Swiss-Prot entry
ID IRK11_MOUSE STANDARD; PRT; 390 AA.
AC Q61743; Q9QX21;
DT 01-NOV-1997 (Rel. 35, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE ATP-sensitive inward rectifier potassium channel 11 (Potassium
DE channel, inwardly rectifying, subfamily J, member 11) (Inward
DE rectifier K(+) channel Kir6.2).
GN Name=Kcnj11;
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.
RC STRAIN=C57BL/6; TISSUE=Pancreatic islets;
RX MEDLINE=96072967; PubMed=7502040 [NCBI, ExPASy, EBI, Israel, Japan];
RA Inagaki N., Gonoi T., Clement J.P. IV, Namba N., Inazawa J.,
RA Gonzalez G., Aguilar-Bryan L., Seino S., Bryan J.;
RT "Reconstitution of IKATP: an inward rectifier subunit plus the
RT sulfonylurea receptor.";
RL Science 270:1166-1170(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pancreatic islets;
RX MEDLINE=96140543; PubMed=8549751 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0014-5793(95)01369-5;
RA Sakura H., Aemmaelae C., Smith P.A., Gribble F.M., Ashcroft F.M.;
RT "Cloning and functional expression of the cDNA encoding a novel ATP-
RT sensitive potassium channel subunit expressed in pancreatic beta-
RT cells, brain, heart and skeletal muscle.";
RL FEBS Lett. 377:338-344(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/Ola;
RA Kooptiwut S., Shelton K.D., Magnuson M.A.;
RT "Structural characterization of the mouse sulfonylurea receptor-1 and
RT potassium inward rectifier 6.2 genes.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6; TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: This receptor is controled by G proteins. Inward
CC rectifier potassium channels are characterized by a greater
CC tendancy to allow potassium to flow into the cell rather than out
CC 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
CC voltages. The inward rectification is mainly due to the blockage
CC of outward current by internal magnesium. Can be blocked by
CC extracellular barium (By similarity).
CC -!- SUBUNIT: Associates with SUR.
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; D50581; BAA09130.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U73626; AAB17355.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF037313; AAD02096.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC052731; AAH52731.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC057006; AAH57006.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; S68403; S68403.
DR HSSP; P35562; 1N9P. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR Ensembl; ENSMUSG00000058694; Mus_musculus
DR MGI; MGI:107501; Kcnj11.
DR GO; GO:0016021; C:integral to membrane; TAS.
DR InterPro; IPR001838; K+channel_IR.
DR InterPro; IPR001622; K+channel_pore.
DR InterPro; IPR003279; KIR62_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; PR01332; KIR62CHANNEL.
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; Q61743.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q61743.
DR ProtoNet; Q61743.
DR ProtoMap; Q61743.
DR PRESAGE; Q61743.
DR DIP; Q61743.
DR ModBase; Q61743.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Ion transport; Ionic channel; Potassium; Potassium transport;
KW Transmembrane; Transport; Voltage-gated channel.
FT TOPO_DOM 1 68 Cytoplasmic (By similarity).
FT TRANSMEM 69 93 M1 (By similarity).
FT TOPO_DOM 94 116 Extracellular (By similarity).
FT TOPO_DOM 136 144 Extracellular (By similarity).
FT TRANSMEM 145 166 M2 (By similarity).
FT TOPO_DOM 167 390 Cytoplasmic (By similarity).
FT REGION 117 128 H5 (pore-forming helix) (By similarity).
FT MOTIF 130 135 Selectivity filter (By similarity).
FT SITE 160 160 Role in the control of polyamine-mediated
FT channel gating and in the blocking by
FT intracellular magnesium (By similarity).
FT CONFLICT 248 248 G -> S (in Ref. 3).
SQ SEQUENCE 390 AA; 43562 MW; 6AFBFFD284C92C3A CRC64;
MLSRKGIIPE EYVLTRLAED PAEPRYRTRE RRARFVSKKG NCNVAHKNIR EQGRFLQDVF
TTLVDLKWPH TLLIFTMSFL CSWLLFAMVW WLIAFAHGDL APGEGTNVPC VTSIHSFSSA
FLFSIEVQVT IGFGGRMVTE ECPLAILILI VQNIVGLMIN AIMLGCIFMK TAQAHRRAET
LIFSKHAVIT LRHGRLCFML RVGDLRKSMI ISATIHMQVV RKTTSPEGEV VPLHQVDIPM
ENGVGGNGIF LVAPLIIYHV IDSNSPLYDL APSDLHHHQD LEIIVILEGV VETTGITTQA
RTSYLADEIL WGQRFVPIVA EEDGRYSVDY SKFGNTIKVP TPLCTARQLD EDRSLLDALT
LASSRGPLRK RSVAVAKAKP KFSISPDSLS
//