KCO2_ORYSJ
ID KCO2_ORYSJ Reviewed; 349 AA.
AC Q8LIN5; A0A0P0X1G6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Two pore potassium channel b;
DE Short=Two K(+) channel b;
DE AltName: Full=Calcium-activated outward-rectifying potassium channel 2;
DE Short=OsKCO2;
GN Name=TPKB; Synonyms=KCO2; OrderedLocusNames=Os07g0108800, LOC_Os07g01810;
GN ORFNames=OJ1567_G09.108, OsJ_22819, P0585H11.123;
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).
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-295.
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 protein storage vacuoles.
CC Functions 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 protein storage 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}.
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DR EMBL; AP003759; BAC06932.1; -; Genomic_DNA.
DR EMBL; AP004342; BAD30634.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20633.1; -; Genomic_DNA.
DR EMBL; AP014963; BAS99736.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ38441.1; -; Genomic_DNA.
DR EMBL; AK109604; BAG98817.1; -; mRNA.
DR AlphaFoldDB; Q8LIN5; -.
DR SMR; Q8LIN5; -.
DR STRING; 4530.OS07T0108800-01; -.
DR PaxDb; Q8LIN5; -.
DR PRIDE; Q8LIN5; -.
DR EnsemblPlants; Os07t0108800-01; Os07t0108800-01; Os07g0108800.
DR Gramene; Os07t0108800-01; Os07t0108800-01; Os07g0108800.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_0_1_1; -.
DR InParanoid; Q8LIN5; -.
DR OMA; KILACIY; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q8LIN5; 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:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
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:0030007; P:cellular potassium ion homeostasis; IC:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
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 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.
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..349
FT /note="Two pore potassium channel b"
FT /id="PRO_0000410873"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 100..119
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 208..227
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 271..306
FT /note="EF-hand 1"
FT DOMAIN 310..345
FT /note="EF-hand 2"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT MUTAGEN 295
FT /note="D->E: No effect on targeting to protein storage
FT vacuole."
FT /evidence="ECO:0000269|PubMed:21224427"
SQ SEQUENCE 349 AA; 37914 MW; 1B0BC09D2F17A357 CRC64;
MAALDQQPLL HDGGDQKPPP EGAARRFRRC RTAPSSEPPP TDKDNSSAAD APPKTLFTGG
GRPSFRLVGL LLVAYLLLGT IAFYLAMDHM SGTRTTRALD ALYFCVVTMT TVGYGDLVPA
SDAAKLLACA FVFAGVAVVG TFLSKAADYL VEKQEALLFR ALHSHTMVRA MEMNKVRYKL
YTAGLLLVAA VASGTVVLWK VEGMRAVDAF YCVCATVTTL GYGDRSFSSE GGRAFAVAWI
TVSTVVVALF FLYAAELYTE RRQRELARWV LRRRTTNMDL EAADLDGDHR VGAADFVLYK
LKELGKISQE DISEFLDEFD NLDADHSGTL SPADLAAAQP TPDPPPSLR
