ID KCJ10_RAT Reviewed; 379 AA. AC P49655; Q62790; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 04-NOV-2026, entry version 184. DE RecName: Full=ATP-sensitive inward rectifier potassium channel 10; DE AltName: Full=ATP-sensitive inward rectifier potassium channel KAB-2 {ECO:0000303|PubMed:7608203}; DE AltName: Full=BIR10; DE AltName: Full=Brain-specific inwardly rectifying K(+) channel 1; DE Short=BIRK1; DE AltName: Full=Inward rectifier K(+) channel Kir4.1; DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 10; GN Name=Kcnj10 {ECO:0000312|RGD:61822}; GN Synonyms=Kab-2 {ECO:0000303|PubMed:7608203}; 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], TISSUE SPECIFICITY, FUNCTION, TRANSPORTER RP ACTIVITY, AND ACTIVITY REGULATION. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX PubMed=7608203; DOI=10.1074/jbc.270.27.16339; RA Takumi T., Ishii T., Horio Y., Morishige K., Takahashi N., Yamada M., RA Yamashita T., Kiyama H., Sohmiya K., Nakanishi S., Kurachi Y.; RT "A novel ATP-dependent inward rectifier potassium channel expressed RT predominantly in glial cells."; RL J. Biol. Chem. 270:16339-16346(1995). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=7624316; DOI=10.1073/pnas.92.15.6753; RA Bredt D.S., Wang T.L., Cohen N.A., Guggino W.B., Snyder S.H.; RT "Cloning and expression of two brain-specific inwardly rectifying potassium RT channels."; RL Proc. Natl. Acad. Sci. U.S.A. 92:6753-6757(1995). RN [4] RP ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-67. RX PubMed=18690035; DOI=10.4161/chan.5176; RA Rapedius M., Paynter J.J., Fowler P.W., Shang L., Sansom M.S., Tucker S.J., RA Baukrowitz T.; RT "Control of pH and PIP2 gating in heteromeric Kir4.1/Kir5.1 channels by H- RT Bonding at the helix-bundle crossing."; RL Channels 1:327-330(2007). RN [5] RP TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-65; RP GLY-77; CYS-140; THR-164; ALA-167; 199-ARG--VAL-379 AND ARG-297. RX PubMed=20807765; DOI=10.1074/jbc.m110.163170; RA Sala-Rabanal M., Kucheryavykh L.Y., Skatchkov S.N., Eaton M.J., RA Nichols C.G.; RT "Molecular mechanisms of EAST/SeSAME syndrome mutations in Kir4.1 RT (KCNJ10)."; RL J. Biol. Chem. 285:36040-36048(2010). RN [6] RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH PTDINS(4,5)P2, TOPOLOGY, RP DISULFIDE BONDS, AND SUBUNIT. RX PubMed=38355723; DOI=10.1038/s41589-024-01555-y; RA Zhou X., Zhao C., Xu H., Xu Y., Zhan L., Wang P., He J., Lu T., Gu Y., RA Yang Y., Xu C., Chen Y., Liu Y., Zeng Y., Tian F., Chen Q., Xie X., Liu J., RA Hu H., Li J., Zheng Y., Guo J., Gao Z.; RT "Pharmacological inhibition of Kir4.1 evokes rapid-onset antidepressant RT responses."; RL Nat. Chem. Biol. 20:857-866(2024). CC -!- FUNCTION: May be responsible for potassium buffering action of glial CC cells in the brain (PubMed:7608203). Inward rectifier potassium CC channels are characterized by a greater tendency to allow potassium to CC flow into the cell rather than out of it. Their voltage dependence is CC regulated by the concentration of extracellular potassium; as external CC potassium is raised, the voltage range of the channel opening shifts to CC more positive voltages. The inward rectification is mainly due to the CC blockage of outward current by internal magnesium. Can be blocked by CC extracellular barium and cesium (PubMed:7608203). In the kidney, CC together with KCNJ16, mediates basolateral K(+) recycling in distal CC tubules; this process is critical for Na(+) reabsorption at the tubules CC (By similarity). {ECO:0000250|UniProtKB:P78508, CC ECO:0000269|PubMed:7608203}. CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:20807765, ECO:0000269|PubMed:7608203}; CC -!