POT3_ARATH
ID POT3_ARATH Reviewed; 775 AA.
AC Q9FE38; O22399; Q9SUR2;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Potassium transporter 3;
DE Short=AtKT3;
DE Short=AtKUP4;
DE Short=AtPOT3;
DE AltName: Full=Tiny root hair 1 protein;
GN Name=POT3; Synonyms=KT3, KUP4, TRH1; OrderedLocusNames=At4g23640;
GN ORFNames=F9D16.110;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11158535; DOI=10.2307/3871159;
RA Rigas S., Debrosses G., Haralampidis K., Vicente-Agullo F., Feldmann K.A.,
RA Grabov A., Dolan L., Hatzopoulos P.;
RT "TRH1 encodes a potassium transporter required for tip growth in
RT Arabidopsis root hairs.";
RL Plant Cell 13:139-151(2001).
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 [MRNA] OF 1-344.
RC STRAIN=cv. Columbia;
RX PubMed=9350997; DOI=10.1016/s0014-5793(97)01125-3;
RA Quintero F.J., Blatt M.R.;
RT "A new family of K+ transporters from Arabidopsis that are conserved across
RT phyla.";
RL FEBS Lett. 415:206-211(1997).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9477571; DOI=10.2307/3870628;
RA Kim E.J., Kwak J.M., Uozumi N., Schroeder J.I.;
RT "AtKUP1: an Arabidopsis gene encoding high-affinity potassium transport
RT activity.";
RL Plant Cell 10:51-62(1998).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: High-affinity potassium transporter required for tip growth
CC of root hairs. {ECO:0000269|PubMed:11158535}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected at very low levels in roots, stems, leaves
CC and flowers of mature plants. {ECO:0000269|PubMed:9477571}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in roots in the early stage of
CC seedlings growth.
CC -!- DISRUPTION PHENOTYPE: Loss-of-function mutation results in the arrest
CC of root hair growth. {ECO:0000269|PubMed:11158535}.
CC -!- SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72.3) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23030.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79319.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ296155; CAC16137.1; -; mRNA.
DR EMBL; AJ296156; CAC16138.1; -; Genomic_DNA.
DR EMBL; AL035394; CAA23030.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161559; CAB79319.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84788.1; -; Genomic_DNA.
DR EMBL; AF012658; AAC49846.1; -; mRNA.
DR PIR; T05596; T05596.
DR RefSeq; NP_194095.2; NM_118495.4.
DR AlphaFoldDB; Q9FE38; -.
DR BioGRID; 13753; 13.
DR IntAct; Q9FE38; 12.
DR STRING; 3702.AT4G23640.1; -.
DR TCDB; 2.A.72.3.10; the k(+) uptake permease (kup) family.
DR iPTMnet; Q9FE38; -.
DR SwissPalm; Q9FE38; -.
DR PaxDb; Q9FE38; -.
DR PRIDE; Q9FE38; -.
DR ProteomicsDB; 249054; -.
DR EnsemblPlants; AT4G23640.1; AT4G23640.1; AT4G23640.
DR GeneID; 828464; -.
DR Gramene; AT4G23640.1; AT4G23640.1; AT4G23640.
DR KEGG; ath:AT4G23640; -.
DR Araport; AT4G23640; -.
DR TAIR; locus:2128399; AT4G23640.
DR eggNOG; ENOG502QSBW; Eukaryota.
DR HOGENOM; CLU_008142_2_0_1; -.
DR InParanoid; Q9FE38; -.
DR OMA; HQTEDTI; -.
DR OrthoDB; 332035at2759; -.
DR PhylomeDB; Q9FE38; -.
DR PRO; PR:Q9FE38; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FE38; baseline and differential.
DR Genevisible; Q9FE38; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009932; P:cell tip growth; IMP:TAIR.
DR GO; GO:0048825; P:cotyledon development; IMP:TAIR.
DR GO; GO:0006813; P:potassium ion transport; IBA:GO_Central.
DR InterPro; IPR003855; K+_transporter.
DR PANTHER; PTHR30540; PTHR30540; 1.
DR Pfam; PF02705; K_trans; 1.
DR TIGRFAMs; TIGR00794; kup; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..775
FT /note="Potassium transporter 3"
FT /id="PRO_0000209079"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..463
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 775 AA; 86843 MW; B0C55068B48E8180 CRC64;
MADRRNRCNQ ILLLAYQSFG LVFGDLSISP LYVYKCTFYG GLRHHQTEDT IFGAFSLIFW
TITLLSLIKY MVFVLSADDN GEGGIFALYA LLCRHARFSL LPNQQAADEE ISTYYGPGDA
SRNLPSSAFK SLIERNKRSK TALLVLVLVG TSMVITIGVL TPAISVSSSI DGLVAKTSLK
HSTVVMIACA LLVGLFVLQH RGTNKVAFLF APIMILWLLI IATAGVYNIV TWNPSVYKAL
SPYYIYVFFR DTGIDGWLSL GGILLCITGT EAIFAELGQF TATSIRFAFC CVVYPCLVLQ
YMGQAAFLSK NFSALPSSFY SSIPDPFFWP VLMMAMLAAM VASQAVIFAT FSIVKQCYAL
GCFPRVKIVH KPRWVLGQIY IPEINWVVMI LTLAVTICFR DTRHIAFAFG LACMTLAFVT
TWLMPLIINF VWNRNIVFSV LFILFFGTIE LIFVASALVK IPKGGWITLL LSLFFTFITY
VWHYGSRKKY LCDQHNKVPM KSILSLGPSL GIIKVPGMGL IYTELASGVP ATFKHFLTNL
PAFYQVVVFV CCKTVPIPYV PQKERYLIGR IGPKTYRMYR CIIRAGYKDV NKDGDDFEDE
LVMSIAEFIQ LESEGYGGSN TDRSIDGRLA VVKASNKFGT RLSRSISEAN IAGSSRSQTT
VTNSKSPALL KLRAEYEQEL PRLSMRRMFQ FRPMDTKFRQ PQVKEELFDL VNAKDAEVAY
IVGHGHVKAK RNSVFVKQLV VNVAYSFLRK NCRSPGVMLN IPHICLIKVG MNYYL
