Swiss-Prot entry

ID   IRK3_CHICK     STANDARD;      PRT;   492 AA.
AC   Q90854;
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   G protein-activated inward rectifier potassium channel 1 (GIRK1)
DE   (Potassium channel, inwardly rectifying, subfamily J, member 3)
DE   (Inward rectifier K(+) channel Kir3.1).
GN   Name=KCNJ3; Synonyms=GIRK1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; 
OC   Gallus. 
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=96198105; PubMed=8626438 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.271.11.6398;
RA   Gadbut A.P., Riccardi D., Wu L.Y., Hebert S.C., Galper J.B.;
RT   "Specificity of coupling of muscarinic receptor isoforms to a novel
RT   chick inward-rectifying acetylcholine-sensitive K+ channel.";
RL   J. Biol. Chem. 271:6398-6402(1996).
CC   -!- FUNCTION: This potassium channel is controlled by G proteins.
CC       Inward 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. This receptor plays a
CC       crucial role in regulating the heartbeat (By similarity).
CC   -!- SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein
CC       activated heteromultimer pore-forming unit. The resulting inward
CC       current is much larger (By similarity).
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; L35555; AAA64786.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; I50235; I50235.
DR   HSSP; P35562; 1N9P. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q90854; 181-362.
DR   Ensembl; ENSGALG00000012537; Gallus_gallus
DR   InterPro; IPR001838; K+channel_IR.
DR   InterPro; IPR001622; K+channel_pore.
DR   InterPro; IPR003274; KIR31_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; PR01327; KIR31CHANNEL.
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; Q90854.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q90854.
DR   ProtoNet; Q90854.
DR   ProtoMap; Q90854.
DR   PRESAGE; Q90854.
DR   DIP; Q90854.
DR   ModBase; Q90854.
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     72       Cytoplasmic (By similarity).
FT   TRANSMEM     73     97       M1 (By similarity).
FT   TOPO_DOM     98    121       Extracellular (By similarity).
FT   TOPO_DOM    141    149       Extracellular (By similarity).
FT   TRANSMEM    150    171       M2 (By similarity).
FT   TOPO_DOM    172    492       Cytoplasmic (By similarity).
FT   REGION      122    133       H5 (pore-forming helix) (By similarity).
FT   MOTIF       135    140       Selectivity filter (By similarity).
FT   SITE        165    165       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
SQ   SEQUENCE   492 AA;  55417 MW;  77E924317413B15B CRC64;
     MSALRRKLGD EYQVVSTSAS GGGLPPPRAA PRGKRQRFVD KNGRCNVQHG NLGGETSRYL
     SDLFTTLVDL KWRWNLFIFV LTYTVAWLFM ASMWWVIAYM RGDLNKAHDD SYTPCVANVY
     NFPSAFLFFI ETEATIGYGY RYITDKCPEG IILFLFQSIL GSIVDAFLIG CMFIKMSQPK
     KRAETLMFSE HAAISMRDGK LTLMFRVGNL RNSHMVSAQI RCKLLKSRQT PEGEFLPLDQ
     LELDVGFSTG ADQLFLVSPL TICHVIDAKS PFYDLSQRTM QTEQFEIVVI LEGIVETTGM
     TCQARTSYTE DEVLWGHRFF PVISLEEGFF KVDYSQFHAT FEVPTPPYSV KEQEEMLLMS
     SPLIAPAVSN SKERNNSVEC LDGLDEVGIK LPSKLQKITG RDDFPKKLLR ISSTTSEKAY
     SMGDLPMKLQ RISSVPGNSE EKLVSKATKM MSDPMSQSVA DLPPKLQKLS GGGRMEGNLP
     PKLRKMNSDR FT
//