KCO6_ARATH
ID KCO6_ARATH Reviewed; 436 AA.
AC Q9SVV6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Two-pore potassium channel 3;
DE Short=AtTPK3;
DE AltName: Full=Calcium-activated outward-rectifying potassium channel 6;
DE Short=AtKCO6;
GN Name=TPK3; Synonyms=KCO6; OrderedLocusNames=At4g18160; ORFNames=F15J5.130;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11821043; DOI=10.1016/s0014-5793(01)03273-2;
RA Schoenknecht G., Spoormaker P., Steinmeyer R., Brueggeman L., Ache P.,
RA Dutta R., Reintanz B., Godde M., Hedrich R., Palme K.;
RT "KCO1 is a component of the slow-vacuolar (SV) ion channel.";
RL FEBS Lett. 511:28-32(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15505206; DOI=10.1073/pnas.0401502101;
RA Becker D., Geiger D., Dunkel M., Roller A., Bertl A., Latz A.,
RA Carpaneto A., Dietrich P., Roelfsema M.R., Voelker C., Schmidt D.,
RA Mueller-Roeber B., Czempinski K., Hedrich R.;
RT "AtTPK4, an Arabidopsis tandem-pore K+ channel, poised to control the
RT pollen membrane voltage in a pH- and Ca2+-dependent manner.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15621-15626(2004).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16984403; DOI=10.1111/j.1365-313x.2006.02868.x;
RA Voelker C., Schmidt D., Mueller-Roeber B., Czempinski K.;
RT "Members of the Arabidopsis AtTPK/KCO family form homomeric vacuolar
RT channels in planta.";
RL Plant J. 48:296-306(2006).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17764516; DOI=10.1111/j.1365-313x.2007.03255.x;
RA Latz A., Becker D., Hekman M., Mueller T., Beyhl D., Marten I., Eing C.,
RA Fischer A., Dunkel M., Bertl A., Rapp U.R., Hedrich R.;
RT "TPK1, a Ca(2+)-regulated Arabidopsis vacuole two-pore K(+) channel is
RT activated by 14-3-3 proteins.";
RL Plant J. 52:449-459(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19825594; DOI=10.1093/mp/ssn064;
RA Dunkel M., Latz A., Schumacher K., Mueller T., Becker D., Hedrich R.;
RT "Targeting of vacuolar membrane localized members of the TPK channel
RT family.";
RL Mol. Plant 1:938-949(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24009357; DOI=10.1126/science.1242113;
RA Carraretto L., Formentin E., Teardo E., Checchetto V., Tomizioli M.,
RA Morosinotto T., Giacometti G.M., Finazzi G., Szabo I.;
RT "A thylakoid-located two-pore potassium channel controls photosynthetic
RT light utilization in plants.";
RL Science 342:114-118(2013).
CC -!- FUNCTION: Two-pore potassium channel modulating the proton motive force
CC (pmf) necessary to convert photochemical energy into physiological
CC functions. Mediates the potassium efflux from the thylakoid lumen
CC required for the regulation of the transmembrane electrical potential,
CC the enhancement of the pH gradient for ATP synthesis, the regulation of
CC electron flow, and pH-mediated photoprotective responses. Requires
CC calcium for channel activity. {ECO:0000269|PubMed:24009357}.
CC -!- ACTIVITY REGULATION: Inhibited by barium, but not by
CC tetraethylammonium. {ECO:0000269|PubMed:24009357}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16984403,
CC ECO:0000269|PubMed:17764516, ECO:0000269|PubMed:19825594}; Multi-pass
CC membrane protein {ECO:0000255}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:24009357}; Multi-pass membrane protein
CC {ECO:0000255}. Note=PubMed:24009357 shows a thylakoid location instead
CC of the tonoplast location previously described.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, hypocotyls, leaves and
CC flowers. Detected in root tips and in mesophyll cells and guard cells
CC of the leaves. {ECO:0000269|PubMed:11821043,
CC ECO:0000269|PubMed:16984403}.
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. The C-terminus is not required for transport to the
CC vacuolar membrane.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of the protein causes no
CC effects on germination or on plants grown under normal conditions, but
CC decreases the rosette size, enhances the accumulation of anthocyans and
CC desorganizes the photosynthetic membranes when the plants are grown
CC under high light. {ECO:0000269|PubMed:24009357}.
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; AL110123; CAB53657.1; -; Genomic_DNA.
DR EMBL; AL161548; CAB78818.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84005.1; -; Genomic_DNA.
DR PIR; T14816; T14816.
DR RefSeq; NP_193550.1; NM_117926.3.
DR AlphaFoldDB; Q9SVV6; -.
DR SMR; Q9SVV6; -.
DR BioGRID; 12834; 2.
DR IntAct; Q9SVV6; 1.
DR STRING; 3702.AT4G18160.1; -.
DR TCDB; 1.A.1.7.7; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q9SVV6; -.
DR PRIDE; Q9SVV6; -.
DR ProteomicsDB; 230170; -.
DR EnsemblPlants; AT4G18160.1; AT4G18160.1; AT4G18160.
DR GeneID; 827541; -.
DR Gramene; AT4G18160.1; AT4G18160.1; AT4G18160.
DR KEGG; ath:AT4G18160; -.
DR Araport; AT4G18160; -.
DR TAIR; locus:2117681; AT4G18160.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_2_0_1; -.
DR InParanoid; Q9SVV6; -.
DR OMA; NEVAIPM; -.
DR OrthoDB; 774951at2759; -.
DR PhylomeDB; Q9SVV6; -.
DR PRO; PR:Q9SVV6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVV6; baseline and differential.
DR Genevisible; Q9SVV6; AT.
DR GO; GO:0009533; C:chloroplast stromal thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0034705; C:potassium channel complex; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
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:0005267; F:potassium channel activity; IDA:TAIR.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IDA:TAIR.
DR GO; GO:0010196; P:nonphotochemical quenching; IMP:TAIR.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:TAIR.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:TAIR.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:TAIR.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
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 2: Evidence at transcript level;
KW Calcium; Chloroplast; Ion channel; Ion transport; Membrane; Metal-binding;
KW Plastid; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Repeat; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..436
FT /note="Two-pore potassium channel 3"
FT /id="PRO_0000101779"
FT TOPO_DOM 1..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 185..204
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 302..321
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 365..400
FT /note="EF-hand 1"
FT DOMAIN 404..436
FT /note="EF-hand 2"
FT REGION 62..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48732 MW; 0F5C43B82B318761 CRC64;
MANEGSDPLL QYMISPRLKK PPQLLFPLPE DNEVAIPMPM TPSEFKERLI FGPFSCSPRD
SSHFIDSMKQ PSPSSSSTAV NNPFSDSSTL DPLLPPPPPQ PEPWLSDQTS SHCQGHALHR
SKTAPAMAVI NDLHHPIRQK DPTETSRSVV RQAFALLVVY LSLGVLIYWL NRDHYVVNQT
HPVVDGLYFC IVTMCTIGYG DITPNSVVTK LFSIMFVLVG FGFIDILLSG MVSYVLDLQE
SYMLDSAKRR DEPEKRRSYI IDVKKGRMRI RLKVALALGV VVLCIAVGVG IMHFIEEIGW
LDSFYLSVMS VTTVGYGDRA FKTLPGRLFA AIWLLVSTLA VARAFLYLAE ARVDKRNRER
AKKVLCETMS VSQFFAADID NNGCVSKAEY VIYKLKEMEK ITDKDILPIS KQFDKLDRCS
NGKITLLDLL EGGSGD
