KCJ10_RAT
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 03-AUG-2022, entry version 166.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 10;
DE AltName: Full=ATP-sensitive inward rectifier potassium channel KAB-2;
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; Synonyms=Kab-2;
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], AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: May be responsible for potassium buffering action of glial
CC cells in the brain. Inward rectifier potassium channels are
CC characterized by a greater tendency to allow potassium to flow into the
CC cell rather than out of it. Their voltage dependence is regulated by
CC the 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. Can be blocked by
CC extracellular barium and cesium. In the kidney, together with KCNJ16,
CC mediates basolateral K(+) recycling in distal tubules; this process is
CC critical for Na(+) reabsorption at the tubules (By similarity).
CC {ECO:0000250|UniProtKB:P78508}.
CC -!- SUBUNIT: Heterodimer with Kir5.1/KCNJ16; this interaction is required
CC for KCNJ16 localization to the basolateral membrane in kidney cells.
CC Interacts with MAGI1, alone and possibly as a heterodimer with KCNJ16;
CC this interaction may facilitate KCNJ10/KCNJ16 potassium channel
CC expression at the basolateral membrane in kidney cells (By similarity).
CC Interacts with PATJ (By similarity). {ECO:0000250|UniProtKB:P78508,
CC ECO:0000250|UniProtKB:Q9JM63}.
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 (TC
CC 1.A.2.1) family. KCNJ10 subfamily. {ECO:0000305}.
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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 RefSeq; XP_008767959.1; XM_008769737.2.
DR RefSeq; XP_017454263.1; XM_017598774.1.
DR AlphaFoldDB; P49655; -.
DR SMR; P49655; -.
DR BioGRID; 248335; 2.
DR CORUM; P49655; -.
DR IntAct; P49655; 3.
DR MINT; P49655; -.
DR STRING; 10116.ENSRNOP00000010146; -.
DR GuidetoPHARMACOLOGY; 438; -.
DR iPTMnet; P49655; -.
DR PhosphoSitePlus; P49655; -.
DR PaxDb; P49655; -.
DR PRIDE; P49655; -.
DR Ensembl; ENSRNOT00000119639; ENSRNOP00000086322; ENSRNOG00000068444.
DR GeneID; 29718; -.
DR KEGG; rno:29718; -.
DR UCSC; RGD:61822; rat.
DR CTD; 3766; -.
DR RGD; 61822; Kcnj10.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_3_3_1; -.
DR InParanoid; P49655; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P49655; -.
DR TreeFam; TF313676; -.
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 Genevisible; P49655; RN.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006954; P:inflammatory response; IEP: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:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
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:0051930; P:regulation of sensory perception of pain; IMP: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 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; IPR003269; K_chnl_inward-rec_Kir1.2.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF21; PTHR11767:SF21; 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; SSF81296; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Ion channel; Ion transport; Membrane;
KW Nucleotide-binding; Potassium; Potassium transport; Reference proteome;
KW Transmembrane; 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..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..89
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..114
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 115..126
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 127..133
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 134..142
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..164
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 165..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 128..133
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
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 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"
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
