KCO2_ARATH
ID KCO2_ARATH Reviewed; 443 AA.
AC Q9FL25; Q1PDM4; Q9SCY7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Two-pore potassium channel 2;
DE Short=AtTPK2;
DE AltName: Full=Calcium-activated outward-rectifying potassium channel 2;
DE Short=AtKCO2;
GN Name=TPK2; Synonyms=KCO2; OrderedLocusNames=At5g46370; ORFNames=MPL12.17;
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 Czempinski K., Wiese S., Zimmermann S., Mueller-Roeber B.;
RT "KCO2, a new member of the two-pore K+ channel family in plants.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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, 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:0000305}.
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 roots, stems, leaves and flowers.
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.
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; AJ131641; CAB64717.1; -; mRNA.
DR EMBL; AB010698; BAB11092.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95375.1; -; Genomic_DNA.
DR EMBL; DQ447044; ABE66226.1; -; mRNA.
DR RefSeq; NP_199449.1; NM_124007.3.
DR AlphaFoldDB; Q9FL25; -.
DR SMR; Q9FL25; -.
DR BioGRID; 19929; 1.
DR STRING; 3702.AT5G46370.1; -.
DR PaxDb; Q9FL25; -.
DR PRIDE; Q9FL25; -.
DR EnsemblPlants; AT5G46370.1; AT5G46370.1; AT5G46370.
DR GeneID; 834680; -.
DR Gramene; AT5G46370.1; AT5G46370.1; AT5G46370.
DR KEGG; ath:AT5G46370; -.
DR Araport; AT5G46370; -.
DR TAIR; locus:2170423; AT5G46370.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_2_0_1; -.
DR InParanoid; Q9FL25; -.
DR OMA; WLNRDSY; -.
DR OrthoDB; 774951at2759; -.
DR PhylomeDB; Q9FL25; -.
DR PRO; PR:Q9FL25; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FL25; baseline and differential.
DR Genevisible; Q9FL25; 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; 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; 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..443
FT /note="Two-pore potassium channel 2"
FT /id="PRO_0000101776"
FT TOPO_DOM 1..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 181..200
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..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..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 365..400
FT /note="EF-hand 1"
FT DOMAIN 404..439
FT /note="EF-hand 2"
FT REGION 67..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..95
FT /note="Polar 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"
FT CONFLICT 393
FT /note="Y -> H (in Ref. 1; CAB64717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 49326 MW; 071543B69B26E508 CRC64;
MANDGNGDNN DDPLRQYLMN PRINPPPPSL LTLPENNDVT IPMPITPLEL KNRLIFGSFV
RSRKESSLPI DALSQNPSTS SSATTSFSDS TDLLLPLTEP NKPVRKSKPT INFHRSKTAP
AMAAINNISH PNDPKTDQQS DSKTIVNQAV ALLVVYLSLG VLIYWLNRDS YNVKQTHPVV
DALYFCIVTM CTIGYGDITP DSVVTKLFSI FFVLVGFGFM DILLSGMVTY VLDLQENYML
ETARNESLNL NDRDKVRSYI IDVKKGRMRI RLKVGLALGV VVLCLGFGVL IMHFVEKIGW
LDSFYFSVMS VTTVGYGDRA FNTLAGRLLA AMWLLVSTLA VARAILFLAE SRVDKRNRER
AKKVLGESMS ISQFLDADID CNGCVSKAEF VIYKLKKMDK ITEKDINPIG FQFDKLDRTN
SGRITLLDLL ESSTKDLPTA TSI
