HMA3B_ARATH
ID HMA3B_ARATH Reviewed; 760 AA.
AC P0CW78; Q1PE33; Q8LPW0; Q9LCZ8; Q9SZW5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Cadmium/zinc-transporting ATPase HMA3;
DE EC=7.2.2.12;
DE EC=7.2.2.21;
DE AltName: Full=Cadmium/zinc-transporting ATPase 4;
DE AltName: Full=Protein HEAVY METAL ATPASE 3;
GN Name=HMA3;
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], MUTAGENESIS OF ASP-397, FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Wassilewskija; TISSUE=Leaf;
RX PubMed=15013746; DOI=10.1016/s0014-5793(04)00072-9;
RA Gravot A., Lieutaud A., Verret F., Auroy P., Vavasseur A., Richaud P.;
RT "AtHMA3, a plant P(1B)-ATPase, functions as a Cd/Pb transporter in yeast.";
RL FEBS Lett. 561:22-28(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wassilewskija;
RX PubMed=15100400; DOI=10.1105/tpc.020487;
RA Hussain D., Haydon M.J., Wang Y., Wong E., Sherson S.M., Young J.,
RA Camakaris J., Harper J.F., Cobbett C.S.;
RT "P-type ATPase heavy metal transporters with roles in essential zinc
RT homeostasis in Arabidopsis.";
RL Plant Cell 16:1327-1339(2004).
CC -!- FUNCTION: In a heterologous system, involved in cadmium and lead
CC transport, but not in zinc transport. May have a detoxification
CC function through a vacuolar sequestration.
CC {ECO:0000269|PubMed:15013746}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.21;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15013746};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15013746}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:15013746}.
CC -!- INDUCTION: Not induced by cadmium or zinc treatments.
CC {ECO:0000269|PubMed:15013746}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- CAUTION: In cv. Columbia (AC P0CW77), a naturally occurring frameshift
CC at position 543 results in a shortened C-terminus. The sequence shown
CC is from strain cv. Wassilewskija. {ECO:0000305}.
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DR EMBL; AY055217; AAL16382.1; -; mRNA.
DR EMBL; AY434729; AAR10768.1; -; mRNA.
DR PIR; A85352; A85352.
DR PIR; T08988; T08988.
DR AlphaFoldDB; P0CW78; -.
DR SMR; P0CW78; -.
DR TCDB; 3.A.3.6.20; the p-type atpase (p-atpase) superfamily.
DR PRIDE; P0CW78; -.
DR BRENDA; 7.2.2.21; 399.
DR ExpressionAtlas; P0CW78; baseline and differential.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0016463; F:P-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0071585; P:detoxification of cadmium ion; IMP:CACAO.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cadmium; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW Vacuole; Zinc.
FT CHAIN 1..760
FT /note="Cadmium/zinc-transporting ATPase HMA3"
FT /id="PRO_0000408534"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..678
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 13..79
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 739..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 603
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 397
FT /note="D->A: Loss of metal transport."
FT /evidence="ECO:0000269|PubMed:15013746"
SQ SEQUENCE 760 AA; 81856 MW; A8044EDA786FBA71 CRC64;
MAEGEESKKM NLQTSYFDVV GICCSSEVSI VGNVLRQVDG VKEFSVIVPS RTVIVVHDTF
LISPLQIVKA LNQARLEASV RPYGETSLKS QWPSPFAIVS GVLLVLSFFK YFYSPLEWLA
IVAVVAGVFP ILAKAVASVT RFRLDINALT LIAVIATLCM QDFTEAATIV FLFSVADWLE
SSAAHKASIV MSSLMSLAPR KAVIADTGLE VDVDEVGINT VVSVKAGESI PIDGVVVDGS
CDVDEKTLTG ESFPVSKQRE STVMAATINL NGYIKVKTTA LARDCVVAKM TKLVEEAQKS
QTKTQRFIDK CSRYYTPAVV VSAACFAVIP VLLKVQDLSH WFHLALVVLV SGCPCGLILS
TPVATFCALT KAATSGFLIK TGDCLETLAK IKIVAFDKTG TITKAEFMVS DFRSLSPSIN
LHKLLNWVSS IECKSSHPMA AALIDYAISV SVEPKPDIVE NFQNFPGEGV YGRIDGQDIY
IGNKRIAQRA GCLTDNVPDI EATMKRGKTI GYIYMGAKLT GSFNLLDGCR YGVAQALKEL
KSLGIQTAML TGDNQDAAMS TQEQLENALD IVHSELLPQD KARIIDDFKI QGPTMMVGDG
LNDAPALAKA DIGISMGISG SALATETGDI ILMSNDIRKI PKGMRLAKRS HKKVIENVVL
SVSIKGAIMV LGFVGYPLVW AAVLADAGTC LLVILNSMIL LRDEREAVST CYRSSTSSPV
KLEEDEVEDL EVGLLQKSEE TSKKSCCSGC CSGPKDNQQK
