HKT1_ARATH
ID HKT1_ARATH Reviewed; 506 AA.
AC Q84TI7; O82614; Q68KI5; Q9M570; Q9SV90;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Sodium transporter HKT1;
DE Short=AtHKT1;
GN Name=HKT1; OrderedLocusNames=At4g10310; ORFNames=T9A4.5;
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 TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10759522; DOI=10.1104/pp.122.4.1249;
RA Uozumi N., Kim E.J., Rubio F., Yamaguchi T., Muto S., Tsuboi A.,
RA Bakker E.P., Nakamura T., Schroeder J.I.;
RT "The Arabidopsis HKT1 gene homolog mediates inward Na(+) currents in
RT Xenopus laevis oocytes and Na(+) uptake in Saccharomyces cerevisiae.";
RL Plant Physiol. 122:1249-1259(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang J.L., Wang D., Zhang J.W.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP TOPOLOGY, GLYCOSYLATION AT ASN-429, AND MUTAGENESIS OF GLU-194; GLY-213;
RP ASN-429 AND PHE-443.
RX PubMed=11344270; DOI=10.1073/pnas.101556598;
RA Kato Y., Sakaguchi M., Mori Y., Saito K., Nakamura T., Bakker E.P.,
RA Sato Y., Goshima S., Uozumi N.;
RT "Evidence in support of a four transmembrane-pore-transmembrane topology
RT model for the Arabidopsis thaliana Na+/K+ translocating AtHKT1 protein, a
RT member of the superfamily of K+ transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6488-6493(2001).
RN [7]
RP FUNCTION.
RX PubMed=11698666; DOI=10.1073/pnas.241501798;
RA Rus A., Yokoi S., Sharkhuu A., Reddy M., Lee B.-H., Matsumoto T.K.,
RA Koiwa H., Zhu J.-K., Bressan R.A., Hasegawa P.M.;
RT "AtHKT1 is a salt tolerance determinant that controls Na(+) entry into
RT plant roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14150-14155(2001).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF SER-68.
RX PubMed=11959905; DOI=10.1073/pnas.082123799;
RA Maeser P., Hosoo Y., Goshima S., Horie T., Eckelman B., Yamada K.,
RA Yoshida K., Bakker E.P., Shinmyo A., Oiki S., Schroeder J.I., Uozumi N.;
RT "Glycine residues in potassium channel-like selectivity filters determine
RT potassium selectivity in four-loop-per-subunit HKT transporters from
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6428-6433(2002).
RN [9]
RP FUNCTION.
RX PubMed=12417304; DOI=10.1016/s0014-5793(02)03488-9;
RA Maeser P., Eckelman B., Vaidyanathan R., Horie T., Fairbairn D.J., Kubo M.,
RA Yamagami M., Yamaguchi K., Nishimura M., Uozumi N., Robertson W.,
RA Sussman M.R., Schroeder J.I.;
RT "Altered shoot/root Na+ distribution and bifurcating salt sensitivity in
RT Arabidopsis by genetic disruption of the Na+ transporter AtHKT1.";
RL FEBS Lett. 531:157-161(2002).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-282 AND GLY-325.
RX PubMed=12727868; DOI=10.1093/emboj/cdg207;
RA Berthomieu P., Conejero G., Nublat A., Brackenbury W.J., Lambert C.,
RA Savio C., Uozumi N., Oiki S., Yamada K., Cellier F., Gosti F.,
RA Simonneau T., Essah P.A., Tester M., Very A.-A., Sentenac H., Casse F.;
RT "Functional analysis of AtHKT1 in Arabidopsis shows that Na(+)
RT recirculation by the phloem is crucial for salt tolerance.";
RL EMBO J. 22:2004-2014(2003).
RN [11]
RP FUNCTION.
RX PubMed=15347798; DOI=10.1104/pp.104.042234;
RA Rus A., Lee B.-H., Munoz-Mayor A., Sharkhuu A., Miura K., Zhu J.-K.,
RA Bressan R.A., Hasegawa P.M.;
RT "AtHKT1 facilitates Na+ homeostasis and K+ nutrition in planta.";
RL Plant Physiol. 136:2500-2511(2004).
RN [12]
RP FUNCTION.
RX PubMed=15486089; DOI=10.1073/pnas.0404780101;
RA Gong J.-M., Waner D.A., Horie T., Li S.L., Horie R., Abid K.B.,
RA Schroeder J.I.;
RT "Microarray-based rapid cloning of an ion accumulation deletion mutant in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15404-15409(2004).
CC -!- FUNCTION: Sodium transporter protein, which plays a central role in
CC plant tolerance to salt. Upon prolongated exposure to high
CC concentrations, Na(+) translocates from the roots to the transpiring
CC leaves where it can increase to toxic level. Involved in Na(+)
CC recirculation from shoots to roots, probably by mediating Na(+) loading
CC into the phloem sap in shoots and unloading in roots, thereby removing
CC large amounts of Na(+) from the shoot. Does not transport K(+) but
CC regulates K(+) nutrient status via its ability to facilitate Na(+)
CC homeostasis. Probably not involved in root uptake of Na(+).
CC {ECO:0000269|PubMed:10759522, ECO:0000269|PubMed:11698666,
CC ECO:0000269|PubMed:11959905, ECO:0000269|PubMed:12417304,
CC ECO:0000269|PubMed:12727868, ECO:0000269|PubMed:15347798,
CC ECO:0000269|PubMed:15486089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10759522,
CC ECO:0000269|PubMed:11959905};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed in flowers,
CC leaves and stems. Expressed in the vascular tissues of every organs. In
CC roots, leaves and flower peduncles, it is only expressed in the phloem
CC tissues. Not expressed in root peripheral cells.
