NHX6_ARATH
ID NHX6_ARATH Reviewed; 535 AA.
AC Q8RWU6; Q8S395; Q9MA14;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Sodium/hydrogen exchanger 6;
DE AltName: Full=Na(+)/H(+) exchanger 6;
DE Short=NHE-6;
GN Name=NHX6; OrderedLocusNames=At1g79610; ORFNames=F20B17.4;
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 2), AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 1).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470, 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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21278129; DOI=10.1105/tpc.110.079426;
RA Bassil E., Ohto M.A., Esumi T., Tajima H., Zhu Z., Cagnac O., Belmonte M.,
RA Peleg Z., Yamaguchi T., Blumwald E.;
RT "The Arabidopsis intracellular Na+/H+ antiporters NHX5 and NHX6 are
RT endosome associated and necessary for plant growth and development.";
RL Plant Cell 23:224-239(2011).
CC -!- FUNCTION: Involved in trafficking to the vacuole (PubMed:21278129).
CC Required for cell proliferation and cell expansion, but not for cell
CC differentiation (PubMed:21278129). Acts in low affinity electroneutral
CC exchange of protons for cations such as Na(+) or K(+) across membranes
CC (By similarity). May also exchange Li(+) and Cs(+) with a lower
CC affinity (By similarity). {ECO:0000250|UniProtKB:Q68KI4,
CC ECO:0000269|PubMed:21278129}.
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: Endosome membrane {ECO:0000269|PubMed:21278129};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21278129}. Golgi
CC apparatus, Golgi stack membrane {ECO:0000269|PubMed:21278129}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:21278129}. Golgi apparatus,
CC trans-Golgi network membrane {ECO:0000269|PubMed:21278129}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:21278129}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWU6-2; Sequence=VSP_016703;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Detected at very low levels in roots and shoots.
CC {ECO:0000269|PubMed:12047628, ECO:0000269|PubMed:21278129}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to redundancy with
CC NHX5. Nhx5 and nhx6 double mutant has a slower development, is
CC drastically smaller and is salt sensitive.
CC {ECO:0000269|PubMed:21278129}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
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=AAF68127.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF490590; AAM08407.1; -; mRNA.
DR EMBL; AC010793; AAF68127.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36272.1; -; Genomic_DNA.
DR EMBL; AY091100; AAM14051.1; -; mRNA.
DR EMBL; AY133748; AAM91682.1; -; mRNA.
DR PIR; D96827; D96827.
DR RefSeq; NP_178079.2; NM_106609.4. [Q8RWU6-1]
DR AlphaFoldDB; Q8RWU6; -.
DR SMR; Q8RWU6; -.
DR BioGRID; 29518; 4.
DR IntAct; Q8RWU6; 1.
DR STRING; 3702.AT1G79610.1; -.
DR iPTMnet; Q8RWU6; -.
DR PaxDb; Q8RWU6; -.
DR PRIDE; Q8RWU6; -.
DR ProteomicsDB; 236826; -. [Q8RWU6-1]
DR EnsemblPlants; AT1G79610.1; AT1G79610.1; AT1G79610. [Q8RWU6-1]
DR GeneID; 844299; -.
DR Gramene; AT1G79610.1; AT1G79610.1; AT1G79610. [Q8RWU6-1]
DR KEGG; ath:AT1G79610; -.
DR Araport; AT1G79610; -.
DR TAIR; locus:2019853; AT1G79610.
DR eggNOG; KOG1965; Eukaryota.
DR HOGENOM; CLU_005912_11_1_1; -.
DR InParanoid; Q8RWU6; -.
DR OMA; AGMMMNY; -.
DR OrthoDB; 559433at2759; -.
DR PRO; PR:Q8RWU6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWU6; baseline and differential.
DR Genevisible; Q8RWU6; AT.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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: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: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 1: Evidence at protein level;
KW Alternative splicing; Antiport; Endosome; Glycoprotein; Golgi apparatus;
KW Ion transport; Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..535
FT /note="Sodium/hydrogen exchanger 6"
FT /id="PRO_0000052377"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..49
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..215
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..306
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..382
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..535
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 508..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 520..535
FT /note="EERIPFTRRGNLNNRG -> GNNIIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12047628"
FT /id="VSP_016703"
FT CONFLICT 243
FT /note="L -> H (in Ref. 2; AAF68127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59314 MW; 101E72E26D409080 CRC64;
MSSELQISPA IHDPQGQEKQ QQAAGVGILL QIMMLVLSFV LGHVLRRHKF YYLPEASASL
LIGLIVGGLA NISNTETSIR TWFNFHDEFF FLFLLPPIIF QSGFSLQPKP FFSNFGAIVT
FSVLGTFVAS MVTGLLVYLG GVMFLMYRLP FVECLMFGSL ISATDPVTVL SIFQELGSDV
NLYALVFGES VLNDAMAISL YRTMSLVRSH SSGQNFFMVI VRFLETFVGS MSAGVGVGFT
SALLFKYAGL DVDNLQNLEC CLFVLFPYFS YMLAEGLSLS GIVSILFTGI VMKHYTYSNL
SANSQRFVSA FFHLISSLAE TFVFIYMGFD IAMEKHSWSH LGFIFFSILF IVIARAANVF
GCGYLVNLAR PAHRKIPMTH QKALWYSGLR GAMAFALALQ SVHDLPEGHG QTIFTATTAI
VVLTVLLIGG STGTMLEALE VVGDSHDTSL GDGFEVVNSR YMTSYDDEDT PPGSGFRTKL
REFHKSAASF TELDRNYLTP FFTSNNGDYD DEGNMEQHHE ERIPFTRRGN LNNRG
