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Two-pore potassium channel 1 (AtTPK1) (Calcium-activated outward-rectifying potassium channel 1) (AtKCO1)

 KCO1_ARATH              Reviewed;         363 AA.
Q8LBL1; O04718; Q0WNY4; Q9FM75;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
28-NOV-2003, sequence version 2.
27-SEP-2017, entry version 133.
RecName: Full=Two-pore potassium channel 1;
Short=AtTPK1;
AltName: Full=Calcium-activated outward-rectifying potassium channel 1;
Short=AtKCO1;
Name=TPK1; Synonyms=KCO1; OrderedLocusNames=At5g55630;
ORFNames=MDF20.7;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
STRAIN=cv. C24;
PubMed=9184204; DOI=10.1093/emboj/16.10.2565;
Czempinski K., Zimmermann S., Ehrhardt T., Mueller-Roeber B.;
"New structure and function in plant K+ channels: KCO1, an outward
rectifier with a steep Ca2+ dependency.";
EMBO J. 16:2565-2575(1997).
[2]
ERRATUM.
Czempinski K., Zimmermann S., Ehrhardt T., Mueller-Roeber B.;
EMBO J. 16:6896-6896(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=cv. C24;
PubMed=12148538; DOI=10.1046/j.1365-313X.2002.01260.x;
Czempinski K., Frachisse J.-M., Maurel C., Barbier-Brygoo H.,
Mueller-Roeber B.;
"Vacuolar membrane localization of the Arabidopsis 'two-pore' K+
channel KCO1.";
Plant J. 29:809-820(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11500563; DOI=10.1104/pp.126.4.1646;
Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A.,
Guerinot M.L.;
"Phylogenetic relationships within cation transporter families of
Arabidopsis.";
Plant Physiol. 126:1646-1667(2001).
[9]
CHARACTERIZATION, AND NULL MUTANT KCO1-7.
PubMed=11821043; DOI=10.1016/S0014-5793(01)03273-2;
Schoenknecht G., Spoormaker P., Steinmeyer R., Brueggeman L., Ache P.,
Dutta R., Reintanz B., Godde M., Hedrich R., Palme K.;
"KCO1 is a component of the slow-vacuolar (SV) ion channel.";
FEBS Lett. 511:28-32(2002).
[10]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15505206; DOI=10.1073/pnas.0401502101;
Becker D., Geiger D., Dunkel M., Roller A., Bertl A., Latz A.,
Carpaneto A., Dietrich P., Roelfsema M.R., Voelker C., Schmidt D.,
Mueller-Roeber B., Czempinski K., Hedrich R.;
"AtTPK4, an Arabidopsis tandem-pore K+ channel, poised to control the
pollen membrane voltage in a pH- and Ca2+-dependent manner.";
Proc. Natl. Acad. Sci. U.S.A. 101:15621-15626(2004).
[11]
FUNCTION, AND ENZYME REGULATION.
PubMed=16113216; DOI=10.1104/pp.105.065599;
Bihler H., Eing C., Hebeisen S., Roller A., Czempinski K., Bertl A.;
"TPK1 is a vacuolar ion channel different from the slow-vacuolar
cation channel.";
Plant Physiol. 139:417-424(2005).
[12]
TISSUE SPECIFICITY, AND SUBUNIT.
PubMed=16984403; DOI=10.1111/j.1365-313X.2006.02868.x;
Voelker C., Schmidt D., Mueller-Roeber B., Czempinski K.;
"Members of the Arabidopsis AtTPK/KCO family form homomeric vacuolar
channels in planta.";
Plant J. 48:296-306(2006).
[13]
FUNCTION, INTERACTION WITH GRF1 AND GRF6, MUTAGENESIS OF SER-42,
PHOSPHORYLATION, AND 3D-STRUCTURE MODELING.
PubMed=17764516; DOI=10.1111/j.1365-313X.2007.03255.x;
Latz A., Becker D., Hekman M., Mueller T., Beyhl D., Marten I.,
Eing C., Fischer A., Dunkel M., Bertl A., Rapp U.R., Hedrich R.;
"TPK1, a Ca(2+)-regulated Arabidopsis vacuole two-pore K(+) channel is
activated by 14-3-3 proteins.";
Plant J. 52:449-459(2007).
[14]
FUNCTION, DISRUPTION PHENOTYPE, AND ENZYME REGULATION.
STRAIN=cv. Columbia;
PubMed=17563365; DOI=10.1073/pnas.0702595104;
Gobert A., Isayenkov S., Voelker C., Czempinski K., Maathuis F.J.;
"The two-pore channel TPK1 gene encodes the vacuolar K+ conductance
and plays a role in K+ homeostasis.";
Proc. Natl. Acad. Sci. U.S.A. 104:10726-10731(2007).
