NHX3_ARATH
ID NHX3_ARATH Reviewed; 503 AA.
AC Q84WG1; Q9SQU0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Sodium/hydrogen exchanger 3;
DE AltName: Full=Na(+)/H(+) exchanger 3;
DE Short=NHE-3;
GN Name=NHX3; OrderedLocusNames=At3g06370; ORFNames=F24P17.16;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12047628; DOI=10.1046/j.1365-313x.2002.01309.x;
RA Yokoi S., Quintero F.J., Cubero B., Ruiz M.T., Bressan R.A., Hasegawa P.M.,
RA Pardo J.M.;
RT "Differential expression and function of Arabidopsis thaliana NHX
RT Na(+)/H(+) antiporters in the salt stress response.";
RL Plant J. 30:529-539(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
CC -!- FUNCTION: May act in low affinity electroneutral exchange of protons
CC for cations such as Na(+) or K(+) across membranes. May also exchange
CC Li(+) and Cs(+) with a lower affinity. {ECO:0000250|UniProtKB:Q68KI4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out);
CC Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:Q68KI4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q68KI4};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019};
CC Multi-pass membrane protein {ECO:0000255}. Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:12047628}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF08577.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011623; AAF08577.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74383.1; -; Genomic_DNA.
DR EMBL; BT003855; AAO41905.1; -; mRNA.
DR RefSeq; NP_001327377.1; NM_001337652.1.
DR RefSeq; NP_001327379.1; NM_001337651.1.
DR RefSeq; NP_187288.2; NM_111512.3.
DR AlphaFoldDB; Q84WG1; -.
DR SMR; Q84WG1; -.
DR BioGRID; 5146; 2.
DR IntAct; Q84WG1; 2.
DR STRING; 3702.AT3G06370.1; -.
DR PaxDb; Q84WG1; -.
DR EnsemblPlants; AT3G06370.1; AT3G06370.1; AT3G06370.
DR GeneID; 819811; -.
DR Gramene; AT3G06370.1; AT3G06370.1; AT3G06370.
DR KEGG; ath:AT3G06370; -.
DR Araport; AT3G06370; -.
DR TAIR; locus:2081111; AT3G06370.
DR eggNOG; KOG1965; Eukaryota.
DR HOGENOM; CLU_005912_11_2_1; -.
DR InParanoid; Q84WG1; -.
DR OrthoDB; 546232at2759; -.
DR PhylomeDB; Q84WG1; -.
DR PRO; PR:Q84WG1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84WG1; baseline and differential.
DR Genevisible; Q84WG1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR InterPro; IPR004709; NaH_exchanger.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
PE 1: Evidence at protein level;
KW Antiport; Glycoprotein; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..503
FT /note="Sodium/hydrogen exchanger 3"
FT /id="PRO_0000052374"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..51
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..138
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..219
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..305
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..383
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..503
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 102
FT /note="K -> E (in Ref. 3; AAO41905)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="V -> F (in Ref. 3; AAO41905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 55606 MW; 80196C98546FAFEC CRC64;
MVIGLSTMLE KTEALFASDH ASVVSMNLFV ALLCACIVLG HLLEETRWMN ESITALIIGS
CTGIVILLIS GGKSSRILVF SEDLFFIYLL PPIIFNAGFQ VKKKQFFRNF MTIMLFGAIG
TLISFVIISF GAKHLFEKMN IGDLTIADYL AIGAIFSATD SVCTLQVLNQ DETPLLYSLV
FGEGVVNDAT SVVLFNAIQR FDLTNINSAI ALEFAGNFFY LFILSTALGV AAGLLSAFVI
KKLYIGRHST DREVALMMLL AYLSYMLAEL FHLSSILTVF FCGIVMSHYT WHNVTDKSKV
TTKHTFAAMS FLAEIFIFLY VGMDALDIEK WDVVRNSPGQ SIGVSSILLG LILLGRAAFV
FPLSFLSNLT KSSPDEKIDL KKQVTIWWAG LMRGAVSMAL AYNQFTTSGH TKVLGNAIMI
TSTITVVLFS TVVFGLLTKP LVKHLQPSSK QSSTTALQIT LRSSFHDPIL HEPLLSTQGQ
SEYDPEQHVS FRMFWKSPSR FTH
