Swiss-Prot entry

ID   IRK5_PIG       STANDARD;      PRT;   419 AA.
AC   O02670;
DT   16-OCT-2001 (Rel. 40, Created)
DT   16-OCT-2001 (Rel. 40, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   G protein-activated inward rectifier potassium channel 4 (GIRK4)
DE   (Potassium channel, inwardly rectifying, subfamily J, member 5)
DE   (Inward rectifier K(+) channel Kir3.4) (Heart KATP channel) (KATP-1)
DE   (Cardiac inward rectifier) (CIR).
GN   Name=KCNJ5;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; 
OC   Sus. 
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Heart;
RX   MEDLINE=96430921; PubMed=8834003 [NCBI, ExPASy, EBI, Israel, Japan];
RA   Iizuka M., Kubo Y., Tsunenari I., Pan C.X., Akiba I., Kono T.;
RT   "Functional characterization and localization of a cardiac-type
RT   inwardly rectifying K+ channel.";
RL   Recept. Channels 3:299-315(1995).
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. Can be blocked by
CC       external barium.
CC   -!- SUBUNIT: May associate with GIRK1 and GIRK2 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; D50133; BAA08813.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P35562; 1N9P. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   InterPro; IPR001838; K+channel_IR.
DR   InterPro; IPR001622; K+channel_pore.
DR   InterPro; IPR003277; KIR34_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; PR01330; KIR34CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   ProDom; PD001103; K+channel_IR; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; O02670.
DR   ProtoNet; O02670.
DR   ProtoMap; O02670.
DR   PRESAGE; O02670.
DR   DIP; O02670.
DR   ModBase; O02670.
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     86       Cytoplasmic (By similarity).
FT   TRANSMEM     87    111       M1 (By similarity).
FT   TOPO_DOM    112    135       Extracellular (By similarity).
FT   TOPO_DOM    155    163       Extracellular (By similarity).
FT   TRANSMEM    164    185       M2 (By similarity).
FT   TOPO_DOM    186    419       Cytoplasmic (By similarity).
FT   REGION      136    147       H5 (pore-forming helix) (By similarity).
FT   MOTIF       149    154       Selectivity filter (By similarity).
FT   SITE        179    179       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
SQ   SEQUENCE   419 AA;  47778 MW;  8FCB123056EB10AF CRC64;
     MAGDSRNAMN QDMEIGVTPR DPKKIPKQAR DYIPIATDRT RLLAEGKKPR QRYMEKSGKC
     NVHHGNVQET YRYLSDLFTT LVDLKWRFNL LVFTMVYTVT WLFFGFIWWL IAYIRGDLDH
     VGDQEWIPCV ENLSGFVSAF LFSIETETTI GYGFRVITEK CPEGIVLLLV QAILGSIVNA
     FMVGCMFVKI SQPKKRAETL MFSNHAVISL RDEKLCLMFR VGDLRNSHIV EASIRAKLIK
     SRQTKEGEFI PLNQTDINVG FDTGDDRLFL VSPLIISHEI NEKSPFWEMS RAQLNQEEFE
     VVVILEGMVE ATGMTCQARS SYMDTEVLWG HRFTPVLTLE KGFYEVDYNT FHDTYETNTP
     SCCAKELAEM KREGRLLQYL PSPPLPGGCA GAELEAEAEQ EGEDEPEGLR GSRETRDSV
//