KCJ16_RAT
ID KCJ16_RAT Reviewed; 419 AA.
AC P52191; Q9JI87;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Inward rectifier potassium channel 16;
DE AltName: Full=BIR9;
DE AltName: Full=Inward rectifier K(+) channel Kir5.1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 16;
GN Name=Kcnj16;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7874445;
RA Bond C.T., Pessia M., Xia X.-M., Lagrutta A., Kavanaugh M.P., Adelman J.P.;
RT "Cloning and expression of a family of inward rectifier potassium
RT channels.";
RL Recept. Channels 2:183-191(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=10764726; DOI=10.1074/jbc.c000127200;
RA Tucker S.J., Imbrici P., Salvatore L., D'Adamo M.C., Pessia M.;
RT "pH dependence of the inwardly rectifying potassium channel, Kir5.1, and
RT localization in renal tubular epithelia.";
RL J. Biol. Chem. 275:16404-16407(2000).
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 (By similarity). In the kidney, together with
CC KCNJ10, mediates basolateral K(+) recycling in distal tubules; this
CC process is critical for Na(+) reabsorption at the tubules.
CC {ECO:0000250, 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: Expressed in the brain, testis, liver, spleen,
CC kidney, submaxillary gland and adrenals. In the kidney, expressed in
CC the epithelial cells of both proximal and distal convoluted tubules, in
CC the endothelial cells surrounding glomerular capillaries and in the
CC flattened parietal layer of Bowman's capsule.
CC {ECO:0000269|PubMed:10764726}.
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; X83581; CAA58564.1; -; mRNA.
DR EMBL; AF249676; AAF74265.1; -; Genomic_DNA.
DR AlphaFoldDB; P52191; -.
DR SMR; P52191; -.
DR STRING; 10116.ENSRNOP00000006238; -.
DR iPTMnet; P52191; -.
DR PhosphoSitePlus; P52191; -.
DR PaxDb; P52191; -.
DR PRIDE; P52191; -.
DR RGD; 61824; Kcnj16.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; P52191; -.
DR PhylomeDB; P52191; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-1296067; Potassium transport channels.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P52191; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; IMP:RGD.
DR GO; GO:0010037; P:response to carbon dioxide; IMP:RGD.
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 2: Evidence at transcript 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_0000154977"
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:0000250|UniProtKB:Q9Z307"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z307"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z307"
FT CONFLICT 361..419
FT /note="RGSCTSDTNTRRRSFSAVAMVSSCENPEETSLSPQDECKEVPYQKALLTLNR
FT ISMESQM -> PRILHLGHQHQEEILQRSCHGEQL (in Ref. 1; CAA58564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 47936 MW; ACE54A72D511A11C CRC64;
MSYYGSSYRI VNVDSKYPGY PPEHAIAEKR RARRRLLHKD GSCNVYFKHI FGEWGSYMVD
IFTTLVDTKW RHMFVVFSLS YILSWLIFGS IFWLIALHHG DLLSDPDITP CVDNVHSFTA
AFLFSLETQT TIGYGYRCVT EECSVAVLTV ILQSILSCII NTFIIGAALA KMATARKRAQ
TIRFSYFALI GMRDGKLCLM WRIGDFRPNH VVEGTVRAQL LRYSEDSEGR MTMAFKDLKL
VNDQIILVTP VTIVHEIDHE SPLYALDRKA VAKDNFEILV TFIYTGDSTG TSHQSRSSYV
PREILWGHRF HDVLEVKRKY YKVNCLQFEG SVEVYAPFCS AKQLDWKDQQ LNNLEKTSPA
RGSCTSDTNT RRRSFSAVAM VSSCENPEET SLSPQDECKE VPYQKALLTL NRISMESQM
