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NHX7_ARATH
ID   NHX7_ARATH              Reviewed;        1146 AA.
AC   Q9LKW9; Q9ZPS6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Sodium/hydrogen exchanger 7;
DE   AltName: Full=Na(+)/H(+) exchanger 7;
DE            Short=NHE-7;
DE   AltName: Full=Protein SALT OVERLY SENSITIVE 1;
GN   Name=NHX7; Synonyms=SOS1; OrderedLocusNames=At2g01980; ORFNames=F14H20.5;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION,
RP   AND MUTAGENESIS OF GLY-136; ARG-365; GLY-777 AND GLY-784.
RX   PubMed=10823923; DOI=10.1073/pnas.120170197;
RA   Shi H., Ishitani M., Kim C., Zhu J.-K.;
RT   "The Arabidopsis thaliana salt tolerance gene SOS1 encodes a putative
RT   Na(+)/H(+) antiporter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:6896-6901(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   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   [5]
RP   FUNCTION, AND MUTAGENESIS OF ARG-365.
RX   PubMed=12239394; DOI=10.2307/3870339;
RA   Wu S.-J., Ding L., Zhu J.-K.;
RT   "SOS1, a genetic locus essential for salt tolerance and potassium
RT   acquisition.";
RL   Plant Cell 8:617-627(1996).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=11884687; DOI=10.1105/tpc.010371;
RA   Shi H., Quintero F.J., Pardo J.M., Zhu J.-K.;
RT   "The putative plasma membrane Na(+)/H(+) antiporter SOS1 controls long-
RT   distance Na(+) transport in plants.";
RL   Plant Cell 14:465-477(2002).
RN   [7]
RP   FUNCTION, AND REGULATION.
RX   PubMed=12034882; DOI=10.1073/pnas.122224699;
RA   Qiu Q.-S., Guo Y., Dietrich M.A., Schumaker K.S., Zhu J.-K.;
RT   "Regulation of SOS1, a plasma membrane Na(+)/H(+) exchanger in Arabidopsis
RT   thaliana, by SOS2 and SOS3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8436-8441(2002).
RN   [8]
RP   PHOSPHORYLATION, INTERACTION WITH CIPK24/SOS2 AND CBL4/SOS3, AND
RP   REGULATION.
RX   PubMed=12070350; DOI=10.1073/pnas.132092099;
RA   Quintero F.J., Ohta M., Shi H., Zhu J.-K., Pardo J.M.;
RT   "Reconstitution in yeast of the Arabidopsis SOS signaling pathway for Na(+)
RT   homeostasis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9061-9066(2002).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. La-0;
RX   PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT   immobilized metal ion affinity chromatography and mass spectrometry.";
RL   Mol. Cell. Proteomics 2:1234-1243(2003).
RN   [10]
RP   FUNCTION.
RX   PubMed=12469134; DOI=10.1038/nbt766;
RA   Shi H., Lee B.-H., Wu S.-J., Zhu J.-K.;
RT   "Overexpression of a plasma membrane Na(+)/H(+) antiporter gene improves
RT   salt tolerance in Arabidopsis thaliana.";
RL   Nat. Biotechnol. 21:81-85(2003).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12805632; DOI=10.1104/pp.102.010421;
RA   Qiu Q.-S., Barkla B.J., Vera-Estrella R., Zhu J.-K., Schumaker K.S.;
RT   "Na(+)/H(+) exchange activity in the plasma membrane of Arabidopsis.";
RL   Plant Physiol. 132:1041-1052(2003).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT   phosphorylation site database.";
RL   Plant Cell 16:2394-2405(2004).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA   Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT   "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT   phosphorylation sites in secondary active transporters.";
RL   Biochem. Biophys. Res. Commun. 363:375-380(2007).
CC   -!- FUNCTION: Acts in electroneutral exchange of protons for cations such
CC       as Na(+) or Li(+) across plasma membrane. Involved in Na(+) and K(+)
CC       homeostasis. Required for cytoplasmic Na(+) and Li(+) detoxification by
CC       secreting them from the cytoplasm to the extracellular space. Regulates
CC       Na(+) content of the xylem sap. {ECO:0000269|PubMed:10823923,
CC       ECO:0000269|PubMed:11884687, ECO:0000269|PubMed:12034882,
CC       ECO:0000269|PubMed:12239394, ECO:0000269|PubMed:12469134,
CC       ECO:0000269|PubMed:12805632}.
