Swiss-Prot entry
ID IRK10_MOUSE STANDARD; PRT; 379 AA.
AC Q9JM63;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 13-SEP-2005 (Rel. 48, Last annotation update)
DE ATP-sensitive inward rectifier potassium channel 10 (Potassium
DE channel, inwardly rectifying, subfamily J, member 10) (Inward
DE rectifier K(+) channel Kir4.1).
GN Name=Kcnj10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Inanobe A., Takahashi K., Tanemoto M., Fujita A., Kurachi Y.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CD-1, and ICR; TISSUE=Brain;
RX MEDLINE=21100968; PubMed=11169792 [NCBI, ExPASy, EBI, Israel, Japan];
RX DOI=10.1002/1098-1136(20010101)33:1<57::AID-GLIA1006>3.0.CO;2-0;
RA Li L., Head V., Timpe L.C.;
RT "Identification of an inward rectifier potassium channel gene
RT expressed in mouse cortical astrocytes.";
RL Glia 33:57-71(2001).
RN [3]
RP INTERACTION WITH INADL.
RX MEDLINE=98313406; PubMed=9647694 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1006/mcne.1998.0679;
RA Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT "CIPP, a novel multivalent PDZ domain protein, selectively interacts
RT with Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT neuroligins.";
RL Mol. Cell. Neurosci. 11:161-172(1998).
CC -!- FUNCTION: May be responsible for potassium buffering action of
CC glial cells in the brain. Inward rectifier potassium channels are
CC characterized by a greater tendancy to allow potassium to flow
CC into the cell rather than out of it. Their voltage dependence is
CC regulated by the concentration of extracellular potassium; as
CC external potassium is raised, the voltage range of the channel
CC opening shifts to more positive voltages. The inward rectification
CC is mainly due to the blockage of outward current by internal
CC magnesium. Can be blocked by extracellular barium and cesium (By
CC similarity).
CC -!- SUBUNIT: Seems to form heterodimer with Kir5.1/KCNJ16 (By
CC similarity). Interacts with INADL.
CC -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC family.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; AB039879; BAA92432.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF322631; AAG42845.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P35562; 1N9P. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR Ensembl; ENSMUSG00000044708; Mus_musculus
DR MGI; MGI:1194504; Kcnj10.
DR GO; GO:0016021; C:integral to membrane; TAS.
DR InterPro; IPR001838; K+channel_IR.
DR InterPro; IPR001622; K+channel_pore.
DR InterPro; IPR003269; KIR12_channel.
DR InterPro; Graphical view of domain structure.
DR PANTHER; PTHR11767; K+channel_IR; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR01322; KIR12CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR ProDom; PD001103; K+channel_IR; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR CMR; Q9JM63.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q9JM63.
DR ProtoNet; Q9JM63.
DR ProtoMap; Q9JM63.
DR PRESAGE; Q9JM63.
DR DIP; Q9JM63.
DR ModBase; Q9JM63.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW ATP-binding; Ion transport; Ionic channel; Nucleotide-binding;
KW Potassium; Potassium transport; Transmembrane; Transport;
KW Voltage-gated channel.
FT TOPO_DOM 1 64 Cytoplasmic (By similarity).
FT TRANSMEM 65 89 M1 (By similarity).
FT TOPO_DOM 90 114 Extracellular (By similarity).
FT TOPO_DOM 134 142 Extracellular (By similarity).
FT TRANSMEM 143 164 M2 (By similarity).
FT TOPO_DOM 165 379 Cytoplasmic (By similarity).
FT NP_BIND 210 217 ATP (Potential).
FT REGION 115 126 H5 (pore-forming helix) (By similarity).
FT MOTIF 128 133 Selectivity filter (By similarity).
FT SITE 158 158 Role in the control of polyamine-mediated
FT channel gating and in the blocking by
FT intracellular magnesium (By similarity).
SQ SEQUENCE 379 AA; 42432 MW; 7FF08446B7F43453 CRC64;
MTSVAKVYYS QTTQTESRPL VAPGIRRRRV LTKDGRSNVR MEHIADKRFL YLKDLWTTFI
DMQWRYKLLL FSATFAGTWF LFGVVWYLVA VAHGDLLELG PPANHTPCVV QVHTLTGAFL
FSLESQTTIG YGFRYISEEC PLAIVLLIAQ LVLTTILEIF ITGTFLAKIA RPKKRAETIR
FSQHAVVASH NGKPCLMIRV ANMRKSLLIG CQVTGKLLQT HQTKEGENIR LNQVNVTFQV
DTASDSPFLI LPLTFYHVVD ETSPLKDLPL RSGEGDFELV LILSGTVEST SATCQVRTSY
LPEEILWGYE FTPAISLSAS GKYIADFSLF DQVVKVASPS GLRDSTVRYG DPEKLKLEES
LREQAEKEGS ALSVRISNV
//