Swiss-Prot entry

ID   IRK9_HUMAN     STANDARD;      PRT;   393 AA.
AC   Q92806;
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 3 (GIRK3)
DE   (Potassium channel, inwardly rectifying, subfamily J, member 9)
DE   (Inwardly rectifier K(+) channel Kir3.3).
GN   Name=KCNJ9; Synonyms=GIRK3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; 
OC   Homo. 
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Schoots O., van Tol H.H.M.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20374464; PubMed=10913335 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1006/bbrc.2000.3136;
RA   Vaughn J., Wolford J.K., Prochazka M., Permana P.A.;
RT   "Genomic structure and expression of human KCNJ9 (Kir3.3/GIRK3).";
RL   Biochem. Biophys. Res. Commun. 274:302-309(2000).
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 (By similarity).
CC   -!- SUBUNIT: Associates with GIRK1 to form a G-protein-activated
CC       heteromultimer pore-forming unit (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; U52152; AAB07043.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF193615; AAF89098.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P35562; 1N9P. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   Ensembl; ENSG00000162728; Homo_sapiens
DR   HGNC; HGNC:6270; KCNJ9.
DR   CleanEx; HGNC:6270; KCNJ9.
DR   MIM; 600932; -. [NCBI / EBI]
DR   GeneCards; KCNJ9.
DR   GeneLynx; KCNJ9.
DR   GenAtlas; KCNJ9.
DR   SOURCE; KCNJ9.
DR   InterPro; IPR001838; K+channel_IR.
DR   InterPro; IPR001622; K+channel_pore.
DR   InterPro; IPR003276; KIR33_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; PR01329; KIR33CHANNEL.
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; Q92806.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q92806.
DR   ProtoNet; Q92806.
DR   ProtoMap; Q92806.
DR   PRESAGE; Q92806.
DR   DIP; Q92806.
DR   ModBase; Q92806.
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     57       Cytoplasmic (By similarity).
FT   TRANSMEM     58     82       M1 (By similarity).
FT   TOPO_DOM     83    106       Extracellular (By similarity).
FT   TOPO_DOM    126    134       Extracellular (By similarity).
FT   TRANSMEM    135    156       M2 (By similarity).
FT   TOPO_DOM    157    393       Cytoplasmic (By similarity).
FT   REGION      107    118       H5 (pore-forming helix) (By similarity).
FT   MOTIF       120    125       Selectivity filter (By similarity).
FT   SITE        150    150       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
SQ   SEQUENCE   393 AA;  44048 MW;  C6F79F96D21C01C9 CRC64;
     MAQENAAFSP GQEEPPRRRG RQRYVEKDGR CNVQQGNVRE TYRYLTDLFT TLVDLQWRLS
     LLFFVLAYAL TWLFFGAIWW LIAYGRGDLE HLEDTAWTPC VNNLNGFVAA FLFSIETETT
     IGYGHRVITD QCPEGIVLLL LQAILGSMVN AFMVGCMFVK ISQPNKRAAT LVFSSHAVVS
     LRDGRLCLMF RVGDLRSSHI VEASIRAKLI RSRQTLEGEF IPLHQTDLSV GFDTGDDRLF
     LVSPLVISHE IDAASPFWEA SRRALERDDF EIVVILEGMV EATGMTCQAR SSYLVDEVLW
     GHRFTSVLTL EDGFYEVDYA SFHETFEVPT PSCSARELAE AAARLDAHLY WSIPSRLDEK
     VEEEGVGEGA GGEAGADKEQ NGCLPPPESE SKV
//