CC {ECO:0000269|PubMed:10759522, ECO:0000269|PubMed:12727868}.
CC -!- PTM: N-glycosylated. Not essential for functional expression and
CC membrane targeting. {ECO:0000269|PubMed:11344270}.
CC -!- MISCELLANEOUS: In contrast to K(+) channel proteins, it lacks a
CC conserved Gly at position 68, explaining why it does not act as a K(+)
CC transporter.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family. HKT (TC
CC 2.A.38.3) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62807.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB39784.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78154.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF237672; AAF68393.1; -; mRNA.
DR EMBL; AY685182; AAT95386.1; -; mRNA.
DR EMBL; AF096373; AAC62807.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049488; CAB39784.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161517; CAB78154.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82866.1; -; Genomic_DNA.
DR EMBL; BT005751; AAO64157.1; -; mRNA.
DR PIR; T01969; T01969.
DR PIR; T04046; T04046.
DR RefSeq; NP_567354.1; NM_117099.6.
DR AlphaFoldDB; Q84TI7; -.
DR STRING; 3702.AT4G10310.1; -.
DR TCDB; 2.A.38.3.2; the k(+) transporter (trk) family.
DR iPTMnet; Q84TI7; -.
DR PaxDb; Q84TI7; -.
DR PRIDE; Q84TI7; -.
DR ProteomicsDB; 230397; -.
DR EnsemblPlants; AT4G10310.1; AT4G10310.1; AT4G10310.
DR GeneID; 826623; -.
DR Gramene; AT4G10310.1; AT4G10310.1; AT4G10310.
DR KEGG; ath:AT4G10310; -.
DR Araport; AT4G10310; -.
DR TAIR; locus:2122749; AT4G10310.
DR eggNOG; KOG1341; Eukaryota.
DR HOGENOM; CLU_008384_2_0_1; -.
DR InParanoid; Q84TI7; -.
DR OMA; MFEISSA; -.
DR OrthoDB; 385384at2759; -.
DR PhylomeDB; Q84TI7; -.
DR BioCyc; MetaCyc:MON-14577; -.
DR PRO; PR:Q84TI7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84TI7; baseline and differential.
DR Genevisible; Q84TI7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0006814; P:sodium ion transport; IMP:TAIR.
DR InterPro; IPR003445; Cat_transpt.
DR InterPro; IPR004773; K/Na_transp_Trk/HKT.
DR Pfam; PF02386; TrkH; 1.
DR TIGRFAMs; TIGR00934; 2a38euk; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..506
FT /note="Sodium transporter HKT1"
FT /id="PRO_0000070465"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11344270"
FT MUTAGEN 68
FT /note="S->G: Gives some permeability to potassium."
FT /evidence="ECO:0000269|PubMed:11959905"
FT MUTAGEN 194
FT /note="E->N: Does not create a new N-glycosylation site;
FT when associated with Q-429."
FT /evidence="ECO:0000269|PubMed:11344270"
FT MUTAGEN 213
FT /note="G->S: Creates a new N-glycosylation site."
FT /evidence="ECO:0000269|PubMed:11344270"
FT MUTAGEN 282
FT /note="S->L: In sas2-1; induces a strong decrease in sodium
FT in the phloem sap leading to sodium accumulation in aerial
FT organs."
FT /evidence="ECO:0000269|PubMed:12727868"
FT MUTAGEN 325
FT /note="G->E: In sas2-2; induces increased sensitivity to
FT salt."
FT /evidence="ECO:0000269|PubMed:12727868"
FT MUTAGEN 429
FT /note="N->Q: Loss of N-glycosylation. no effect on
FT function. Does not create a new N-glycosylation site; when
FT associated with N-194."
FT /evidence="ECO:0000269|PubMed:11344270"
FT MUTAGEN 443
FT /note="F->N: Compensate the N-glycosylation site; when
FT associated with Q-429."
FT /evidence="ECO:0000269|PubMed:11344270"
FT CONFLICT 148
FT /note="K -> R (in Ref. 2; AAT95386)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="K -> E (in Ref. 2; AAT95386)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="Y -> H (in Ref. 2; AAT95386)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="V -> L (in Ref. 1; AAF68393)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="A -> V (in Ref. 1; AAF68393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 57450 MW; 606CD744E74C3943 CRC64;
MDRVVAKIAK IRSQLTKLRS LFFLYFIYFL FFSFLGFLAL KITKPRTTSR PHDFDLFFTS
VSAITVSSMS TVDMEVFSNT QLIFLTILMF LGGEIFTSFL NLYVSYFTKF VFPHNKIRHI
LGSYNSDSSI EDRCDVETVT DYREGLIKID ERASKCLYSV VLSYHLVTNL VGSVLLLVYV
NFVKTARDVL SSKEISPLTF SVFTTVSTFA NCGFVPTNEN MIIFRKNSGL IWLLIPQVLM
GNTLFPCFLV LLIWGLYKIT KRDEYGYILK NHNKMGYSHL LSVRLCVLLG VTVLGFLIIQ
LLFFCAFEWT SESLEGMSSY EKLVGSLFQV VNSRHTGETI VDLSTLSPAI LVLFILMMYL
PPYTLFMPLT EQKTIEKEGG DDDSENGKKV KKSGLIVSQL SFLTICIFLI SITERQNLQR
DPINFNVLNI TLEVISAYGN VGFTTGYSCE RRVDISDGGC KDASYGFAGR WSPMGKFVLI
IVMFYGRFKQ FTAKSGRAWI LYPSSS
