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Q9M3H5 (HMA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic

EC=3.6.3.3
EC=3.6.3.5
Alternative name(s):
Protein HEAVY METAL ATPASE 1
Gene names
Name:HMA1
Ordered Locus Names:At4g37270
ORF Names:AP22.4, C7A10.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length819 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in cadmium/zinc transport Potential.

Catalytic activity

ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).

ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).

Subcellular location

Plastidchloroplast inner membrane; Multi-pass membrane protein Potential Ref.6.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Ontologies

Keywords
   Cellular componentChloroplast
Membrane
Plastid
Plastid inner membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
Transmembrane
Transmembrane helix
   LigandATP-binding
Cadmium
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from mutant phenotype PubMed 16282320. Source: GOC

cadmium ion transmembrane transport

Inferred from genetic interaction PubMed 18252706. Source: GOC

calcium ion transmembrane transport

Inferred from genetic interaction PubMed 18252706. Source: GOC

calcium ion transport

Inferred from genetic interaction PubMed 18252706. Source: TAIR

cellular copper ion homeostasis

Inferred from mutant phenotype PubMed 16282320. Source: TAIR

response to light intensity

Inferred from mutant phenotype PubMed 16282320. Source: TAIR

response to toxic substance

Inferred from genetic interaction PubMed 18252706. Source: TAIR

zinc ion homeostasis

Inferred from mutant phenotype PubMed 19207208. Source: TAIR

zinc ion transmembrane transport

Inferred from direct assay PubMed 19207208. Source: GOC

   Cellular_componentchloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

chloroplast envelope

Inferred from direct assay Ref.6PubMed 16282320PubMed 19207208PubMed 20061580. Source: TAIR

chloroplast inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plastid

Inferred from direct assay PubMed 22923678. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from mutant phenotype PubMed 16282320. Source: TAIR

cadmium-exporting ATPase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cadmium-transporting ATPase activity

Inferred from genetic interaction PubMed 18252706. Source: TAIR

calcium-transporting ATPase activity

Inferred from genetic interaction PubMed 18252706. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc transporting ATPase activity

Inferred from direct assay PubMed 19207208. Source: TAIR

zinc-exporting ATPase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1717Chloroplast Potential
Chain18 – 819802Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic
PRO_0000046398

Regions

Topological domain18 – 122105Stromal Potential
Transmembrane123 – 14422Helical; Potential
Topological domain145 – 1539Lumenal Potential
Transmembrane154 – 17320Helical; Potential
Topological domain174 – 1807Stromal Potential
Transmembrane181 – 20121Helical; Potential
Topological domain2021Lumenal Potential
Transmembrane203 – 22321Helical; Potential
Topological domain224 – 361138Stromal Potential
Transmembrane362 – 38423Helical; Potential
Topological domain385 – 39814Lumenal Potential
Transmembrane399 – 41618Helical; Potential
Topological domain417 – 737321Stromal Potential
Transmembrane738 – 75720Helical; Potential
Topological domain758 – 7625Lumenal Potential
Transmembrane763 – 78119Helical; Potential
Topological domain782 – 81938Stromal Potential
Compositional bias79 – 8911Poly-His
Compositional bias809 – 8179Poly-Ser

Sites

Active site45314-aspartylphosphate intermediate By similarity
Metal binding6821Magnesium By similarity
Metal binding6861Magnesium By similarity

Natural variations

Natural variant531N → S in strain: cv. Landsberg erecta.
Natural variant1051M → V in strain: cv. Landsberg erecta.
Natural variant6591P → S in strain: cv. Landsberg erecta.

