KCO5_ARATH
ID KCO5_ARATH Reviewed; 408 AA.
AC Q9S6Z8;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Two-pore potassium channel 5;
DE Short=AtTPK5;
DE AltName: Full=Calcium-activated outward-rectifying potassium channel 5, chloroplastic;
DE Short=AtKCO5;
GN Name=TPK5; Synonyms=KCO5; OrderedLocusNames=At4g01840; ORFNames=T7B11.10;
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 [MRNA].
RC STRAIN=cv. C24;
RA Greven K.K., Czempinski K., Mueller-Roeber B.;
RT "New members of the KCO family in Arabidopsis.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY, SUBUNIT, 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 [8]
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).
CC -!- FUNCTION: Probable voltage-independent potassium-selective tonoplast
CC ion channel.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16984403}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16984403,
CC ECO:0000269|PubMed:17764516}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16984403, ECO:0000269|PubMed:17764516}.
CC -!- TISSUE SPECIFICITY: Expressed in hydathodes and the vascular tissues of
CC roots, stems, leaves and flowers. {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.
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; AJ243456; CAB62162.1; -; mRNA.
DR EMBL; AC007138; AAD22646.1; -; Genomic_DNA.
DR EMBL; AL161493; CAB80677.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82083.1; -; Genomic_DNA.
DR EMBL; AY084857; AAM61421.1; -; mRNA.
DR PIR; F85023; F85023.
DR RefSeq; NP_192093.1; NM_116414.4.
DR AlphaFoldDB; Q9S6Z8; -.
DR SMR; Q9S6Z8; -.
DR BioGRID; 13382; 3.
DR IntAct; Q9S6Z8; 2.
DR STRING; 3702.AT4G01840.1; -.
DR TCDB; 1.A.1.7.5; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q9S6Z8; -.
DR PaxDb; Q9S6Z8; -.
DR PRIDE; Q9S6Z8; -.
DR ProteomicsDB; 247144; -.
DR EnsemblPlants; AT4G01840.1; AT4G01840.1; AT4G01840.
DR GeneID; 828091; -.
DR Gramene; AT4G01840.1; AT4G01840.1; AT4G01840.
DR KEGG; ath:AT4G01840; -.
DR Araport; AT4G01840; -.
DR TAIR; locus:2141375; AT4G01840.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_0_1_1; -.
DR InParanoid; Q9S6Z8; -.
DR OMA; HRRITNW; -.
DR OrthoDB; 774951at2759; -.
DR PhylomeDB; Q9S6Z8; -.
DR PRO; PR:Q9S6Z8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S6Z8; baseline and differential.
DR Genevisible; Q9S6Z8; AT.
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: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; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
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..408
FT /note="Two-pore potassium channel 5"
FT /id="PRO_0000035873"
FT TOPO_DOM 22..115
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 152..171
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..248
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 276..295
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..408
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT DOMAIN 339..374
FT /note="EF-hand 1"
FT DOMAIN 378..408
FT /note="EF-hand 2"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 408 AA; 46259 MW; FCF22402122F8F2A CRC64;
MEPLISPQPR FRLQPIPENP SSSSSSASIT IPRSISNTSF FHEISQERLL LHHQDLEQSV
QDDKEDQDSD SDETNRFLSQ TRPLHRSRTA PAMVIIKDLR TKPPETKKPS PVSKSIIRQA
IFLLIVYLTL GVSIYSFNRD HYSGIETHPV VDALYFCIVT MCTIGYGDIA PLTPWTKIFA
VVFVLFGFGF LDILLSGVVN YVLDLQESMI LTGIQTRQHH QHHHHHRFSA KDYIIDFEKG
RMRIRMKVCL ALCVVVLCIG VGALVLHFVE ELGFVDSVYL SVMSVTTVGY GDRAFKTLQG
RLFAAVWLLV STLAVARAFL YLAEARIDRR HRKAVKLALN REITVDDLLK ADTYQHGFIS
KSEYIVLKLK EMGKITQKDI DQVVIQFEKL DPNQIGKITL PDLLGDPL
