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Database: UniProt
Entry: KCJ16_HUMAN
LinkDB: KCJ16_HUMAN
Original site: KCJ16_HUMAN 
ID   KCJ16_HUMAN             Reviewed;         418 AA.
AC   Q9NPI9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-OCT-2019, entry version 157.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11060447; DOI=10.1159/000015662;
RA   Liu Y., McKenna E., Figueroa D.J., Blevins R., Austin C.P.,
RA   Bennett P.B., Swanson R.;
RT   "The human inward rectifier K(+) channel subunit kir5.1 (KCNJ16) maps
RT   to chromosome 17q25 and is expressed in kidney and pancreas.";
RL   Cytogenet. Cell Genet. 90:60-63(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH KCNJ2.
RC   TISSUE=Kidney, and Parathyroid;
RX   PubMed=11240146; DOI=10.1016/s0014-5793(01)02202-5;
RA   Derst C., Karschin C., Wischmeyer E., Hirsch J.R., Preisig-Muller R.,
RA   Rajan S., Engel H., Grzeschik K., Daut J., Karschin A.;
RT   "Genetic and functional linkage of Kir5.1 and Kir2.1 channel
RT   subunits.";
RL   FEBS Lett. 491:305-311(2001).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH KCNJ10
RP   AND MAGI1.
RX   PubMed=24561201; DOI=10.1016/j.febslet.2014.02.024;
RA   Tanemoto M., Abe T., Uchida S., Kawahara K.;
RT   "Mislocalization of K+ channels causes the renal salt wasting in
RT   EAST/SeSAME syndrome.";
RL   FEBS Lett. 588:899-905(2014).
CC   -!- FUNCTION: Inward rectifier potassium channels are characterized by
CC       a greater tendency to allow potassium to flow into the cell rather
CC       than out of it. Their voltage dependence is regulated by the
CC       concentration of extracellular potassium; as external potassium is
CC       raised, the voltage range of the channel opening shifts to more
CC       positive voltages. The inward rectification is mainly due to the
CC       blockage of outward current by internal magnesium. KCNJ16 may be
CC       involved in the regulation of fluid and pH balance. In the kidney,
CC       together with KCNJ10, mediates basolateral K(+) recycling in
CC       distal tubules; this process is critical for Na(+) reabsorption at
CC       the tubules (PubMed:24561201). {ECO:0000305|PubMed:24561201}.
CC   -!- SUBUNIT: Heterodimer with Kir4.1/KCNJ10; this interaction is
CC       required for KCNJ16 localization to the basolateral membrane in
CC       kidney cells. As a heterodimer with KCNJ10, may interact with
CC       MAGI1; this interaction may facilitate KCNJ10/KCNJ16 potassium
CC       channel expression at the basolateral membrane in kidney cells
CC       (PubMed:24561201). May form heterodimers with Kir2.1/KCNJ2
CC       (Probable). {ECO:0000269|PubMed:24561201,
CC       ECO:0000305|PubMed:11240146}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:24561201};
CC       Multi-pass membrane protein. Basolateral cell membrane
CC       {ECO:0000269|PubMed:24561201}. Note=In kidney distal convoluted
CC       tubules, located in the basolateral membrane in the presence of
CC       KCNJ10. {ECO:0000269|PubMed:24561201}.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in adult
CC       and fetal kidney (at protein level). In the kidney, expressed in
CC       the proximal and distal convoluted tubules, but not in glomeruli
CC       nor collecting ducts. {ECO:0000269|PubMed:11060447,
CC       ECO:0000269|PubMed:11240146, ECO:0000269|PubMed:24561201}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ16 subfamily. {ECO:0000305}.
DR   EMBL; AF179353; AAG09401.1; -; mRNA.
DR   EMBL; AF153814; AAF73244.1; -; Genomic_DNA.
DR   EMBL; AF153815; AAF73238.1; -; mRNA.
DR   EMBL; AF153816; AAF73239.1; -; mRNA.
DR   EMBL; AF153817; AAF73240.1; -; mRNA.
DR   CCDS; CCDS11687.1; -.
DR   RefSeq; NP_001257351.1; NM_001270422.1.
DR   RefSeq; NP_001278551.1; NM_001291622.1.
DR   RefSeq; NP_001278552.1; NM_001291623.1.
DR   RefSeq; NP_001278553.1; NM_001291624.1.
DR   RefSeq; NP_001278554.1; NM_001291625.1.
DR   RefSeq; NP_061128.2; NM_018658.2.
DR   RefSeq; NP_733937.2; NM_170741.2.
DR   RefSeq; NP_733938.2; NM_170742.2.
DR   RefSeq; XP_011523083.1; XM_011524781.2.
DR   RefSeq; XP_016880102.1; XM_017024613.1.
DR   SMR; Q9NPI9; -.
DR   BioGrid; 109975; 1.