- ACTIVITY REGULATION: Channel activity is strongly regulated by CC variations of cytosolic pH; channels are activated by alkaline and CC inhibited by acidic pH values (PubMed:20807765). Activated by CC phosphatidylinositol 4,5 biphosphate (PtdIns(4,5)P2) (PubMed:18690035). CC Inhibited by Ba(2+) and Cs(+) (PubMed:7608203). CC {ECO:0000269|PubMed:18690035, ECO:0000269|PubMed:20807765, CC ECO:0000269|PubMed:7608203}. CC -!- SUBUNIT: Homotetramer (PubMed:38355723). In kidney cells, it forms CC heteromeric channels with Kir5.1/KCNJ16; this interaction is required CC for KCNJ16 localization to the basolateral membrane. Interacts with CC MAGI1, alone and possibly as a heteromer with KCNJ16; this interaction CC may facilitate KCNJ10/KCNJ16 potassium channel expression at the CC basolateral membrane in kidney cells (By similarity). Interacts with CC PATJ (By similarity). {ECO:0000250|UniProtKB:P78508, CC ECO:0000250|UniProtKB:Q9JM63, ECO:0000269|PubMed:38355723}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P78508}; Multi- CC pass membrane protein {ECO:0000250|UniProtKB:P78508}. Basolateral cell CC membrane {ECO:0000250|UniProtKB:P78508}. Note=In kidney distal CC convoluted tubules, located in the basolateral membrane where it CC colocalizes with KCNJ16. {ECO:0000250|UniProtKB:P78508}. CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, including in CC glial cells of the cerebellum and forebrain. Expressed at lower levels CC in the kidney, and other peripheral tissues. CC {ECO:0000269|PubMed:7608203, ECO:0000269|PubMed:7624316}. CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel CC (TC 1.A.2.1) family. KCNJ10 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X86818; CAA60501.1; -; mRNA. DR EMBL; X83585; CAA58568.1; -; mRNA. DR EMBL; U27558; AAA87811.1; -; mRNA. DR PIR; A57477; A57477. DR RefSeq; NP_113790.2; NM_031602.2. DR PDB; 8I5M; EM; 2.85 A; A/B/C/D=22-357. DR PDB; 8I5N; EM; 2.85 A; A/B/C/D=22-357. DR AlphaFoldDB; P49655; -. DR EMDB; EMD-35195; -. DR EMDB; EMD-35196; -. DR EMDB; EMD-48154; -. DR SMR; P49655; -. DR BioGRID; 248335; 2. DR CORUM; P49655; -. DR FunCoup; P49655; 428. DR IntAct; P49655; 3. DR STRING; 10116.ENSRNOP00000010146; -. DR GuidetoPHARMACOLOGY; 438; -. DR iPTMnet; P49655; -. DR PhosphoSitePlus; P49655; -. DR PaxDb; 10116-ENSRNOP00000010146; -. DR Ensembl; ENSRNOT00000119639.2; ENSRNOP00000086322.1; ENSRNOG00000068444.2. DR Ensembl; ENSRNOT00000131663.1; ENSRNOP00000111743.1; ENSRNOG00000068444.2. DR Ensembl; ENSRNOT00055037599; ENSRNOP00055030661; ENSRNOG00055021910. DR Ensembl; ENSRNOT00060039563; ENSRNOP00060032741; ENSRNOG00060022823. DR Ensembl; ENSRNOT00065045849; ENSRNOP00065037620; ENSRNOG00065026536. DR GeneID; 29718; -. DR KEGG; rno:29718; -. DR UCSC; RGD:61822; rat. DR AGR; RGD:61822; -. DR CTD; 3766; -. DR RGD; 61822; Kcnj10. DR eggNOG; KOG3827; Eukaryota. DR GeneTree; ENSGT01140000282491; -. DR HOGENOM; CLU_022738_3_3_1; -. DR InParanoid; P49655; -. DR OrthoDB; 273257at2759; -. DR PhylomeDB; P49655; -. 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:P49655; -. DR Proteomes; UP000002494; Chromosome 13. DR ExpressionAtlas; P49655; baseline. DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD. DR GO; GO:0097449; C:astrocyte projection; IDA:RGD. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD. DR GO; GO:0044297; C:cell body; ISO:RGD. DR GO; GO:0097546; C:ciliary base; ISO:RGD. