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Q9M3H5

- HMA1_ARATH

UniProt

Q9M3H5 - HMA1_ARATH

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Protein
Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic
Gene
HMA1, At4g37270, AP22.4, C7A10.90
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Involved in cadmium/zinc transport Reviewed prediction.

Catalytic activityi

ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).
ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei453 – 45314-aspartylphosphate intermediate By similarity
Metal bindingi682 – 6821Magnesium By similarity
Metal bindingi686 – 6861Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: TAIR
  3. cadmium-exporting ATPase activity Source: UniProtKB-EC
  4. cadmium-transporting ATPase activity Source: TAIR
  5. calcium-transporting ATPase activity Source: TAIR
  6. metal ion binding Source: UniProtKB-KW
  7. zinc transporting ATPase activity Source: TAIR
  8. zinc-exporting ATPase activity Source: UniProtKB-EC

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cadmium ion transmembrane transport Source: GOC
  3. calcium ion transmembrane transport Source: GOC
  4. calcium ion transport Source: TAIR
  5. cellular copper ion homeostasis Source: TAIR
  6. response to light intensity Source: TAIR
  7. response to toxic substance Source: TAIR
  8. zinc ion homeostasis Source: TAIR
  9. zinc ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Cadmium, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G37270-MONOMER.

Protein family/group databases

TCDBi3.A.3.6.6. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HMA1
Ordered Locus Names:At4g37270
ORF Names:AP22.4, C7A10.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G37270.

Subcellular locationi

Plastidchloroplast inner membrane; Multi-pass membrane protein Reviewed prediction 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 122105Stromal Reviewed prediction
Add
BLAST
Transmembranei123 – 14422Helical; Reviewed prediction
Add
BLAST
Topological domaini145 – 1539Lumenal Reviewed prediction
Transmembranei154 – 17320Helical; Reviewed prediction
Add
BLAST
Topological domaini174 – 1807Stromal Reviewed prediction
Transmembranei181 – 20121Helical; Reviewed prediction
Add
BLAST
Topological domaini202 – 2021Lumenal Reviewed prediction
Transmembranei203 – 22321Helical; Reviewed prediction
Add
BLAST
Topological domaini224 – 361138Stromal Reviewed prediction
Add
BLAST
Transmembranei362 – 38423Helical; Reviewed prediction
Add
BLAST
Topological domaini385 – 39814Lumenal Reviewed prediction
Add
BLAST
Transmembranei399 – 41618Helical; Reviewed prediction
Add
BLAST
Topological domaini417 – 737321Stromal Reviewed prediction
Add
BLAST
Transmembranei738 – 75720Helical; Reviewed prediction
Add
BLAST
Topological domaini758 – 7625Lumenal Reviewed prediction
Transmembranei763 – 78119Helical; Reviewed prediction
Add
BLAST
Topological domaini782 – 81938Stromal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast envelope Source: TAIR
  3. chloroplast inner membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Plastid inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717Chloroplast Reviewed prediction
Add
BLAST
Chaini18 – 819802Probable cadmium/zinc-transporting ATPase HMA1, chloroplastic
PRO_0000046398Add
BLAST

Proteomic databases

PaxDbiQ9M3H5.
PRIDEiQ9M3H5.

Expressioni

Gene expression databases

GenevestigatoriQ9M3H5.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G37270.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9M3H5.
SMRiQ9M3H5. Positions 126-786.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi79 – 8911Poly-His
Add
BLAST
Compositional biasi809 – 8179Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2217.
HOGENOMiHOG000250399.
InParanoidiQ9M3H5.
OMAiAWIRLTD.
PhylomeDBiQ9M3H5.