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:12239394};
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:12239394};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22.8 mM for Na(+) {ECO:0000269|PubMed:12805632};
CC   -!- SUBUNIT: Interacts with CIPK24/SOS2 and CBL4/SOS3.
CC       {ECO:0000269|PubMed:12070350}.
CC   -!- INTERACTION:
CC       Q9LKW9; Q9LDI3: CIPK24; NbExp=4; IntAct=EBI-2368285, EBI-537551;
CC       Q9LKW9; Q8RY59: RCD1; NbExp=5; IntAct=EBI-2368285, EBI-2118043;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11884687,
CC       ECO:0000269|PubMed:12805632}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11884687, ECO:0000269|PubMed:12805632}.
CC   -!- TISSUE SPECIFICITY: More expressed in roots than in shoots. Mostly
CC       localized in parenchyma cells at the xylem/symplast boundary in roots,
CC       hypocotyls, stems and leaves. Also present in root tips epidermal
CC       cells. {ECO:0000269|PubMed:10823923, ECO:0000269|PubMed:11884687}.
CC   -!- INDUCTION: By Na(+), in a SOS signaling pathway-dependent manner.
CC       {ECO:0000269|PubMed:10823923, ECO:0000269|PubMed:11884687}.
CC   -!- PTM: Phosphorylated by CIPK24/SOS2 in complex with CBL4/SOS3.
CC       {ECO:0000269|PubMed:12070350}.
CC   -!- MISCELLANEOUS: Positively regulated by the salt overly sensitive (SOS)
CC       signaling pathway that involves the kinase CIPK24/SOS2 and the calcium
CC       sensor CBL4/SOS3.
CC   -!- MISCELLANEOUS: Transgenic plants that overexpress NHX7 have enhanced
CC       capability to grow on high saline soils.
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=AAD20091.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF256224; AAF76139.1; -; Genomic_DNA.
DR   EMBL; AC006532; AAD20091.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC05529.1; -; Genomic_DNA.
DR   EMBL; AY062746; AAL32824.1; -; mRNA.
DR   PIR; E84431; E84431.
DR   RefSeq; NP_178307.2; NM_126259.4.
DR   AlphaFoldDB; Q9LKW9; -.
DR   SMR; Q9LKW9; -.
DR   BioGRID; 132; 3.
DR   DIP; DIP-52883N; -.
DR   IntAct; Q9LKW9; 2.
DR   STRING; 3702.AT2G01980.1; -.
DR   TCDB; 2.A.36.7.6; the monovalent cation:proton antiporter-1 (cpa1) family.
DR   iPTMnet; Q9LKW9; -.
DR   PaxDb; Q9LKW9; -.
DR   PRIDE; Q9LKW9; -.
DR   ProteomicsDB; 249438; -.
DR   EnsemblPlants; AT2G01980.1; AT2G01980.1; AT2G01980.
DR   GeneID; 814729; -.
DR   Gramene; AT2G01980.1; AT2G01980.1; AT2G01980.
DR   KEGG; ath:AT2G01980; -.
DR   Araport; AT2G01980; -.
DR   TAIR; locus:2041100; AT2G01980.
DR   eggNOG; KOG1965; Eukaryota.
DR   HOGENOM; CLU_008625_0_0_1; -.
DR   InParanoid; Q9LKW9; -.
DR   OMA; DMITSHP; -.
DR   OrthoDB; 99426at2759; -.
DR   PhylomeDB; Q9LKW9; -.
DR   PRO; PR:Q9LKW9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9LKW9; baseline and differential.
DR   Genevisible; Q9LKW9; AT.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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; IMP:TAIR.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEP:TAIR.
