MHX_ARATH
ID MHX_ARATH Reviewed; 539 AA.
AC O22252; Q9S7N1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Magnesium/proton exchanger;
DE AltName: Full=Mg(2+)/H(+) exchanger;
DE Short=AtMHX;
DE AltName: Full=Zinc/proton exchanger;
DE AltName: Full=Zn(2+)/H(+) exchanger;
GN Name=MHX; Synonyms=MHX1; OrderedLocusNames=At2g47600; ORFNames=T30B22.10;
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 / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=10406802; DOI=10.1093/emboj/18.14.3973;
RA Shaul O., Hilgemann D.W., de-Almeida-Engler J., Van Montagu M., Inz D.,
RA Galili G.;
RT "Cloning and characterization of a novel Mg(2+)/H(+) exchanger.";
RL EMBO J. 18:3973-3980(1999).
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.
RX PubMed=12206396; DOI=10.1023/a:1016091118585;
RA Shaul O.;
RT "Magnesium transport and function in plants: the tip of the iceberg.";
RL BioMetals 15:309-323(2002).
RN [6]
RP FUNCTION.
RX PubMed=17080942; DOI=10.1111/j.1365-3040.2006.01500.x;
RA Elbaz B., Shoshani-Knaani N., David-Assael O., Mizrachy-Dagri T.,
RA Mizrahi K., Saul H., Brook E., Berezin I., Shaul O.;
RT "High expression in leaves of the zinc hyperaccumulator Arabidopsis halleri
RT of AhMHX, a homolog of an Arabidopsis thaliana vacuolar metal/proton
RT exchanger.";
RL Plant Cell Environ. 29:1179-1190(2006).
RN [7]
RP FUNCTION.
RX PubMed=18327593; DOI=10.1007/s00299-007-0502-9;
RA Berezin I., Mizrachy-Dagry T., Brook E., Mizrahi K., Elazar M., Zhuo S.,
RA Saul-Tcherkas V., Shaul O.;
RT "Overexpression of AtMHX in tobacco causes increased sensitivity to Mg2+,
RT Zn2+, and Cd2+ ions, induction of V-ATPase expression, and a reduction in
RT plant size.";
RL Plant Cell Rep. 27:939-949(2008).
CC -!- FUNCTION: Vacuolar transporter that exchanges protons with Mg(2+),
CC Zn(2+) and Fe(2+) ions. May control the partitioning of Mg(2+) and
CC Zn(2+) between plant organs. Could also transport Cd(2+) in vitro.
CC {ECO:0000269|PubMed:10406802, ECO:0000269|PubMed:12206396,
CC ECO:0000269|PubMed:17080942, ECO:0000269|PubMed:18327593}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10406802};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10406802}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the vascular cylinder.
CC {ECO:0000269|PubMed:10406802}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. MHX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY080737; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF109178; AAF14229.1; -; mRNA.
DR EMBL; AF109182; AAF14230.1; -; Genomic_DNA.
DR EMBL; AC002535; AAC62871.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10863.1; -; Genomic_DNA.
DR EMBL; AY080737; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T00424; T00424.
DR RefSeq; NP_566105.1; NM_130328.3.
DR AlphaFoldDB; O22252; -.
DR BioGRID; 4708; 30.
DR IntAct; O22252; 25.
DR STRING; 3702.AT2G47600.1; -.
DR TCDB; 2.A.19.6.1; the ca(2+):cation antiporter (caca) family.
DR PaxDb; O22252; -.
DR PRIDE; O22252; -.
DR ProteomicsDB; 250848; -.
DR EnsemblPlants; AT2G47600.1; AT2G47600.1; AT2G47600.
DR GeneID; 819373; -.
DR Gramene; AT2G47600.1; AT2G47600.1; AT2G47600.
DR KEGG; ath:AT2G47600; -.
DR Araport; AT2G47600; -.
DR TAIR; locus:2061951; AT2G47600.
DR eggNOG; KOG1306; Eukaryota.
DR HOGENOM; CLU_012872_2_0_1; -.
DR InParanoid; O22252; -.
DR OMA; RLWAWIT; -.
DR OrthoDB; 490546at2759; -.
DR PhylomeDB; O22252; -.
DR PRO; PR:O22252; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22252; baseline and differential.
DR Genevisible; O22252; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015491; F:cation:cation antiporter activity; IBA:GO_Central.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR Pfam; PF01699; Na_Ca_ex; 2.
PE 2: Evidence at transcript level;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..539
FT /note="Magnesium/proton exchanger"
FT /id="PRO_0000416777"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 539 AA; 59792 MW; 71036ACE8AD920A9 CRC64;
MASILNQTQE LQESSKVLGH LRCENFFLFP GENTLSDGLR GVLYFLGLAY CFIGLSAITA
RFFKSMENVV KHSRKVVTID PITKAEVITY KKVWNFTIAD ISLLAFGTSF PQISLATIDA
IRNMGERYAG GLGPGTLVGS AAFDLFPIHA VCVVVPKAGE LKKISDLGVW LVELVWSFWA
YIWLYIILEV WSPNVITLVE ALLTVLQYGL LLVHAYAQDK RWPYLSLPMS RGDRPEEWVP
EEIDTSKDDN DNDVHDVYSD AAQDAVESGS RNIVDIFSIH SANNDTGITY HTVADTPPDS
ATKKGKAKNS TVFDIWKHQF VDAITLETSE SKKVDSIYLR IAKSFWHLLL APWKLLFAFV
PPCNIAHGWI AFICSLLFIS GVAFVVTRFT DLISCVTGIN PYVIAFTALA SGTSWPDLVA
SKIAAERQLT ADSAIANITC SNSVNIYVGI GVPWLINTVY NYFAYREPLY IENAKGLSFS
LLIFFATSVG CIVVLVLRRL IIGAELGGPR LWAWLTSAYF MMLWVVFVVL SSLKVSGVI