[15]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 296-ASP--GLU-298 AND
301-ASP--ASP-303.
PubMed=19825594; DOI=10.1093/mp/ssn064;
Dunkel M., Latz A., Schumacher K., Mueller T., Becker D., Hedrich R.;
"Targeting of vacuolar membrane localized members of the TPK channel
family.";
Mol. Plant 1:938-949(2008).
[16]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=cv. Columbia;
PubMed=21697507; DOI=10.1104/pp.111.177816;
Maitrejean M., Wudick M.M., Voelker C., Prinsi B., Mueller-Roeber B.,
Czempinski K., Pedrazzini E., Vitale A.;
"Assembly and sorting of the tonoplast potassium channel AtTPK1 and
its turnover by internalization into the vacuole.";
Plant Physiol. 156:1783-1796(2011).
-!- FUNCTION: Voltage-independent, large conductance and potassium-
selective tonoplast ion channel. Regulated by cytoplasmic calcium
and pH. Does not mediate slow-vacuolar (SV) ionic currents, but
essential to establish VK currents. Has some permeability for
Rb(+) and NH(4)(+), but none for Na(+), Cs(+) or Li(+). Involved
in intracellular K(+) redistribution and/or K(+) retranslocation
between different tissues. {ECO:0000269|PubMed:16113216,
ECO:0000269|PubMed:17563365, ECO:0000269|PubMed:17764516,
ECO:0000269|PubMed:21697507}.
-!- ENZYME REGULATION: Could be activated by protein kinase C (By
similarity). Strongly induced by calcium. Blocked by barium,
tetraethylammonium (TEA), quinine and quinidine. {ECO:0000250,
ECO:0000269|PubMed:16113216, ECO:0000269|PubMed:17563365}.
-!- SUBUNIT: Homodimer. Interacts with GRF1 and GRF6, but only GRF6
modulates the channel activity. {ECO:0000269|PubMed:16984403,
ECO:0000269|PubMed:17764516, ECO:0000269|PubMed:21697507}.
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:12148538, ECO:0000269|PubMed:19825594,
ECO:0000269|PubMed:21697507}; Multi-pass membrane protein
{ECO:0000269|PubMed:12148538, ECO:0000269|PubMed:19825594,
ECO:0000269|PubMed:21697507}. Note=Tonoplast.
-!- TISSUE SPECIFICITY: Detected in mesophyll cells, guard cells and
vascular tissues of the leaves. Expressed in the hilum, where the
funiculus is attached during fruit maturation and in the embryo.
Also expressed at a lower level in seedlings, root tips and
elongation zones, and flowers. Could be detected in mitotically
active tissues. {ECO:0000269|PubMed:12148538,
ECO:0000269|PubMed:16984403}.
-!- DOMAIN: Each of the two pore-forming region (also called P-domain
or P-loop) is enclosed by two transmembrane segments (2P/4TM) and
contains the GYGD signature motif which seems to be involved in
potassium selectivity. The C-terminus (328-363) is required for
vacuolar targeting.
-!- PTM: Phosphorylation at Ser-42 increases and stabilizes the
interaction with 14-3-3 proteins. {ECO:0000269|PubMed:17764516}.
-!- DISRUPTION PHENOTYPE: Reduced growth in both high and low K(+)
conditions. Slower germination and increased sensitivity to
abscisic acid. Reduction of the total tonoplast current density.
{ECO:0000269|PubMed:17563365}.
-!- MISCELLANEOUS: 14-3-3 protein binding is not involved in
endoplasmic reticulum export and tonoplast targeting.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.7) family. {ECO:0000305}.
-!- CAUTION: Was initially described as an outward slow-vacuolar (SV)
ion channel (PubMed:9184204 and PubMed:11821043). {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X97323; CAA65988.1; -; mRNA.
EMBL; Y07825; CAA69158.1; -; Genomic_DNA.
EMBL; AB009050; BAB09230.1; -; Genomic_DNA.
EMBL; CP002688; AED96660.1; -; Genomic_DNA.
EMBL; CP002688; AED96661.1; -; Genomic_DNA.
EMBL; AK229302; BAF01165.1; -; mRNA.
EMBL; AY087147; AAM64705.1; -; mRNA.
RefSeq; NP_200374.1; NM_124945.4.
RefSeq; NP_851196.1; NM_180865.1.
UniGene; At.20254; -.
ProteinModelPortal; Q8LBL1; -.
SMR; Q8LBL1; -.
BioGrid; 20901; 27.
