HMA3A_ARATH
ID HMA3A_ARATH Reviewed; 542 AA.
AC P0CW77; 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 71.
DE RecName: Full=Putative inactive cadmium/zinc-transporting ATPase HMA3;
DE AltName: Full=Putative inactive cadmium/zinc-transporting ATPase 4;
DE AltName: Full=Putative inactive protein HEAVY METAL ATPASE 3;
GN Name=HMA3; OrderedLocusNames=At4g30120; ORFNames=F6G3.150;
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], AND IDENTIFICATION OF FRAMESHIFT.
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 [2]
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 [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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. In strain cv. Columbia,
CC a naturally frameshift at position 543 results in a truncated HMA3
CC protein. Lacks the magnesium binding sites, suggesting that it has no
CC cadmium/zinc-transporting ATPase activity. A complete sequence for HMA3
CC can be found in strain cv. Wassilewskija (AC P0CW78). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43847.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81005.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY434730; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL078464; CAB43847.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161576; CAB81005.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85723.1; -; Genomic_DNA.
DR EMBL; DQ446885; ABE66104.1; -; mRNA.
DR PIR; A85352; A85352.
DR PIR; T08988; T08988.
DR RefSeq; NP_194741.2; NM_119158.4.
DR AlphaFoldDB; P0CW77; -.
DR SMR; P0CW77; -.
DR BioGRID; 14422; 2.
DR IntAct; P0CW77; 1.
DR STRING; 3702.AT4G30120.1; -.
DR PaxDb; P0CW77; -.
DR EnsemblPlants; AT4G30120.1; AT4G30120.1; AT4G30120.
DR GeneID; 829135; -.
DR Gramene; AT4G30120.1; AT4G30120.1; AT4G30120.
DR KEGG; ath:AT4G30120; -.
DR Araport; AT4G30120; -.
DR TAIR; locus:2126500; AT4G30120.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_6_1_1; -.
DR InParanoid; P0CW77; -.
DR OMA; TESQNIC; -.
DR OrthoDB; 649559at2759; -.
DR BioCyc; MetaCyc:MON-14750; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P0CW77; baseline and differential.
DR Genevisible; P0CW77; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter 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:InterPro.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071585; P:detoxification of cadmium ion; IMP:TAIR.
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; 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 SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 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 5: Uncertain;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..542
FT /note="Putative inactive cadmium/zinc-transporting ATPase
FT HMA3"
FT /id="PRO_0000046401"
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..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 13..79
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ SEQUENCE 542 AA; 58642 MW; D647B43C205E4059 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
LHKLLYWVSS IECKSSHPMA AALIDYARSV SVEPKPDIVE NFQNFPGEGV YGRIDGQDIY
IGNKRIAQRA GCLTDNVPDI EATMKRGKTI GYIYMGAKLT GSFNLLDGCR YGVAQALKEL
KS
