KCO3_ARATH
ID KCO3_ARATH Reviewed; 260 AA.
AC Q9XFR0; F4KHG2;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Potassium inward rectifier (Kir)-like channel 3;
DE Short=AtKCO3;
GN Name=KCO3; OrderedLocusNames=At5g46360; ORFNames=MPL12.16;
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] (ISOFORM 1).
RC STRAIN=cv. C24; TISSUE=Seedling;
RA Wiese S., Czempinski K., Zimmermann S., Mueller-Roeber B.;
RT "Association of novel structural features of a KCO-like protein with a new
RT function for plant potassium channels?";
RL Submitted (SEP-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 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 [5]
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 [6]
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 calcium-activated potassium channel. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XFR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XFR0-2; Sequence=VSP_043863;
CC -!- TISSUE SPECIFICITY: Expressed in hydathodes and the vascular tissues of
CC roots, stems, leaves and flowers. {ECO:0000269|PubMed:16984403}.
CC -!- DOMAIN: The pore-forming region (also called P-domain or P-loop) is
CC enclosed by two transmembrane segments (1P/2TM) and contains a pseudo
CC GYGD signature motif such as GYFD which seems to be involved in
CC potassium selectivity.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.7) family. {ECO:0000305}.
CC -!- CAUTION: KCO3 shares similarity to the TPK family (2P/4TM) but lacks
CC the conserved internal part including one pore-forming region and two
CC transmembrane segments. As a result and according to its structure,
CC KCO3 could also be classified as a member of the IRK family (1P/2TM).
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ010873; CAB40380.1; -; mRNA.
DR EMBL; AB010698; BAB11091.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95373.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95374.1; -; Genomic_DNA.
DR RefSeq; NP_001190480.1; NM_001203551.1. [Q9XFR0-2]
DR RefSeq; NP_199448.1; NM_124006.3. [Q9XFR0-1]
DR AlphaFoldDB; Q9XFR0; -.
DR SMR; Q9XFR0; -.
DR STRING; 3702.AT5G46360.2; -.
DR TCDB; 1.A.1.7.6; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q9XFR0; -.
DR PRIDE; Q9XFR0; -.
DR EnsemblPlants; AT5G46360.1; AT5G46360.1; AT5G46360. [Q9XFR0-1]
DR EnsemblPlants; AT5G46360.2; AT5G46360.2; AT5G46360. [Q9XFR0-2]
DR GeneID; 834679; -.
DR Gramene; AT5G46360.1; AT5G46360.1; AT5G46360. [Q9XFR0-1]
DR Gramene; AT5G46360.2; AT5G46360.2; AT5G46360. [Q9XFR0-2]
DR KEGG; ath:AT5G46360; -.
DR Araport; AT5G46360; -.
DR TAIR; locus:2170413; AT5G46360.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_3_0_1; -.
DR InParanoid; Q9XFR0; -.
DR OMA; DVAQICK; -.
DR OrthoDB; 774951at2759; -.
DR PhylomeDB; Q9XFR0; -.
DR PRO; PR:Q9XFR0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XFR0; baseline and differential.
DR Genevisible; Q9XFR0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
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; 2.
DR Pfam; PF07885; Ion_trans_2; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Ion channel; Ion transport; Membrane;
KW Metal-binding; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..260
FT /note="Potassium inward rectifier (Kir)-like channel 3"
FT /id="PRO_0000101777"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 127..146
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 190..225
FT /note="EF-hand 1"
FT DOMAIN 229..256
FT /note="EF-hand 2"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT VAR_SEQ 237..259
FT /note="QFDKLDRTQSGRITLVDLTTATS -> HNTHYNMIEDGSGKSAVLDIVEP
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043863"
SQ SEQUENCE 260 AA; 29108 MW; 66A110AB5AD68414 CRC64;
MPMTPSEFKN RLLFGSLPRS SSDPTDLQFT EPNVPPSLFS LPEHNDDTAT DMAPDQETEQ
SVSKSIARQA LALLVVYLSL GVLIYWLTLD SDNAYQTHPV AVALYFFVVT FCGFLIVHFV
VKIGWLDSFC FSVMMVTTVG FGDRAFNTWL GTFLAAVWLL VSTLAVARAF LFLADARADK
RNRERAKKVL GESISISQFF AADIDNDGRL SLAEFAIYKL KQMEKITQED FIQICNQFDK
LDRTQSGRIT LVDLTTATSV
