POT5_ARATH
ID POT5_ARATH Reviewed; 785 AA.
AC Q9M7K4; Q9T0L3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Potassium transporter 5;
DE Short=AtHAK1;
DE Short=AtHAK5;
DE Short=AtPOT5;
GN Name=POT5; Synonyms=HAK5; OrderedLocusNames=At4g13420; ORFNames=T9E8.160;
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, TISSUE SPECIFICITY, INDUCTION, AND
RP MUTANT HAK5-1.
RC STRAIN=cv. Columbia;
RA Rubio F., Santa-Maria G.E., Rodriguez-Navarro A.;
RT "Cloning of Arabidopsis and barley cDNAs encoding HAK potassium
RT transporters in root and shoot cells.";
RL Physiol. Plantarum 109:34-43(2000).
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP 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 [6]
RP INDUCTION.
RX PubMed=20028724; DOI=10.1093/mp/ssp102;
RA Nieves-Cordones M., Aleman F., Martinez V., Rubio F.;
RT "The Arabidopsis thaliana HAK5 K+ transporter is required for plant growth
RT and K+ acquisition from low K+ solutions under saline conditions.";
RL Mol. Plant 3:326-333(2010).
RN [7]
RP FUNCTION.
RX PubMed=20413648; DOI=10.1104/pp.110.154369;
RA Pyo Y.J., Gierth M., Schroeder J.I., Cho M.H.;
RT "High-affinity K(+) transport in Arabidopsis: AtHAK5 and AKT1 are vital for
RT seedling establishment and postgermination growth under low-potassium
RT conditions.";
RL Plant Physiol. 153:863-875(2010).
RN [8]
RP MUTAGENESIS OF PHE-130.
RX PubMed=25228905; DOI=10.3389/fpls.2014.00430;
RA Aleman F., Caballero F., Rodenas R., Rivero R.M., Martinez V., Rubio F.;
RT "The F130S point mutation in the Arabidopsis high-affinity K(+) transporter
RT AtHAK5 increases K(+) over Na(+) and Cs(+) selectivity and confers Na(+)
RT and Cs(+) tolerance to yeast under heterologous expression.";
RL Front. Plant Sci. 5:430-430(2014).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=26474642; DOI=10.1104/pp.15.01401;
RA Ragel P., Rodenas R., Garcia-Martin E., Andres Z., Villalta I.,
RA Nieves-Cordones M., Rivero R.M., Martinez V., Pardo J.M., Quintero F.J.,
RA Rubio F.;
RT "The CBL-interacting protein kinase CIPK23 regulates HAK5-mediated high-
RT affinity K+ uptake in Arabidopsis roots.";
RL Plant Physiol. 169:2863-2873(2015).
RN [10]
RP INTERACTION WITH ILK1.
RX PubMed=27208244; DOI=10.1104/pp.16.00035;
RA Brauer E.K., Ahsan N., Dale R., Kato N., Coluccio A.E., Pineros M.A.,
RA Kochian L.V., Thelen J.J., Popescu S.C.;
RT "The Raf-like kinase ILK1 and the high affinity K+ transporter HAK5 are
RT required for innate immunity and abiotic stress response.";
RL Plant Physiol. 171:1470-1484(2016).
CC -!- FUNCTION: High-affinity potassium transporter. Can also transport
CC rubidium and cesium (Ref.1). Is essential with AKT1 for high-affinity
CC potassium uptake in roots during seedling establishment and
CC postgermination growth under low potassium conditions
CC (PubMed:20413648). Mediates potassium uptake by plant roots in response
CC to low potassium conditions, by a calcium-, CBL-, and CIPK-dependent
CC pathway. Positively regulated by the calcium sensors calcineurin B-like
CC genes CBL1, CBL8, CBL9 and CBL10, and by phosphorylation by CIPK23
CC (PubMed:26474642). {ECO:0000269|PubMed:20413648,
CC ECO:0000269|PubMed:26474642, ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Interacts with ILK1. {ECO:0000269|PubMed:27208244}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the roots.
CC {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Induced in both roots and shoots by potassium starvation
CC (Ref.1). Down-regulated by salt stress in roots (PubMed:20028724).
CC {ECO:0000269|PubMed:20028724, ECO:0000269|Ref.1}.