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   GO; GO:0006814; P:sodium ion transport; IMP:TAIR.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   PANTHER; PTHR10110; PTHR10110; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
PE   1: Evidence at protein level;
KW   Antiport; Cell membrane; Ion transport; Membrane; Phosphoprotein;
KW   Potassium; Potassium transport; Reference proteome; Sodium;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1146
FT                   /note="Sodium/hydrogen exchanger 7"
FT                   /id="PRO_0000052378"
FT   TOPO_DOM        1..28
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..99
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..159
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..191
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..352
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..387
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        409..420
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        442..1146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          981..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         136
FT                   /note="G->E: In sos1-12; hypersensitivity to Na(+) and
FT                   Li(+)."
FT                   /evidence="ECO:0000269|PubMed:10823923"
FT   MUTAGEN         365
FT                   /note="R->C: In sos1-3; hypersensitivity to Na(+) and
FT                   Li(+)."
FT                   /evidence="ECO:0000269|PubMed:10823923,
FT                   ECO:0000269|PubMed:12239394"
FT   MUTAGEN         777
FT                   /note="G->E: In sos1-8; hypersensitivity to Na(+) and
FT                   Li(+)."
FT                   /evidence="ECO:0000269|PubMed:10823923"
FT   MUTAGEN         784
FT                   /note="G->D: In sos1-9; hypersensitivity to Na(+) and
FT                   Li(+)."
FT                   /evidence="ECO:0000269|PubMed:10823923"
SQ   SEQUENCE   1146 AA;  127188 MW;  DAEA315426F8AE7A CRC64;
     MTTVIDATMA YRFLEEATDS SSSSSSSKLE SSPVDAVLFV GMSLVLGIAS RHLLRGTRVP
     YTVALLVIGI ALGSLEYGAK HNLGKIGHGI RIWNEIDPEL LLAVFLPALL FESSFSMEVH
     QIKRCLGQMV LLAVPGVLIS TACLGSLVKV TFPYEWDWKT SLLLGGLLSA TDPVAVVALL
     KELGASKKLS TIIEGESLMN DGTAIVVFQL FLKMAMGQNS DWSSIIKFLL KVALGAVGIG
     LAFGIASVIW LKFIFNDTVI EITLTIAVSY FAYYTAQEWA GASGVLTVMT LGMFYAAFAR
     TAFKGDSQKS LHHFWEMVAY IANTLIFILS GVVIAEGILD SDKIAYQGNS WRFLFLLYVY
     IQLSRVVVVG VLYPLLCRFG YGLDWKESII LVWSGLRGAV ALALSLSVKQ SSGNSHISKE
     TGTLFLFFTG GIVFLTLIVN GSTTQFVLRL LRMDILPAPK KRILEYTKYE MLNKALRAFQ
     DLGDDEELGP ADWPTVESYI SSLKGSEGEL VHHPHNGSKI GSLDPKSLKD IRMRFLNGVQ
     ATYWEMLDEG RISEVTANIL MQSVDEALDQ VSTTLCDWRG LKPHVNFPNY YNFLHSKVVP
     RKLVTYFAVE RLESACYISA AFLRAHTIAR QQLYDFLGES NIGSIVINES EKEGEEAKKF
     LEKVRSSFPQ VLRVVKTKQV TYSVLNHLLG YIENLEKVGL LEEKEIAHLH DAVQTGLKKL
     LRNPPIVKLP KLSDMITSHP LSVALPPAFC EPLKHSKKEP MKLRGVTLYK EGSKPTGVWL
     IFDGIVKWKS KILSNNHSLH PTFSHGSTLG LYEVLTGKPY LCDLITDSMV LCFFIDSEKI
     LSLQSDSTID DFLWQESALV LLKLLRPQIF ESVAMQELRA LVSTESSKLT TYVTGESIEI
     DCNSIGLLLE GFVKPVGIKE ELISSPAALS PSNGNQSFHN SSEASGIMRV SFSQQATQYI
     VETRARAIIF NIGAFGADRT LHRRPSSLTP PRSSSSDQLQ RSFRKEHRGL MSWPENIYAK
     QQQEINKTTL SLSERAMQLS IFGSMVNVYR RSVSFGGIYN NKLQDNLLYK KLPLNPAQGL
     VSAKSESSIV TKKQLETRKH ACQLPLKGES STRQNTMVES SDEEDEDEGI VVRIDSPSKI
     VFRNDL
 
 
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