Family and domain databases

Gene3Di1.20.1110.10. 1 hit.
2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR023299. 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]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 3 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9M3H5-1 [UniParc]FASTAAdd to Basket

« Hide

MEPATLTRSS SLTRFPYRRG LSTLRLARVN SFSILPPKTL LRQKPLRISA    50
SLNLPPRSIR LRAVEDHHHD HHHDDEQDHH NHHHHHHQHG CCSVELKAES 100
KPQKMLFGFA KAIGWVRLAN YLREHLHLCC SAAAMFLAAA VCPYLAPEPY 150
IKSLQNAFMI VGFPLVGVSA SLDALMDIAG GKVNIHVLMA LAAFASVFMG 200
NALEGGLLLA MFNLAHIAEE FFTSRSMVDV KELKESNPDS ALLIEVHNGN 250
VPNISDLSYK SVPVHSVEVG SYVLVGTGEI VPVDCEVYQG SATITIEHLT 300
GEVKPLEAKA GDRVPGGARN LDGRMIVKAT KAWNDSTLNK IVQLTEEAHS 350
NKPKLQRWLD EFGENYSKVV VVLSLAIAFL GPFLFKWPFL STAACRGSVY 400
RALGLMVAAS PCALAVAPLA YATAISSCAR KGILLKGAQV LDALASCHTI 450
AFDKTGTLTT GGLTCKAIEP IYGHQGGTNS SVITCCIPNC EKEALAVAAA 500
MEKGTTHPIG RAVVDHSVGK DLPSIFVESF EYFPGRGLTA TVNGVKTVAE 550
ESRLRKASLG SIEFITSLFK SEDESKQIKD AVNASSYGKD FVHAALSVDQ 600
KVTLIHLEDQ PRPGVSGVIA ELKSWARLRV MMLTGDHDSS AWRVANAVGI 650
TEVYCNLKPE DKLNHVKNIA REAGGGLIMV GEGINDAPAL AAATVGIVLA 700
QRASATAIAV ADILLLRDNI TGVPFCVAKS RQTTSLVKQN VALALTSIFL 750
AALPSVLGFV PLWLTVLLHE GGTLLVCLNS VRGLNDPSWS WKQDIVHLIN 800
KLRSQEPTSS SSNSLSSAH 819
Length:819
Mass (Da):88,189
Last modified:January 11, 2001 - v2
Checksum:iF281EA8F33C0ED52
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531N → S in strain: cv. Landsberg erecta.
Natural varianti105 – 1051M → V in strain: cv. Landsberg erecta.
Natural varianti659 – 6591P → S in strain: cv. Landsberg erecta.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiD85440.
RefSeqiNP_195444.1. NM_119890.6.
UniGeneiAt.56989.
At.74483.

Genome annotation databases

EnsemblPlantsiAT4G37270.1; AT4G37270.1; AT4G37270.
GeneIDi829881.
KEGGiath:AT4G37270.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi D85440.
RefSeqi NP_195444.1. NM_119890.6.
UniGenei At.56989.
At.74483.

3D structure databases

ProteinModelPortali Q9M3H5.
SMRi Q9M3H5. Positions 126-786.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G37270.1-P.

Protein family/group databases

TCDBi 3.A.3.6.6. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbi Q9M3H5.
PRIDEi Q9M3H5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G37270.1 ; AT4G37270.1 ; AT4G37270 .
GeneIDi 829881.
KEGGi ath:AT4G37270.

Organism-specific databases

TAIRi AT4G37270.

Phylogenomic databases

eggNOGi COG2217.
HOGENOMi HOG000250399.
InParanoidi Q9M3H5.
OMAi AWIRLTD.
PhylomeDBi Q9M3H5.

Enzyme and pathway databases

BioCyci ARA:AT4G37270-MONOMER.

Gene expression databases

Genevestigatori Q9M3H5.

Family and domain databases

Gene3Di 1.20.1110.10. 1 hit.
2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 1 hit.
InterProi IPR023299. 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 ]
Pfami PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SUPFAMi SSF56784. SSF56784. 3 hits.
TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiHMA1_ARATH
AccessioniPrimary (citable) accession number: Q9M3H5
Secondary accession number(s): Q5JZZ1, Q9SW66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: June 11, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi