouse.
DR CTD; 3773; -.
DR MGI; MGI:1314842; Kcnj16.
DR VEuPathDB; HostDB:ENSMUSG00000051497; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_3_2_1; -.
DR InParanoid; Q9Z307; -.
DR OMA; HIFGEWE; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q9Z307; -.
DR TreeFam; TF313676; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-1296067; Potassium transport channels.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 16517; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Kcnj16; mouse.
DR PRO; PR:Q9Z307; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9Z307; protein.
DR Bgee; ENSMUSG00000051497; Expressed in adult mammalian kidney and 124 other tissues.
DR ExpressionAtlas; Q9Z307; baseline and differential.
DR Genevisible; Q9Z307; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; ISO:MGI.
DR GO; GO:0010037; P:response to carbon dioxide; ISO:MGI.
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; IPR008061; K_chnl_inward-rec_Kir5.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF24; PTHR11767:SF24; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01678; KIR5CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..419
FT /note="Inward rectifier potassium channel 16"
FT /id="PRO_0000154976"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..95
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 96..117
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 118..129
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 130..136
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 137..145
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 146..167
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 168..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 131..136
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT SITE 161
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 75
FT /note="V -> I (in Ref. 1; BAA34723)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="L -> P (in Ref. 1; BAA34723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 48023 MW; 533D95129D7EB7AF CRC64;
MSYYGSSYRI VNVDSKYPGY PPEHAIAEKR RARRRLLHKD GSCNVYFKHI FGEWGSYMVD
IFTTLVDTKW RHMFVIFSLS YILSWLIFGS IFWLIAFHHG DLLSDPDITP CVDNVHSFTA
AFLFSLETQT TIGYGYRCVT EECSVAVLTV ILQSILSCII NTFIIGAALA KMATARKRAQ
TIRFSYFALI GMRDGKLCLM WRIGDFRPNH VVEGTVRAQL LRYSEDSEGR MTMAFKDLKL
VNDQIILVTP VTIVHEIDHE SPLYALDRKA VAKDNFEILV TFIYTGDSTG TSHQSRSSYI
PREILWGHRF HDVLEVKRKY YKVNCLQFEG SVEVYAPFCS AKQLDWKDQQ LNNLEKTSPA
RGSCNSDTNT RRRSFSAVAV VSSCENPEET VLSPQDECKE MPYQKALLTL NRISMESQM
