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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

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.Curated

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 intermediateBy similarity
Metal bindingi682 – 6821MagnesiumBy similarity
Metal bindingi686 – 6861MagnesiumBy similarity

GO - Molecular functioni

  1. ATPase activity Source: TAIR
  2. ATP binding Source: UniProtKB-KW
  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-exporting ATPase activity Source: UniProtKB-EC
  8. zinc transporting ATPase activity Source: TAIR

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 122105StromalSequence AnalysisAdd
BLAST
Transmembranei123 – 14422HelicalSequence AnalysisAdd
BLAST
Topological domaini145 – 1539LumenalSequence Analysis
Transmembranei154 – 17320HelicalSequence AnalysisAdd
BLAST
Topological domaini174 – 1807StromalSequence Analysis
Transmembranei181 – 20121HelicalSequence AnalysisAdd
BLAST
Topological domaini202 – 2021LumenalSequence Analysis
Transmembranei203 – 22321HelicalSequence AnalysisAdd
BLAST
Topological domaini224 – 361138StromalSequence AnalysisAdd
BLAST
Transmembranei362 – 38423HelicalSequence AnalysisAdd
BLAST
Topological domaini385 – 39814LumenalSequence AnalysisAdd
BLAST
Transmembranei399 – 41618HelicalSequence AnalysisAdd
BLAST
Topological domaini417 – 737321StromalSequence AnalysisAdd
BLAST
Transmembranei738 – 75720HelicalSequence AnalysisAdd
BLAST
Topological domaini758 – 7625LumenalSequence Analysis
Transmembranei763 – 78119HelicalSequence AnalysisAdd
BLAST
Topological domaini782 – 81938StromalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Plastid inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717ChloroplastSequence AnalysisAdd
BLAST
Chaini18 – 819802Probable cadmium/zinc-transporting ATPase HMA1, chloroplasticPRO_0000046398Add
BLAST

Proteomic databases

PaxDbiQ9M3H5.
PRIDEiQ9M3H5.

Expressioni

Gene expression databases

ExpressionAtlasiQ9M3H5. baseline and differential.
GenevestigatoriQ9M3H5.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G37270.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9M3H5.
SMRiQ9M3H5. Positions 153-785.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi79 – 8911Poly-HisAdd
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

        10         20         30         40         50
MEPATLTRSS SLTRFPYRRG LSTLRLARVN SFSILPPKTL LRQKPLRISA
60 70 80 90 100
SLNLPPRSIR LRAVEDHHHD HHHDDEQDHH NHHHHHHQHG CCSVELKAES
110 120 130 140 150
KPQKMLFGFA KAIGWVRLAN YLREHLHLCC SAAAMFLAAA VCPYLAPEPY
160 170 180 190 200
IKSLQNAFMI VGFPLVGVSA SLDALMDIAG GKVNIHVLMA LAAFASVFMG
210 220 230 240 250
NALEGGLLLA MFNLAHIAEE FFTSRSMVDV KELKESNPDS ALLIEVHNGN
260 270 280 290 300
VPNISDLSYK SVPVHSVEVG SYVLVGTGEI VPVDCEVYQG SATITIEHLT
310 320 330 340 350
GEVKPLEAKA GDRVPGGARN LDGRMIVKAT KAWNDSTLNK IVQLTEEAHS
360 370 380 390 400
NKPKLQRWLD EFGENYSKVV VVLSLAIAFL GPFLFKWPFL STAACRGSVY
410 420 430 440 450
RALGLMVAAS PCALAVAPLA YATAISSCAR KGILLKGAQV LDALASCHTI
460 470 480 490 500
AFDKTGTLTT GGLTCKAIEP IYGHQGGTNS SVITCCIPNC EKEALAVAAA
510 520 530 540 550
MEKGTTHPIG RAVVDHSVGK DLPSIFVESF EYFPGRGLTA TVNGVKTVAE
560 570 580 590 600
ESRLRKASLG SIEFITSLFK SEDESKQIKD AVNASSYGKD FVHAALSVDQ
610 620 630 640 650
KVTLIHLEDQ PRPGVSGVIA ELKSWARLRV MMLTGDHDSS AWRVANAVGI
660 670 680 690 700
TEVYCNLKPE DKLNHVKNIA REAGGGLIMV GEGINDAPAL AAATVGIVLA
710 720 730 740 750
QRASATAIAV ADILLLRDNI TGVPFCVAKS RQTTSLVKQN VALALTSIFL
760 770 780 790 800
AALPSVLGFV PLWLTVLLHE GGTLLVCLNS VRGLNDPSWS WKQDIVHLIN
810
KLRSQEPTSS SSNSLSSAH
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 153-785.
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

ExpressionAtlasi Q9M3H5. baseline and differential.
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: November 26, 2014
This is version 128 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