Sequences

Sequence LengthMass (Da)Tools
Q9M3H5 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: F281EA8F33C0ED52

FASTA81988,189
        10         20         30         40         50         60 
MEPATLTRSS SLTRFPYRRG LSTLRLARVN SFSILPPKTL LRQKPLRISA SLNLPPRSIR 

        70         80         90        100        110        120 
LRAVEDHHHD HHHDDEQDHH NHHHHHHQHG CCSVELKAES KPQKMLFGFA KAIGWVRLAN 

       130        140        150        160        170        180 
YLREHLHLCC SAAAMFLAAA VCPYLAPEPY IKSLQNAFMI VGFPLVGVSA SLDALMDIAG 

       190        200        210        220        230        240 
GKVNIHVLMA LAAFASVFMG NALEGGLLLA MFNLAHIAEE FFTSRSMVDV KELKESNPDS 

       250        260        270        280        290        300 
ALLIEVHNGN VPNISDLSYK SVPVHSVEVG SYVLVGTGEI VPVDCEVYQG SATITIEHLT 

       310        320        330        340        350        360 
GEVKPLEAKA GDRVPGGARN LDGRMIVKAT KAWNDSTLNK IVQLTEEAHS NKPKLQRWLD 

       370        380        390        400        410        420 
EFGENYSKVV VVLSLAIAFL GPFLFKWPFL STAACRGSVY RALGLMVAAS PCALAVAPLA 

       430        440        450        460        470        480 
YATAISSCAR KGILLKGAQV LDALASCHTI AFDKTGTLTT GGLTCKAIEP IYGHQGGTNS 

       490        500        510        520        530        540 
SVITCCIPNC EKEALAVAAA MEKGTTHPIG RAVVDHSVGK DLPSIFVESF EYFPGRGLTA 

       550        560        570        580        590        600 
TVNGVKTVAE ESRLRKASLG SIEFITSLFK SEDESKQIKD AVNASSYGKD FVHAALSVDQ 

       610        620        630        640        650        660 
KVTLIHLEDQ PRPGVSGVIA ELKSWARLRV MMLTGDHDSS AWRVANAVGI TEVYCNLKPE 

       670        680        690        700        710        720 
DKLNHVKNIA REAGGGLIMV GEGINDAPAL AAATVGIVLA QRASATAIAV ADILLLRDNI 

       730        740        750        760        770        780 
TGVPFCVAKS RQTTSLVKQN VALALTSIFL AALPSVLGFV PLWLTVLLHE GGTLLVCLNS 

       790        800        810 
VRGLNDPSWS WKQDIVHLIN KLRSQEPTSS SSNSLSSAH 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a putative heavy metal P-type ATPase in Arabidopsis."
Page S.L., Pittman J.K., Krijger G.C., Williams L.E.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Landsberg erecta.
[2]"Functional characterization of AtHMA1."
Mills R.F., Williams L.E.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
Tissue: Leaf and Root.
[3]"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. expand/collapse author list , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Wassilewskija.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ400906 mRNA. Translation: CAB90352.1.
AJ872069 mRNA. Translation: CAI43274.1.
Z99707 Genomic DNA. Translation: CAB16773.1.
AL161591 Genomic DNA. Translation: CAB80393.1.
CP002687 Genomic DNA. Translation: AEE86775.1.
PIRD85440.
RefSeqNP_195444.1. NM_119890.6.
UniGeneAt.56989.
At.74483.

3D structure databases

ProteinModelPortalQ9M3H5.
SMRQ9M3H5. Positions 143-792.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G37270.1-P.

Protein family/group databases

TCDB3.A.3.6.6. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbQ9M3H5.
PRIDEQ9M3H5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G37270.1; AT4G37270.1; AT4G37270.
GeneID829881.
KEGGath:AT4G37270.

Organism-specific databases

TAIRAT4G37270.

Phylogenomic databases

eggNOGCOG2217.
HOGENOMHOG000250399.
InParanoidQ9M3H5.
OMALYVKVVL.
PhylomeDBQ9M3H5.
ProtClustDBCLSN2685780.

Enzyme and pathway databases

BioCycARA:AT4G37270-MONOMER.

Gene expression databases

GenevestigatorQ9M3H5.

Family and domain databases

Gene3D1.20.1110.10. 1 hit.
2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 1 hit.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMA1_ARATH
AccessionPrimary (citable) accession number: Q9M3H5
Secondary accession number(s): Q5JZZ1, Q9SW66
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names