DR   IntAct; Q9NPI9; 2.
DR   MINT; Q9NPI9; -.
DR   STRING; 9606.ENSP00000465295; -.
DR   TCDB; 1.A.2.1.11; the inward rectifier k(+) channel (irk-c) family.
DR   PhosphoSitePlus; Q9NPI9; -.
DR   BioMuta; KCNJ16; -.
DR   DMDM; 13878562; -.
DR   MassIVE; Q9NPI9; -.
DR   PaxDb; Q9NPI9; -.
DR   PeptideAtlas; Q9NPI9; -.
DR   PRIDE; Q9NPI9; -.
DR   ProteomicsDB; 82023; -.
DR   DNASU; 3773; -.
DR   Ensembl; ENST00000283936; ENSP00000283936; ENSG00000153822.
DR   Ensembl; ENST00000392670; ENSP00000376438; ENSG00000153822.
DR   Ensembl; ENST00000392671; ENSP00000376439; ENSG00000153822.
DR   Ensembl; ENST00000589377; ENSP00000465967; ENSG00000153822.
DR   Ensembl; ENST00000615244; ENSP00000479817; ENSG00000153822.
DR   GeneID; 3773; -.
DR   KEGG; hsa:3773; -.
DR   UCSC; uc002jin.5; human.
DR   CTD; 3773; -.
DR   DisGeNET; 3773; -.
DR   GeneCards; KCNJ16; -.
DR   HGNC; HGNC:6262; KCNJ16.
DR   HPA; HPA059563; -.
DR   MIM; 605722; gene.
DR   neXtProt; NX_Q9NPI9; -.
DR   OpenTargets; ENSG00000153822; -.
DR   PharmGKB; PA30047; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193347; -.
DR   HOGENOM; HOG000237325; -.
DR   InParanoid; Q9NPI9; -.
DR   KO; K05009; -.
DR   OrthoDB; 956263at2759; -.
DR   PhylomeDB; Q9NPI9; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-HSA-1296067; Potassium transport channels.
DR   Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   GeneWiki; KCNJ16; -.
DR   GenomeRNAi; 3773; -.
DR   Pharos; Q9NPI9; -.
DR   PRO; PR:Q9NPI9; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000153822; Expressed in 141 organ(s), highest expression level in adult mammalian kidney.
DR   ExpressionAtlas; Q9NPI9; baseline and differential.
DR   Genevisible; Q9NPI9; HS.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; NAS:UniProtKB.
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; NAS:UniProtKB.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; Complete proteome; Ion channel; Ion transport;
KW   Membrane; Phosphoprotein; Polymorphism; Potassium;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    418       Inward rectifier potassium channel 16.
FT                                /FTId=PRO_0000154975.
FT   TOPO_DOM      1     70       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     71     95       Helical; Name=M1. {ECO:0000250}.
FT   TOPO_DOM     96    117       Extracellular. {ECO:0000250}.
FT   INTRAMEM    118    129       Helical; Pore-forming; Name=H5.
FT                                {ECO:0000250}.
FT   INTRAMEM    130    136       Pore-forming. {ECO:0000250}.
FT   TOPO_DOM    137    145       Extracellular. {ECO:0000250}.
FT   TRANSMEM    146    167       Helical; Name=M2. {ECO:0000250}.
FT   TOPO_DOM    168    418       Cytoplasmic. {ECO:0000250}.
FT   MOTIF       131    136       Selectivity filter. {ECO:0000250}.
FT   SITE        161    161       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium. {ECO:0000250}.
FT   MOD_RES     373    373       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z307}.
FT   MOD_RES     375    375       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z307}.
FT   VARIANT      11     11       I -> V (in dbSNP:rs9302912).
FT                                /FTId=VAR_024510.
SQ   SEQUENCE   418 AA;  47949 MW;  1E241B4C15CBD264 CRC64;
     MSYYGSSYHI INADAKYPGY PPEHIIAEKR RARRRLLHKD GSCNVYFKHI FGEWGSYVVD
     IFTTLVDTKW RHMFVIFSLS YILSWLIFGS VFWLIAFHHG DLLNDPDITP CVDNVHSFTG
     AFLFSLETQT TIGYGYRCVT EECSVAVLMV ILQSILSCII NTFIIGAALA KMATARKRAQ
     TIRFSYFALI GMRDGKLCLM WRIGDFRPNH VVEGTVRAQL LRYTEDSEGR MTMAFKDLKL
     VNDQIILVTP VTIVHEIDHE SPLYALDRKA VAKDNFEILV TFIYTGDSTG TSHQSRSSYV
     PREILWGHRF NDVLEVKRKY YKVNCLQFEG SVEVYAPFCS AKQLDWKDQQ LHIEKAPPVR
     ESCTSDTKAR RRSFSAVAIV SSCENPEETT TSATHEYRET PYQKALLTLN RISVESQM
//
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