HMA2_ARATH
ID HMA2_ARATH Reviewed; 951 AA.
AC Q9SZW4; Q8LPW1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cadmium/zinc-transporting ATPase HMA2;
DE EC=7.2.2.12;
DE EC=7.2.2.21;
DE AltName: Full=Cadmium/zinc-transporting ATPase 3;
DE AltName: Full=Protein HEAVY METAL ATPASE 2;
GN Name=HMA2; OrderedLocusNames=At4g30110; ORFNames=F6G3.140;
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. Wassilewskija; TISSUE=Leaf;
RA Richaud P.;
RT "AtHMA2, a putative heavy-metal P-type ATPase in Arabidopsis.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
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).
RN [3]
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 [4]
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: Plays an important role in zinc transport and homeostasis.
CC Could also be involved in cadmium detoxification.
CC {ECO:0000269|PubMed:15100400}.
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: Cell membrane {ECO:0000269|PubMed:15100400};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15100400}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the vascular tissues of
CC roots, stems, and leaves. Also detected in developing anthers.
CC {ECO:0000269|PubMed:15100400}.
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; AY054390; AAL14248.1; -; mRNA.
DR EMBL; AY434728; AAR10767.1; -; mRNA.
DR EMBL; AL078464; CAB43846.1; -; Genomic_DNA.
DR EMBL; AL161576; CAB81004.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85722.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67783.1; -; Genomic_DNA.
DR PIR; T08987; T08987.
DR RefSeq; NP_001320088.1; NM_001341993.1.
DR RefSeq; NP_194740.1; NM_119157.4.
DR AlphaFoldDB; Q9SZW4; -.
DR SMR; Q9SZW4; -.
DR BioGRID; 14421; 1.
DR STRING; 3702.AT4G30110.1; -.
DR TCDB; 3.A.3.6.7; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9SZW4; -.
DR PaxDb; Q9SZW4; -.
DR PRIDE; Q9SZW4; -.
DR ProteomicsDB; 230368; -.
DR EnsemblPlants; AT4G30110.1; AT4G30110.1; AT4G30110.
DR EnsemblPlants; AT4G30110.2; AT4G30110.2; AT4G30110.
DR GeneID; 829134; -.
DR Gramene; AT4G30110.1; AT4G30110.1; AT4G30110.
DR Gramene; AT4G30110.2; AT4G30110.2; AT4G30110.
DR KEGG; ath:AT4G30110; -.
DR Araport; AT4G30110; -.
DR TAIR; locus:2126490; AT4G30110.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_3_1_1; -.
DR InParanoid; Q9SZW4; -.
DR OMA; HEHSHCE; -.
DR OrthoDB; 649559at2759; -.
DR PhylomeDB; Q9SZW4; -.
DR BioCyc; ARA:AT4G30110-MON; -.
DR BRENDA; 7.2.2.12; 399.
DR PRO; PR:Q9SZW4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZW4; baseline and differential.
DR Genevisible; Q9SZW4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
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:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055069; P:zinc ion homeostasis; IGI: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; 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 2: Evidence at transcript level;
KW ATP-binding; Cadmium; Cell membrane; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..951
FT /note="Cadmium/zinc-transporting ATPase HMA2"
FT /id="PRO_0000046400"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..671
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 692..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 7..73
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 841..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 391
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 596
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT CONFLICT 459
FT /note="F -> L (in Ref. 1; AAR10767 and 2; AAL14248)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="A -> T (in Ref. 1; AAR10767 and 2; AAL14248)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="N -> K (in Ref. 1; AAR10767 and 2; AAL14248)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="S -> N (in Ref. 1; AAR10767 and 2; AAL14248)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="F -> C (in Ref. 1; AAR10767 and 2; AAL14248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 101990 MW; 82E51995034FCF9D CRC64;
MASKKMTKSY FDVLGICCTS EVPLIENILN SMDGVKEFSV IVPSRTVIVV HDTLILSQFQ
IVKALNQAQL EANVRVTGET NFKNKWPSPF AVVSGILLLL SFFKYLYSPF RWLAVAAVVA
GIYPILAKAV ASLARFRIDI NILVVVTVGA TIGMQDYTEA AVVVFLFTIA EWLQSRASYK
ASAVMQSLMS LAPQKAVIAE TGEEVEVDEL KTNTVIAVKA GETIPIDGVV VDGNCEVDEK
TLTGEAFPVP KLKDSTVWAG TINLNGYITV NTTALAEDCV VAKMAKLVEE AQNSKTETQR
FIDKCSKYYT PAIILISICF VAIPFALKVH NLKHWVHLAL VVLVSACPCG LILSTPVATF
CALTKAATSG LLIKGADYLE TLAKIKIVAF DKTGTITRGE FIVMDFQSLS EDISLQSLLY
WVSSTESKSS HPMAAAVVDY ARSVSVEPKP EAVEDYQNFP GEGIYGKIDG KEVYIGNKRI
ASRAGCLSVP DIDVDTKGGK TIGYVYVGET LAGVFNLSDA CRSGVAQAMK ELKSLGIKIA
MLTGDNHAAA MHAQEQLGNA MDIVRAELLP EDKSEIIKQL KREEGPTAMV GDGLNDAPAL
ATADIGISMG VSGSALATET GNIILMSNDI RRIPQAIKLA KRAKRKVVEN VVISITMKGA
ILALAFAGHP LIWAAVLADV GTCLLVILNS MLLLSDKHKT GNKCYRESSS SSVLIAEKLE
GDAAGDMEAG LLPKISDKHC KPGCCGTKTQ EKAMKPAKAS SDHSHSGCCE TKQKDNVTVV
KKSCCAEPVD LGHGHDSGCC GDKSQQPHQH EVQVQQSCHN KPSGLDSGCC GGKSQQPHQH
ELQQSCHDKP SGLDIGTGPK HEGSSTLVNL EGDAKEELKV LVNGFCSSPA DLAITSLKVK
SDSHCKSNCS SRERCHHGSN CCRSYAKESC SHDHHHTRAH GVGTLKEIVI E