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005902; C:microvillus; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:RGD. DR GO; GO:0005267; F:potassium channel activity; ISO:RGD. DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD. DR GO; GO:0007628; P:adult walking behavior; ISO:RGD. DR GO; GO:0035865; P:cellular response to potassium ion; ISO:RGD. DR GO; GO:0022010; P:central nervous system myelination; ISO:RGD. DR GO; GO:0051935; P:glutamate reuptake; ISO:RGD. DR GO; GO:0051938; P:L-glutamate import; IMP:RGD. DR GO; GO:0060081; P:membrane hyperpolarization; IMP:RGD. DR GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD. DR GO; GO:0014003; P:oligodendrocyte development; ISO:RGD. DR GO; GO:0021554; P:optic nerve development; IEP:RGD. DR GO; GO:0055075; P:potassium ion homeostasis; ISO:RGD. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IMP:RGD. DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD. DR GO; GO:0006813; P:potassium ion transport; ISO:RGD. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD. DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD. DR GO; GO:0060075; P:regulation of resting membrane potential; ISO:RGD. DR GO; GO:0009637; P:response to blue light; IEP:RGD. DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD. DR GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD. DR GO; GO:0007601; P:visual perception; ISO:RGD. DR FunFam; 1.10.287.70:FF:000036; ATP-sensitive inward rectifier potassium channel 1; 1. DR FunFam; 2.60.40.1400:FF:000002; ATP-sensitive inward rectifier potassium channel 1; 1. 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; IPR003269; K_chnl_inward-rec_Kir1.2. DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto. DR InterPro; IPR040445; Kir_TM. DR PANTHER; PTHR11767:SF21; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 10; 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; PR01322; KIR12CHANNEL. DR PRINTS; PR01320; KIRCHANNEL. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Disulfide bond; Ion channel; KW Ion transport; Membrane; Nucleotide-binding; Potassium; KW Potassium transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1..379 FT /note="ATP-sensitive inward rectifier potassium channel 10" FT /id="PRO_0000154955" FT TOPO_DOM 1..61 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT TRANSMEM 62..88 FT /note="Helical; Name=M1" FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT TOPO_DOM 89..114 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT INTRAMEM 115..131 FT /note="Discontinuously helical; Pore-forming" FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT TOPO_DOM 132..140 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT TRANSMEM 141..166 FT /note="Helical; Name=M2" FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT TOPO_DOM 167..379 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT MOTIF 128..133 FT /note="Selectivity filter" FT /evidence="ECO:0000250" FT BINDING 36 FT /ligand="1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:83419" FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT BINDING 168 FT /ligand="1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:83419" FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT BINDING 171 FT /ligand="1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:83419" FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT BINDING 173 FT /ligand="1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:83419" FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT BINDING 210..217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT SITE 158 FT /note="Role in the control of polyamine-mediated channel FT gating and in the blocking by intracellular magnesium" FT /evidence="ECO:0000250" FT DISULFID 