NHX2_ARATH
ID NHX2_ARATH Reviewed; 546 AA.
AC Q56XP4; Q9CAW6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Sodium/hydrogen exchanger 2;
DE AltName: Full=Na(+)/H(+) exchanger 2;
DE Short=NHE-2;
GN Name=NHX2; OrderedLocusNames=At3g05030; ORFNames=T9J14.2;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INDUCTION.
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 [2]
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 [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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in low affinity electroneutral exchange of protons for
CC cations such as Na(+) or K(+) across membranes. May also exchange Li(+)
CC and Cs(+) with a lower affinity. Involved in vacuolar ion
CC compartmentalization necessary for cell volume regulation and
CC cytoplasmic Na(+) detoxification. {ECO:0000269|PubMed:12047628}.
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:0000269|PubMed:12047628};
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:0000269|PubMed:12047628};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12047628};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12047628}.
CC Note=Tonoplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q56XP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q56XP4-2; Sequence=VSP_016701, VSP_016702;
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:12047628}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), and by NaCl and sorbitol in
CC a ABA-dependent manner. {ECO:0000269|PubMed:12047628}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
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DR EMBL; AF490586; AAM08403.1; -; mRNA.
DR EMBL; AC009465; AAG51408.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74177.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74178.2; -; Genomic_DNA.
DR EMBL; CP002686; ANM64164.1; -; Genomic_DNA.
DR EMBL; AK221629; BAD95253.1; -; mRNA.
DR RefSeq; NP_001319475.1; NM_001337553.1. [Q56XP4-1]
DR RefSeq; NP_001326210.1; NM_001337555.1. [Q56XP4-1]
DR RefSeq; NP_187154.1; NM_111375.4. [Q56XP4-1]
DR AlphaFoldDB; Q56XP4; -.
DR SMR; Q56XP4; -.
DR STRING; 3702.AT3G05030.1; -.
DR TCDB; 2.A.36.5.9; the monovalent cation:proton antiporter-1 (cpa1) family.
DR iPTMnet; Q56XP4; -.
DR PaxDb; Q56XP4; -.
DR PRIDE; Q56XP4; -.
DR ProteomicsDB; 250511; -. [Q56XP4-1]
DR EnsemblPlants; AT3G05030.1; AT3G05030.1; AT3G05030. [Q56XP4-1]
DR EnsemblPlants; AT3G05030.2; AT3G05030.2; AT3G05030. [Q56XP4-1]
DR EnsemblPlants; AT3G05030.4; AT3G05030.4; AT3G05030. [Q56XP4-1]
DR GeneID; 819665; -.
DR Gramene; AT3G05030.1; AT3G05030.1; AT3G05030. [Q56XP4-1]
DR Gramene; AT3G05030.2; AT3G05030.2; AT3G05030. [Q56XP4-1]
DR Gramene; AT3G05030.4; AT3G05030.4; AT3G05030. [Q56XP4-1]
DR KEGG; ath:AT3G05030; -.
DR Araport; AT3G05030; -.
DR TAIR; locus:2114810; AT3G05030.
DR eggNOG; KOG1965; Eukaryota.
DR HOGENOM; CLU_005912_11_2_1; -.
DR InParanoid; Q56XP4; -.
DR OMA; GLIVGHD; -.
DR PhylomeDB; Q56XP4; -.
DR PRO; PR:Q56XP4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q56XP4; baseline and differential.
DR Genevisible; Q56XP4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IDA:TAIR.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:TAIR.
DR GO; GO:0055075; P:potassium ion homeostasis; IGI:TAIR.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:TAIR.
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:0090333; P:regulation of stomatal closure; IGI: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.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antiport; Glycoprotein; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Sodium;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..546
FT /note="Sodium/hydrogen exchanger 2"
FT /id="PRO_0000052373"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..47
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..148
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT INTRAMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..218
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..304
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..381
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..546
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_016701"
FT VAR_SEQ 126..129
FT /note="IISL -> MFET (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_016702"
SQ SEQUENCE 546 AA; 60523 MW; BEA270D40446360B CRC64;
MTMFASLTSK MLSVSTSDHA SVVSLNLFVA LLCACIVIGH LLEENRWMNE SITALLIGLG
TGVVILLISR GKNSHLLVFS EDLFFIYLLP PIIFNAGFQV KKKQFFRNFV TIMAFGAIGT
VVSCTIISLG AIQFFKKLDI GTFDLGDFLA IGAIFAATDS VCTLQVLNQD ETPLLYSLVF
GEGVVNDATS VVLFNAIQSF DLTHLNHEAA FQFLGNFFYL FLLSTGLGVA TGLISAYVIK
KLYFGRHSTD REVALMMLMA YLSYMLAELF ALSGILTVFF CGIVMSHYTW HNVTESSRIT
TKHAFATLSF LAETFIFLYV GMDALDIEKW RFVSDSPGTS VAVSSILMGL VMLGRAAFVF
PLSFLSNLAK KHQSEKISIK QQVVIWWAGL MRGAVSMALA YNKFTRSGHT ELRGNAIMIT
STITVCLFST MVFGMLTKPL IRYLMPHQKA TTSTTSMLSD DSTPKSIHIP LLDGEQLDSF
ELPGSHQDVP RPNSLRGFLM RPTRTVHYYW RQFDDAFMRP VFGGRGFVPF VPGSPTERSS
HDLSKP