STRING; 3702.AT5G55630.1; -.
TCDB; 1.A.1.7.3; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q8LBL1; -.
PaxDb; Q8LBL1; -.
EnsemblPlants; AT5G55630.1; AT5G55630.1; AT5G55630.
EnsemblPlants; AT5G55630.2; AT5G55630.2; AT5G55630.
GeneID; 835657; -.
Gramene; AT5G55630.1; AT5G55630.1; AT5G55630.
Gramene; AT5G55630.2; AT5G55630.2; AT5G55630.
KEGG; ath:AT5G55630; -.
Araport; AT5G55630; -.
TAIR; locus:2162162; AT5G55630.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
HOGENOM; HOG000238193; -.
InParanoid; Q8LBL1; -.
KO; K05389; -.
OMA; HPSKIPM; -.
OrthoDB; EOG09360EZI; -.
PhylomeDB; Q8LBL1; -.
BioCyc; ARA:AT5G55630-MONOMER; -.
BioCyc; MetaCyc:MONOMER-14554; -.
PRO; PR:Q8LBL1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8LBL1; baseline and differential.
Genevisible; Q8LBL1; AT.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005216; F:ion channel activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:TAIR.
GO; GO:0051260; P:protein homooligomerization; IPI:TAIR.
GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
InterPro; IPR003280; 2pore_dom_K_chnl.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR013099; K_chnl_dom.
Pfam; PF07885; Ion_trans_2; 2.
PRINTS; PR01333; 2POREKCHANEL.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
1: Evidence at protein level;
Calcium; Complete proteome; Ion channel; Ion transport; Membrane;
Metal-binding; Phosphoprotein; Potassium; Potassium channel;
Potassium transport; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport; Vacuole.
CHAIN 1 363 Two-pore potassium channel 1.
/FTId=PRO_0000101775.
TOPO_DOM 1 78 Cytoplasmic. {ECO:0000255}.
TRANSMEM 79 99 Helical. {ECO:0000255}.
INTRAMEM 111 130 Pore-forming; Name=Pore-forming 1.
{ECO:0000255}.
TRANSMEM 137 157 Helical. {ECO:0000255}.
TOPO_DOM 158 197 Cytoplasmic. {ECO:0000255}.
TRANSMEM 198 218 Helical. {ECO:0000255}.
INTRAMEM 225 244 Pore-forming; Name=Pore-forming 2.
{ECO:0000255}.
TRANSMEM 251 271 Helical. {ECO:0000255}.
TOPO_DOM 272 363 Cytoplasmic. {ECO:0000255}.
DOMAIN 288 323 EF-hand 1.
DOMAIN 327 362 EF-hand 2.
CA_BIND 301 312 1. {ECO:0000255}.
CA_BIND 340 351 2. {ECO:0000255}.
MOTIF 296 298 Endoplasmic reticulum release signal.
COMPBIAS 33 39 Arg/Lys-rich (basic).
SITE 131 131 Not glycosylated.
MUTAGEN 42 42 S->A: Loss of interaction with GRF6, but
no effect on vacuolar targeting.
{ECO:0000269|PubMed:17764516}.
MUTAGEN 296 298 DLE->GLG: Retention in the endoplasmic
reticulum. {ECO:0000269|PubMed:19825594}.
MUTAGEN 301 303 DLD->GLG: No effect on vacuolar
targeting. {ECO:0000269|PubMed:19825594}.
CONFLICT 227 227 F -> V (in Ref. 7; AAM64705).
{ECO:0000305}.
CONFLICT 261 261 S -> T (in Ref. 1; CAA65988 and 3;
CAA69158). {ECO:0000305}.
SEQUENCE 363 AA; 40727 MW; 149B00AABBE40EFC CRC64;
MSSDAARTPL LPTEKIDTMA QDFNLNSRTS SSRKRRLRRS RSAPRGDCMY NDDVKIDEPP
PHPSKIPMFS DLNPNLRRVI MFLALYLTIG TLCFYLVRDQ ISGHKTSGVV DALYFCIVTM
TTVGYGDLVP NSSASRLLAC AFVFSGMVLV GHLLSRAADY LVEKQEALLV RAFHLRQSFG
PTDILKELHT NKLRYKCYAT CLVLVVLFIV GTIFLVMVEK MPVISAFYCV CSTVTTLGYG
DKSFNSEAGR LFAVFWILTS SICLAQFFLY VAELNTENKQ RALVKWVLTR RITNNDLEAA
DLDEDGVVGA AEFIVYKLKE MGKIDEKDIS GIMDEFEQLD YDESGTLTTS DIVLAQTTSQ
IQR


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