Swiss-Prot entry

ID   IRK13_HUMAN    STANDARD;      PRT;   360 AA.
AC   O60928; O76023; Q8N3Y4;
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   Inward rectifier potassium channel 13 (Potassium channel, inwardly
DE   rectifying, subfamily J, member 13) (Inward rectifier K(+) channel
DE   Kir7.1).
GN   Name=KCNJ13;
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, AND VARIANT ILE-175.
RC   TISSUE=Brain;
RX   MEDLINE=98408852; PubMed=9738472 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0014-5793(98)00972-7;
RA   Partiseti M., Collura V., Agnel M., Culouscou J.-M., Graham D.;
RT   "Cloning and characterization of a novel human inwardly rectifying
RT   potassium channel predominantly expressed in small intestine.";
RL   FEBS Lett. 434:171-176(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=98282025; PubMed=9620703 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0896-6273(00)80480-8;
RA   Krapivinsky G., Medina I., Eng L., Krapivinsky L., Yang Y.,
RA   Clapham D.E.;
RT   "A novel inward rectifier K+ channel with unique pore properties.";
RL   Neuron 20:995-1005(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Small intestine;
RA   Hirose S., Suzuki Y., Nakamura N.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Nakamura N., Matsuki T., Suzuki Y., Sakuta H., Ito T., Hirose S.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis;
RA   Doering F., Derst C., Wischmeyer E., Karschin C., Daut J.,
RA   Karschin A.;
RT   "Unique epithelial Kir7.1 subunit defines a new subfamily of inwardly
RT   rectifying potassium channels.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-175.
RC   TISSUE=Brain;
RX   MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 147-175.
RX   MEDLINE=99097357; PubMed=9878260 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1006/geno.1998.5598;
RA   Derst C., Doring F., Preisig-M ueller R., Daut J., Karschin A.,
RA   Jeck N., Weber S., Engel H., Grzeschik K.-H.;
RT   "Partial gene structure and assignment to chromosome 2q37 of the human
RT   inwardly rectifying K+ channel (Kir7.1) gene (KCNJ13).";
RL   Genomics 54:560-563(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. KCNJ13 has a
CC       very low single channel conductance, low sensitivity to block by
CC       external barium and cesium, and no dependence of its inward
CC       rectification properties on the internal blocking particle
CC       magnesium.
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC   -!- TISSUE SPECIFICITY: Predominantly expresssed in small intestine.
CC       Expression is also detected in stomach, kidney, and all central
CC       nervous system regions tested with the exception of spinal cord.
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; AJ007557; CAA07552.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF061118; AAC15769.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AB013889; BAA28271.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AB013891; BAA28273.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AJ006128; CAA06878.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; BC037290; AAH37290.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF082182; AAD08673.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P35562; 1N9P. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   Ensembl; ENSG00000115474; Homo_sapiens
DR   HGNC; HGNC:6259; KCNJ13.
DR   CleanEx; HGNC:6259; KCNJ13.
DR   MIM; 603208; -. [NCBI / EBI]
DR   GeneCards; KCNJ13.
DR   GeneLynx; KCNJ13.
DR   GenAtlas; KCNJ13.
DR   SOURCE; KCNJ13.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; NAS.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; NAS.
DR   GO; GO:0006813; P:potassium ion transport; NAS.
DR   InterPro; IPR001838; K+channel_IR.
DR   InterPro; IPR001622; K+channel_pore.
DR   InterPro; IPR008062; KIR7_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; PR01679; KIR7CHANNEL.
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; O60928.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; O60928.
DR   ProtoNet; O60928.
DR   ProtoMap; O60928.
DR   PRESAGE; O60928.
DR   DIP; O60928.
DR   ModBase; O60928.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Ion transport; Ionic channel; Polymorphism; Potassium;
KW   Potassium transport; Transmembrane; Transport; Voltage-gated channel.
FT   TOPO_DOM      1     53       Cytoplasmic (By similarity).
FT   TRANSMEM     54     78       M1 (By similarity).
FT   TOPO_DOM     79    105       Extracellular (By similarity).
FT   TOPO_DOM    125    133       Extracellular (By similarity).
FT   TRANSMEM    134    155       M2 (By similarity).
FT   TOPO_DOM    156    360       Cytoplasmic (By similarity).
FT   REGION      106    117       H5 (pore-forming helix) (By similarity).
FT   MOTIF       119    124       Selectivity filter (By similarity).
FT   SITE        149    149       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
FT   VARIANT     175    175       T -> I (in dbSNP:1801251).
FT                                /FTId=VAR_016193.
FT   CONFLICT    290    290       P -> Q (in Ref. 6).
FT   CONFLICT    309    309       G -> C (in Ref. 6).
SQ   SEQUENCE   360 AA;  40530 MW;  0C49D0DBC619BC50 CRC64;
     MDSSNCKVIA PLLSQRYRRM VTKDGHSTLQ MDGAQRGLAY LRDAWGILMD MRWRWMMLVF
     SASFVVHWLV FAVLWYVLAE MNGDLELDHD APPENHTICV KYITSFTAAF SFSLETQLTI
     GYGTMFPSGD CPSAIALLAI QMLLGLMLEA FITGAFVAKI ARPKNRAFSI RFTDTAVVAH
     MDGKPNLIFQ VANTRPSPLT SVRVSAVLYQ ERENGKLYQT SVDFHLDGIS SDECPFFIFP
     LTYYHSITPS SPLATLLQHE NPSHFELVVF LSAMQEGTGE ICQRRTSYLP SEIMLHHCFA
     SLLTRGSKGE YQIKMENFDK TVPEFPTPLV SKSPNRTDLD IHINGQSIDN FQISETGLTE
//