KCO4_ARATH
ID KCO4_ARATH Reviewed; 284 AA.
AC Q9FWX6; Q6X308;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Two-pore potassium channel 4;
DE Short=AtTPK4;
DE AltName: Full=Outward-rectifying potassium channel 4;
DE Short=AtKCO4;
GN Name=TPK4; Synonyms=KCO4; OrderedLocusNames=At1g02510; ORFNames=T14P4.16;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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, AND DEVELOPMENTAL STAGE.
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=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).
CC -!- FUNCTION: Voltage-independent, instantaneously activating, potassium-
CC selective plasma membrane ion channel. Open rectifier. Regulated by
CC cytoplasmic pH and extra-cellular calcium. Has some permeability for
CC Rb(+) and NH(4)(+), but none for Na(+) or Li(+).
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15505206,
CC ECO:0000269|PubMed:19825594}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15505206, ECO:0000269|PubMed:19825594}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in pollen.
CC {ECO:0000269|PubMed:15505206, ECO:0000269|PubMed:16984403}.
CC -!- DEVELOPMENTAL STAGE: Not expressed during very early stages of flower
CC development, but detected when buds are still closed.
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 -!- DISRUPTION PHENOTYPE: No effect on pollen germination rate and growth.
CC {ECO:0000269|PubMed:15505206}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.7) family. {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; AY258073; AAP82009.1; -; mRNA.
DR EMBL; AC022521; AAG10638.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27439.1; -; Genomic_DNA.
DR PIR; D86155; D86155.
DR RefSeq; NP_171752.1; NM_100132.2.
DR AlphaFoldDB; Q9FWX6; -.
DR SMR; Q9FWX6; -.
DR BioGRID; 23086; 2.
DR STRING; 3702.AT1G02510.1; -.
DR TCDB; 1.A.1.7.2; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q9FWX6; -.
DR PRIDE; Q9FWX6; -.
DR EnsemblPlants; AT1G02510.1; AT1G02510.1; AT1G02510.
DR GeneID; 837846; -.
DR Gramene; AT1G02510.1; AT1G02510.1; AT1G02510.
DR KEGG; ath:AT1G02510; -.
DR Araport; AT1G02510; -.
DR TAIR; locus:2196155; AT1G02510.
DR eggNOG; KOG1418; Eukaryota.
DR HOGENOM; CLU_033675_1_0_1; -.
DR InParanoid; Q9FWX6; -.
DR OMA; DALYYIV; -.
DR OrthoDB; 774951at2759; -.
DR PhylomeDB; Q9FWX6; -.
DR PRO; PR:Q9FWX6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FWX6; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
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; 2.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..284
FT /note="Two-pore potassium channel 4"
FT /id="PRO_0000101778"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 70..89
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 184..203
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 32061 MW; AF54B529AE1BBB91 CRC64;
MEEENLLNEN LLHPNESSPE ETQVTTVSKS KWTILVLAMI LLLVYLTFGV CTYSFFRDQF
SGTETNLFVD AFYFSIVTFS TVGYGDIVPS TSTTKILTIV LVSTGVVFLD YLLNRVVSHV
LSLQENAILD RINKTRNRAI RDHIAEDGKI RLKWKLCLAF CAVGLCVGSG ALFLHVFERL
DWLDSVYLSV ISVTTVGYGD KTFKTVEGRG FAVFWLLLST IAMATLFLYL AEMRIDRTTV
MKLPPSESEF IVFKLRESGR ISEDDIKQIV REFENLEEVP SSGS
