KCO1_ORYSJ
ID KCO1_ORYSJ Reviewed; 347 AA.
AC Q850M0; A0A0P0W378;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Two pore potassium channel a;
DE Short=Two K(+) channel a;
DE AltName: Full=Calcium-activated outward-rectifying potassium channel 1;
DE Short=OsKCO1;
GN Name=TPKA; Synonyms=KCO1; OrderedLocusNames=Os03g0752300, LOC_Os03g54100;
GN ORFNames=OJ1112_G08.7, OsJ_12594, OSJNBa0032E21.10, OSJNBa0047E24.7;
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=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
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 [3]
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 [4]
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 [5]
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-292; VAL-303;
RP ASN-313; LYS-326; ASP-330; GLY-333 AND TYR-338.
RX PubMed=21224427; DOI=10.1105/tpc.110.081463;
RA Isayenkov S., Isner J.C., Maathuis F.J.;
RT "Rice two-pore K+ channels are expressed in different types of vacuoles.";
RL Plant Cell 23:756-768(2011).
CC -!- FUNCTION: Highly selective inward-rectifying potassium channel that is
CC specifically located in the tonoplast of large vacuoles. Functions
CC independently of the voltage difference across the membrane.
CC {ECO:0000269|PubMed:21224427}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:21224427};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21224427}.
CC Note=Tonoplast of large vacuoles.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC092556; AAR87255.1; -; Genomic_DNA.
DR EMBL; AC135225; AAP68365.1; -; Genomic_DNA.
DR EMBL; AF377947; AAO32309.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98918.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98919.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13212.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86423.1; -; Genomic_DNA.
DR EMBL; CM000140; EAZ28607.1; -; Genomic_DNA.
DR EMBL; AK069303; BAG91366.1; -; mRNA.
DR RefSeq; XP_015630528.1; XM_015775042.1.
DR RefSeq; XP_015630529.1; XM_015775043.1.
DR RefSeq; XP_015630530.1; XM_015775044.1.
DR RefSeq; XP_015630531.1; XM_015775045.1.
DR AlphaFoldDB; Q850M0; -.
DR SMR; Q850M0; -.
DR STRING; 4530.OS03T0752300-01; -.
DR PaxDb; Q850M0; -.
DR PRIDE; Q850M0; -.
DR EnsemblPlants; Os03t0752300-01; Os03t0752300-01; Os03g0752300.
DR GeneID; 4334137; -.
DR Gramene; Os03t0752300-01; Os03t0752300-01; Os03g0752300.
DR KEGG; osa:4334137; -.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_0_1_1; -.
DR InParanoid; Q850M0; -.
DR OMA; HPSKIPM; -.
DR OrthoDB; 774951at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q850M0; OS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0031004; C:potassium ion-transporting ATPase complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
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:0030007; P:cellular potassium ion homeostasis; IC:UniProtKB.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR031144; TPK_plant.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR PANTHER; PTHR11003:SF137; PTHR11003:SF137; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Ion channel; Ion transport; Membrane; Metal-binding; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..347
FT /note="Two pore potassium channel a"
FT /id="PRO_0000410872"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 99..118
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 213..232
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 276..311
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 315..347
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MUTAGEN 292
FT /note="D->G: No effect on targeting to large vacuole."
FT /evidence="ECO:0000269|PubMed:21224427"
FT MUTAGEN 303
FT /note="V->L: Mainly targeted to large vacuole and partly to
FT protein storage vacuole. Almost completely targeted to
FT protein storage vacuole; when associated with S-313."
FT /evidence="ECO:0000269|PubMed:21224427"
FT MUTAGEN 313
FT /note="N->S: Equally targeted to large vacuole and protein
FT storage vacuole. Almost completely targeted to protein
FT storage vacuole; when associated with L-303."
FT /evidence="ECO:0000269|PubMed:21224427"
FT MUTAGEN 326
FT /note="K->N: Mainly targeted to protein storage vacuole."
FT /evidence="ECO:0000269|PubMed:21224427"
FT MUTAGEN 330
FT /note="D->H: Mainly targeted to large vacuole and partly to
FT the ER; when associated with A-333."
FT /evidence="ECO:0000269|PubMed:21224427"
FT MUTAGEN 333
FT /note="G->A: Mainly targeted to large vacuole and partly to
FT the ER; when associated with H-330."
FT /evidence="ECO:0000269|PubMed:21224427"
FT MUTAGEN 338
FT /note="Y->A: No effect on targeting to large vacuole."
FT /evidence="ECO:0000269|PubMed:21224427"
SQ SEQUENCE 347 AA; 39236 MW; 33F34F43014065DD CRC64;
MDDNSIQQSL LADNPNVLQR KPSEGVNRFR RCRSTPSTDP LQGPPEKGSS VKAKELFKEM
RPSFRLVGLL LFIYLLVGVL AFYAVMDEIS GKRTNRVLDA LYFCVVTMTT VGYGDLVPNN
DTTKLLACAF VFMGMAVVAL FVSKVADYLV EKQEVLFFKA LHTNLKGGET KMLRAIETNR
IKYKFYTNAL LLVLSIISGT VFLWKVEKLS LVDSFYCVCA TITTLGYGDK SFSSKLGRVF
AVFWIITSTI IMAQFFMYLA EIYTERRQKM LANWVLTRKM TKMDLEAADL DDDRQVGAAE
FVVYKLKELG KINQEEISSF LEEFEKLDVD HSGTLSPYDL TLAQSAQ
