MHX_ARAHH
ID MHX_ARAHH Reviewed; 539 AA.
AC B8K1V7;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Magnesium/proton exchanger;
DE AltName: Full=Mg(2+)/H(+) exchanger;
DE Short=AhMHX;
DE AltName: Full=Zinc/proton exchanger;
DE AltName: Full=Zn(2+)/H(+) exchanger;
GN Name=MHX;
OS Arabidopsis halleri subsp. halleri (Arabis halleri).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81971;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
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).
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 play a role in Zn(2+) accumulation
CC or tolerance. {ECO:0000269|PubMed:17080942}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High expression in leaves (at protein level).
CC {ECO:0000269|PubMed:17080942}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. MHX subfamily. {ECO:0000305}.
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DR EMBL; DQ118861; AAZ68034.1; -; mRNA.
DR AlphaFoldDB; B8K1V7; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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 1: Evidence at protein level;
KW Ion transport; Membrane; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..539
FT /note="Magnesium/proton exchanger"
FT /id="PRO_0000416776"
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; 59749 MW; 3F08C0B2368FBB92 CRC64;
MASILNQTQE LQEASKVLGH VRCENFFIFP GENTLSDGLR GVLYFLGLAY CFIGLSAITA
RFFKSMENVV KHSRKVVAID PITKAEIITY KKVWNFTIAD ISLLAFGTSF PQISLATIDA
IRNIGERYAG GLGPGTLVGS AAFDLFPIHA VCVVVPKAGE LKKISDLGVW LVELVWSFWA
YIWLYIILEV WSPNVITLVE ALLTVLQYGL LLVHAYAQDK RWPYLSLPMS RGDRPEEWVP
EEIDTSKDDN DNDVHDVYSD AAQEAVESGS RNIVDIFSIH SANNDTGITY HTVADTPPDS
ATKKGKAKNS SVFDIWKHQF VDAITLETSE SKKVDSIYLR IANSFWQLLL APWKLLFAFV
PPCNIAHGWI AFIFSLLFIS GVAFVVTRFT DLISCVTGIN PYVIAFTALA SGTSWPDLVA
SKIAAERQLT ADSAIANITC SNSVNIYVGI GVPWLINTVY NYFAYREPLY IENAKGLSFS
LLIFFATSVG CIVVLVLRRL IIGAELGGPR LWAWLTSAYF MMLWVVFVVL SSLKVSGVI