CC -!- PTM: Phosphorylated at the N-terminus (amino acids 1-95) by CIPK23.
CC {ECO:0000269|PubMed:26474642}.
CC -!- SIMILARITY: Belongs to the HAK/KUP transporter (TC 2.A.72.3) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40777.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78384.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF129478; AAF36490.1; -; mRNA.
DR EMBL; AL049608; CAB40777.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161536; CAB78384.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83277.1; -; Genomic_DNA.
DR PIR; T06299; T06299.
DR RefSeq; NP_567404.1; NM_117416.3.
DR AlphaFoldDB; Q9M7K4; -.
DR STRING; 3702.AT4G13420.1; -.
DR TCDB; 2.A.72.3.9; the k(+) uptake permease (kup) family.
DR iPTMnet; Q9M7K4; -.
DR PaxDb; Q9M7K4; -.
DR PRIDE; Q9M7K4; -.
DR ProteomicsDB; 250607; -.
DR EnsemblPlants; AT4G13420.1; AT4G13420.1; AT4G13420.
DR GeneID; 826973; -.
DR Gramene; AT4G13420.1; AT4G13420.1; AT4G13420.
DR KEGG; ath:AT4G13420; -.
DR Araport; AT4G13420; -.
DR TAIR; locus:2142110; AT4G13420.
DR eggNOG; ENOG502QPSA; Eukaryota.
DR HOGENOM; CLU_008142_2_0_1; -.
DR InParanoid; Q9M7K4; -.
DR OMA; NRCMDEI; -.
DR OrthoDB; 332035at2759; -.
DR PhylomeDB; Q9M7K4; -.
DR PRO; PR:Q9M7K4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M7K4; baseline and differential.
DR Genevisible; Q9M7K4; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0009674; F:potassium:sodium symporter activity; IMP:TAIR.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:TAIR.
DR GO; GO:0006813; P:potassium ion transport; IMP:TAIR.
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; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..785
FT /note="Potassium transporter 5"
FT /id="PRO_0000209081"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..501
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 660..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 130
FT /note="F->S: Increases potassium transport and selectivity;
FT over sodium and cesium."
FT /evidence="ECO:0000269|PubMed:25228905"
FT MUTAGEN 776
FT /note="L->H: In hak5-1; increases transport."
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 785 AA; 87853 MW; D93C7806CDF1FBB0 CRC64;
MDGEEHQIDG DEVNNHENKL NEKKKSWGKL YRPDSFIIEA GQTPTNTGRR SLMSWRTTMS
LAFQSLGVVY GDIGTSPLYV YASTFTDGIN DKDDVVGVLS LIIYTITLVA LLKYVFIVLQ
ANDNGEGGTF ALYSLICRYA KMGLIPNQEP EDVELSNYTL ELPTTQLRRA HMIKEKLENS
KFAKIILFLV TIMGTSMVIG DGILTPSISV LSAVSGIKSL GQNTVVGVSV AILIVLFAFQ
RFGTDKVGFS FAPIILVWFT FLIGIGLFNL FKHDITVLKA LNPLYIIYYF RRTGRQGWIS
LGGVFLCITG TEAMFADLGH FSVRAVQISF SCVAYPALVT IYCGQAAYLT KHTYNVSNTF
YDSIPDPLYW PTFVVAVAAS IIASQAMISG AFSVISQSLR MGCFPRVKVV HTSAKYEGQV
YIPEINYLLM LACIAVTLAF RTTEKIGHAY GIAVVTVMVI TTLMVTLIML VIWKTNIVWI
AIFLVVFGSI EMLYLSSVMY KFTSGGYLPL TITVVLMAMM AIWQYVHVLK YRYELREKIS
RENAIQMATS PDVNRVPGIG LFYTELVNGI TPLFSHYISN LSSVHSVFVL ISIKTLPVNR
VTSSERFFFR YVGPKDSGMF RCVVRYGYKE DIEEPDEFER HFVYYLKEFI HHEHFMSGGG
GEVDETDKEE EPNAETTVVP SSNYVPSSGR IGSAHSSSSD KIRSGRVVQV QSVEDQTELV
EKAREKGMVY LMGETEITAE KESSLFKKFI VNHAYNFLKK NCREGDKALA IPRSKLLKVG
MTYEL
