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KCO3_ORYSJ
ID   KCO3_ORYSJ              Reviewed;         456 AA.
AC   Q69TN4; A0A0P0XKR3; Q0J2T7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Two pore potassium channel c;
DE            Short=Two K(+) channel c;
DE   AltName: Full=Calcium-activated outward-rectifying potassium channel 3;
DE            Short=OsKCO3;
GN   Name=TPKC; Synonyms=KCO3; OrderedLocusNames=Os09g0299400, LOC_Os09g12790;
GN   ORFNames=OsJ_28764, OSJNBa0062A09.6;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Inward-rectifying potassium channel. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: Each of the two pore-forming region (also called P-domain or P-
CC       loop) is enclosed by two transmembrane segments (2P/4TM) and contains
CC       the GYGD signature motif which seems to be involved in potassium
CC       selectivity.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC       1.A.1.7) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF24728.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP004736; BAD33183.1; -; Genomic_DNA.
DR   EMBL; AP008215; BAF24728.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014965; BAT07337.1; -; Genomic_DNA.
DR   EMBL; CM000146; EAZ44138.1; -; Genomic_DNA.
DR   RefSeq; XP_015651429.1; XM_015795943.1.
DR   AlphaFoldDB; Q69TN4; -.
DR   SMR; Q69TN4; -.
DR   STRING; 4530.OS09T0299400-00; -.
DR   PaxDb; Q69TN4; -.
DR   PRIDE; Q69TN4; -.
DR   EnsemblPlants; Os09t0299400-00; Os09t0299400-00; Os09g0299400.
DR   GeneID; 4346662; -.
DR   Gramene; Os09t0299400-00; Os09t0299400-00; Os09g0299400.
DR   KEGG; osa:4346662; -.
DR   eggNOG; KOG1418; Eukaryota.
DR   HOGENOM; CLU_033675_2_0_1; -.
DR   InParanoid; Q69TN4; -.
DR   OMA; NEVAIPM; -.
DR   OrthoDB; 774951at2759; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   Genevisible; Q69TN4; OS.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR   InterPro; IPR003280; 2pore_dom_K_chnl.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR11003; PTHR11003; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   3: Inferred from homology;
KW   Calcium; Ion channel; Ion transport; Membrane; Metal-binding; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..456
FT                   /note="Two pore potassium channel c"
FT                   /id="PRO_0000410874"
FT   TOPO_DOM        1..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        192..211
FT                   /note="Pore-forming; Name=Pore-forming 1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        310..329
FT                   /note="Pore-forming; Name=Pore-forming 2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..456
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          373..408
FT                   /note="EF-hand 1"
FT   DOMAIN          412..447
FT                   /note="EF-hand 2"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..70
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         386
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         388
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         390
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         392
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         397
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         425
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         431
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         436
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  49658 MW;  2CCC952FCB72542F CRC64;
     MDTEPLLSPL SPSPHLLHPL PEHAEVSTFS PPLSPCPSPA SSYKERIIFG AHPPPPPPPP
     PPPPPPPRGR RYYRRVSGDD LDVPSCSSSP SPPSDEENPP PNPPSLFDFI GGRTNLHRSR
     TAPAMAPLNA AAIAAAAASG DSRNPPPPPR RPAIVLHAFL FLLAYLAMGV TFYAALPGNF
     TSSAGPTHPV ADALYFCIVT LCTIGYGDIT PATPAAKLFS ISFVLIGFGF VDILLSGMVS
     YVLDLQEHLL ITALKNPRSV RKHRHNYIFD LKKGRMRVRM KVALALTVVA ICVGVGAAVL
     KRVENLGWLD AVYLAVMSVT TVGYGDHAFR TLAGRLFASA WLLVSTLAVA RAFLYLAEMR
     IDKRHRAMAN WVLSRDMTVS EFLAADIDNN GYVTKSEFVV YKLKEMGKIS EKDIMMICDQ
     FQRMDSGNCG KITLSDLLES HQLVTDLNEK KKGKKS
 
 
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