108..140 FT /evidence="ECO:0000269|PubMed:38355723, FT ECO:0007744|PDB:8I5M" FT MUTAGEN 65 FT /note="R->P: Decreased potassium ion transport. Results in FT a shift to a more alkaline pH for channel activation." FT /evidence="ECO:0000269|PubMed:20807765" FT MUTAGEN 67 FT /note="K->M: Increased activation rate by PtdIns(4,5)P2." FT /evidence="ECO:0000269|PubMed:18690035" FT MUTAGEN 77 FT /note="G->R: Loss of potassium ion transport." FT /evidence="ECO:0000269|PubMed:20807765" FT MUTAGEN 140 FT /note="C->R: Loss of potassium ion transport." FT /evidence="ECO:0000269|PubMed:20807765" FT MUTAGEN 164 FT /note="T->I: Decreased potassium ion transport. Results in FT a shift to a more alkaline pH for channel activation." FT /evidence="ECO:0000269|PubMed:20807765" FT MUTAGEN 167 FT /note="A->V: Decreased potassium ion transport." FT /evidence="ECO:0000269|PubMed:20807765" FT MUTAGEN 199..379 FT /note="Missing: Loss of potassium ion transport." FT /evidence="ECO:0000269|PubMed:20807765" FT MUTAGEN 297 FT /note="R->C: Loss of potassium ion transport. Results in a FT shift to a more alkaline pH for channel activation." FT /evidence="ECO:0000269|PubMed:20807765" FT CONFLICT 73 FT /note="A -> P (in Ref. 3; AAA87811)" FT /evidence="ECO:0000305" FT CONFLICT 76 FT /note="A -> T (in Ref. 3; AAA87811)" FT /evidence="ECO:0000305" FT CONFLICT 110..112 FT /note="VQV -> GAGA (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 115..116 FT /note="LT -> YL (in Ref. 3)" FT /evidence="ECO:0000305" FT CONFLICT 145 FT /note="V -> E (in Ref. 3; AAA87811)" FT /evidence="ECO:0000305" FT CONFLICT 190 FT /note="H -> L (in Ref. 3; AAA87811)" FT /evidence="ECO:0000305" FT CONFLICT 228 FT /note="N -> D (in Ref. 3; AAA87811)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="K -> Q (in Ref. 3; AAA87811)" FT /evidence="ECO:0000305" FT CONFLICT 304 FT /note="E -> R (in Ref. 2; CAA58568)" FT /evidence="ECO:0000305" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:8I5M" FT HELIX 47..53 FT /evidence="ECO:0007829|PDB:8I5M" FT HELIX 55..61 FT /evidence="ECO:0007829|PDB:8I5M" FT HELIX 64..92 FT /evidence="ECO:0007829|PDB:8I5M" FT HELIX 115..126 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:8I5M" FT HELIX 141..170 FT /evidence="ECO:0007829|PDB:8I5M" FT HELIX 173..178 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 186..190 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 193..202 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 208..219 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 239..244 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:8I5M" FT TURN 264..267 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:8I5N" FT STRAND 277..287 FT /evidence="ECO:0007829|PDB:8I5M" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 293..300 FT /evidence="ECO:0007829|PDB:8I5M" FT TURN 302..304 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 306..311 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:8I5N" FT STRAND 321..326 FT /evidence="ECO:0007829|PDB:8I5M" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:8I5M" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:8I5M" SQ SEQUENCE 379 AA; 42480 MW; 77B3671907B68CB2 CRC64; MTSVAKVYYS QTTQTESRPL VAPGIRRRRV LTKDGRSNVR MEHIADKRFL YLKDLWTTFI DMQWRYKLLL FSATFAGTWF LFGVVWYLVA VAHGDLLELG PPANHTPCVV QVHTLTGAFL FSLESQTTIG YGFRYISEEC PLAIVLLIAQ LVLTTILEIF ITGTFLAKIA RPKKRAETIR FSQHAVVAYH NGKLCLMIRV ANMRKSLLIG CQVTGKLLQT HQTKEGENIR LNQVNVTFQV DTASDSPFLI LPLTFYHVVD ETSPLKDLPL RSGEGDFELV LILSGTVEST SATCQVRTSY LPEEILWGYE FTPAISLSAS GKYVADFSLF DQVVKVASPG GLRDSTVRYG DPEKLKLEES LREQAEKEGS ALSVRISNV //