Swiss-Prot entry

ID   Q969A5_HALRO PRELIMINARY;      PRT;   399 AA.
AC   Q969A5;
DT   01-DEC-2001 (TrEMBLrel. 19, Created)
DT   01-DEC-2001 (TrEMBLrel. 19, Last sequence update)
DT   01-JUN-2003 (TrEMBLrel. 24, Last annotation update)
DE   G-protein coupled inwardly rectifying potassium channel-B.
GN   Name=TuGIRK-B;
OS   Halocynthia roretzi (Sea squirt).
OC   Eukaryota; Metazoa; Chordata; Urochordata; Ascidiacea; 
OC   Stolidobranchia; Pyuridae; Halocynthia. 
OX   NCBI_TaxID=7729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21264655; PubMed=11278535 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.M009644200;
RA   Murata Y., Okado H., Kubo Y.;
RT   "Characterization of heteromultimeric G protein-coupled inwardly
RT   rectifying potassium channels of the tunicate tadpole with a unique
RT   pore property.";
RL   J. Biol. Chem. 276:18529-18539(2001).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       family.
DR   EMBL; AB050441; BAB56015.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P35562; 1N9P. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   GO; GO:0016021; C:integral to membrane; IEA.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potass...; IEA.
DR   GO; GO:0005267; F:potassium channel activity; IEA.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA.
DR   GO; GO:0006811; P:ion transport; IEA.
DR   GO; GO:0006813; P:potassium ion transport; IEA.
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   Pfam; PF01007; IRK; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR01327; KIR31CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   ProtoMap; Q969A5.
DR   PRESAGE; Q969A5.
DR   ModBase; Q969A5.
DR   SMR; Q969A5.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Ion transport; Ionic channel; Potassium; Potassium transport;
KW   Transmembrane; Transport; Voltage-gated channel.
SQ   SEQUENCE   399 AA;  45425 MW;  58BA0438D4F4D3EE CRC64;
     MSLRRHSGGG VQMSAKLAAL RGESIEGASM LDTTTTLSNG DHEVVQIKSK TKQPGRFMTK
     TGHCNIRRSA LQMGTRYMTD IFTTLVDLRW KYNMIIFVFV YTAAWSMFGF LWWMVAFVRG
     DTDINVHNGT DSRKPCVQNV YSYATAFLFY IETETTIGYG KRAMTDQCPE AILLFVIQSL
     LGSIVDAFMV GCIFIKLSQP KNRAETLVFS EHCILTQRDG KYCLMFRVAN LRNSLLIQCK
     IRAKIVKSRQ TLEGEFIGLH QDDINVGFDT GADNLFLVTP LIICHEIDHR SPFYNTNAED
     LQKDKFEIIV ILEGMIESTG MICQARTSYL NTEVLWGHRF MPVLFHARDH FSVDHSEFHT
     TYEVPMPKQS MRRFHDAQVQ NNTKQWHPGS SGYVGNTAA
//