HMA1_ARATH
ID HMA1_ARATH Reviewed; 819 AA.
AC Q9M3H5; Q5JZZ1; Q9SW66;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic;
DE EC=7.2.2.12;
DE EC=7.2.2.21;
DE AltName: Full=Protein HEAVY METAL ATPASE 1;
DE Flags: Precursor;
GN Name=HMA1; OrderedLocusNames=At4g37270; ORFNames=AP22.4, C7A10.90;
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].
RC STRAIN=cv. Landsberg erecta;
RA Page S.L., Pittman J.K., Krijger G.C., Williams L.E.;
RT "Identification of a putative heavy metal P-type ATPase in Arabidopsis.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Root;
RA Mills R.F., Williams L.E.;
RT "Functional characterization of AtHMA1.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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).
CC -!- FUNCTION: Involved in cadmium/zinc transport. {ECO:0000305}.
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: Plastid, chloroplast inner membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AJ400906; CAB90352.1; -; mRNA.
DR EMBL; AJ872069; CAI43274.1; -; mRNA.
DR EMBL; Z99707; CAB16773.1; -; Genomic_DNA.
DR EMBL; AL161591; CAB80393.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86775.1; -; Genomic_DNA.
DR PIR; D85440; D85440.
DR RefSeq; NP_195444.1; NM_119890.7.
DR AlphaFoldDB; Q9M3H5; -.
DR SMR; Q9M3H5; -.
DR STRING; 3702.AT4G37270.1; -.
DR TCDB; 3.A.3.6.6; the p-type atpase (p-atpase) superfamily.
DR PaxDb; Q9M3H5; -.
DR PRIDE; Q9M3H5; -.
DR ProteomicsDB; 230358; -.
DR EnsemblPlants; AT4G37270.1; AT4G37270.1; AT4G37270.
DR GeneID; 829881; -.
DR Gramene; AT4G37270.1; AT4G37270.1; AT4G37270.
DR KEGG; ath:AT4G37270; -.
DR Araport; AT4G37270; -.
DR TAIR; locus:2115020; AT4G37270.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_6_3_1; -.
DR InParanoid; Q9M3H5; -.
DR OMA; SPTWSWV; -.
DR OrthoDB; 649559at2759; -.
DR PhylomeDB; Q9M3H5; -.
DR BioCyc; ARA:AT4G37270-MON; -.
DR PRO; PR:Q9M3H5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M3H5; baseline and differential.
DR Genevisible; Q9M3H5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:TAIR.
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; IDA:TAIR.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:TAIR.
DR GO; GO:0009642; P:response to light intensity; IMP:TAIR.
DR GO; GO:0055069; P:zinc ion homeostasis; IMP:TAIR.
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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR SFLD; SFLDF00027; p-type_atpase; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cadmium; Chloroplast; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Plastid inner membrane; Reference proteome;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..17
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 18..819
FT /note="Probable cadmium/zinc-transporting ATPase HMA1,
FT chloroplastic"
FT /id="PRO_0000046398"
FT TOPO_DOM 18..122
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..153
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..180
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..361
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..737
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..762
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 782..819
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 66..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 686
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VARIANT 53
FT /note="N -> S (in strain: cv. Landsberg erecta)"
FT VARIANT 105
FT /note="M -> V (in strain: cv. Landsberg erecta)"
FT VARIANT 659
FT /note="P -> S (in strain: cv. Landsberg erecta)"
SQ SEQUENCE 819 AA; 88189 MW; F281EA8F33C0ED52 CRC64;
MEPATLTRSS SLTRFPYRRG LSTLRLARVN SFSILPPKTL LRQKPLRISA SLNLPPRSIR
LRAVEDHHHD HHHDDEQDHH NHHHHHHQHG CCSVELKAES KPQKMLFGFA KAIGWVRLAN
YLREHLHLCC SAAAMFLAAA VCPYLAPEPY IKSLQNAFMI VGFPLVGVSA SLDALMDIAG
GKVNIHVLMA LAAFASVFMG NALEGGLLLA MFNLAHIAEE FFTSRSMVDV KELKESNPDS
ALLIEVHNGN VPNISDLSYK SVPVHSVEVG SYVLVGTGEI VPVDCEVYQG SATITIEHLT
GEVKPLEAKA GDRVPGGARN LDGRMIVKAT KAWNDSTLNK IVQLTEEAHS NKPKLQRWLD
EFGENYSKVV VVLSLAIAFL GPFLFKWPFL STAACRGSVY RALGLMVAAS PCALAVAPLA
YATAISSCAR KGILLKGAQV LDALASCHTI AFDKTGTLTT GGLTCKAIEP IYGHQGGTNS
SVITCCIPNC EKEALAVAAA MEKGTTHPIG RAVVDHSVGK DLPSIFVESF EYFPGRGLTA
TVNGVKTVAE ESRLRKASLG SIEFITSLFK SEDESKQIKD AVNASSYGKD FVHAALSVDQ
KVTLIHLEDQ PRPGVSGVIA ELKSWARLRV MMLTGDHDSS AWRVANAVGI TEVYCNLKPE
DKLNHVKNIA REAGGGLIMV GEGINDAPAL AAATVGIVLA QRASATAIAV ADILLLRDNI
TGVPFCVAKS RQTTSLVKQN VALALTSIFL AALPSVLGFV PLWLTVLLHE GGTLLVCLNS
VRGLNDPSWS WKQDIVHLIN KLRSQEPTSS SSNSLSSAH
