Swiss-Prot entry

ID   IRK15_CAVPO    STANDARD;      PRT;   375 AA.
AC   O70339;
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 15 (Potassium
DE   channel, inwardly rectifying, subfamily J, member 15) (Inward
DE   rectifier K(+) channel Kir4.2) (Kir1.3).
GN   Name=KCNJ15;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; 
OC   Hystricognathi; Caviidae; Cavia. 
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9727001 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.273.37.23884;
RA   Derst C., Wischmeyer E., Preisig-Mueller R., Spauschus A., Konrad M.,
RA   Hensen P., Jeck N., Seyberth H.W., Daut J., Karschin A.;
RT   "A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer
RT   medullary potassium) channels reveals a crucial residue for channel
RT   function in Kir1.3 channels.";
RL   J. Biol. Chem. 273:23884-23891(1998).
CC   -!- FUNCTION: Inward rectifier potassium channels are characterized by
CC       a greater tendancy to allow potassium to flow into the cell rather
CC       than out of it. Their voltage dependence is regulated by the
CC       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 (By similarity).
CC   -!- SUBUNIT: Interacts with INADL (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; AF049076; AAC34748.1; -; Genomic_DNA. [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; IPR003270; KIR13_channel.
DR   InterPro; Graphical view of domain structure.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   PANTHER; PTHR11767:SF7; KIR13_channel; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR01323; KIR13CHANNEL.
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; O70339.
DR   ProtoNet; O70339.
DR   ProtoMap; O70339.
DR   PRESAGE; O70339.
DR   DIP; O70339.
DR   ModBase; O70339.
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     63       Cytoplasmic (By similarity).
FT   TRANSMEM     64     88       M1 (By similarity).
FT   TOPO_DOM     89    113       Extracellular (By similarity).
FT   TOPO_DOM    133    141       Extracellular (By similarity).
FT   TRANSMEM    142    163       M2 (By similarity).
FT   TOPO_DOM    164    375       Cytoplasmic (By similarity).
FT   REGION      114    125       H5 (pore-forming helix) (By similarity).
FT   MOTIF       127    132       Selectivity filter (By similarity).
FT   SITE        157    157       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
SQ   SEQUENCE   375 AA;  42829 MW;  1ACC85D34B77CFC0 CRC64;
     MDTIHMSVTR PPPEKHMAGP GLKTHRPRVM SKSGHSNVRI DKVDGIYLLY LQDLWTTVID
     MKWRYKLTLF AATFVMTWFL FGVIYYAIAF IHGDLEPSEA ISNHTPCIMK VDSLTGAFLF
     SLESQTTIGY GVRSITEECP HAIFLLVAQL VITTLIEIFI TGTFLAKIAR PKKRAETIKF
     SHCAVITKQN GKLCLVIQVA NMRKSLLIQC QLSGKLLQTH VTKEGERILL NQATVKFHVD
     SSSESPFLIL PMTFYHVLDE TSPLRDLTPQ NLKEKEFELV VLLNATVEST SAVCQSRTSY
     IPEEIYWGFE FVPVVSLSKN GKYVADFSQF EQIRKSSDCT FYCADSEKQK LEEKYRQEDQ
     RERELRTLLL HQSNV
//