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Protein

Calcium-transporting ATPase 2, plasma membrane-type

Gene

ACA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the endoplasmic reticulum.

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Enzyme regulationi

Activated by calmodulin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei454 – 45414-aspartylphosphate intermediateBy similarity
Metal bindingi755 – 7551MagnesiumBy similarity
Metal bindingi759 – 7591MagnesiumBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion transmembrane transporter activity Source: TAIR
  • calcium-transporting ATPase activity Source: TAIR
  • calmodulin binding Source: TAIR
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • transport Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G37640-MONOMER.
MetaCyc:MONOMER-14659.
ReactomeiR-ATH-418359. Reduction of cytosolic Ca++ levels.
R-ATH-5578775. Ion homeostasis.
R-ATH-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.2.12. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-transporting ATPase 2, plasma membrane-type (EC:3.6.3.8)
Alternative name(s):
Ca(2+)-ATPase isoform 2
Gene namesi
Name:ACA2
Ordered Locus Names:At4g37640
ORF Names:F19F18.130
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G37640.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 160160CytoplasmicSequence analysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence analysisAdd
BLAST
Topological domaini182 – 19918LumenalSequence analysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence analysisAdd
BLAST
Topological domaini221 – 348128CytoplasmicSequence analysisAdd
BLAST
Transmembranei349 – 36820HelicalSequence analysisAdd
BLAST
Topological domaini369 – 39830LumenalSequence analysisAdd
BLAST
Transmembranei399 – 41618HelicalSequence analysisAdd
BLAST
Topological domaini417 – 810394CytoplasmicSequence analysisAdd
BLAST
Transmembranei811 – 82919HelicalSequence analysisAdd
BLAST
Topological domaini830 – 84011LumenalSequence analysisAdd
BLAST
Transmembranei841 – 86121HelicalSequence analysisAdd
BLAST
Topological domaini862 – 88120CytoplasmicSequence analysisAdd
BLAST
Transmembranei882 – 90423HelicalSequence analysisAdd
BLAST
Topological domaini905 – 91612LumenalSequence analysisAdd
BLAST
Transmembranei917 – 93822HelicalSequence analysisAdd
BLAST
Topological domaini939 – 95618CytoplasmicSequence analysisAdd
BLAST
Transmembranei957 – 97822HelicalSequence analysisAdd
BLAST
Topological domaini979 – 98810LumenalSequence analysis
Transmembranei989 – 101022HelicalSequence analysisAdd
BLAST
Topological domaini1011 – 10144CytoplasmicSequence analysis

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • endoplasmic reticulum membrane Source: TAIR
  • integral component of plasma membrane Source: GO_Central
  • membrane Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10141014Calcium-transporting ATPase 2, plasma membrane-typePRO_0000046411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei45 – 451Phosphoserine; by CPK11 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO81108.
PRIDEiO81108.

PTM databases

iPTMnetiO81108.

Expressioni

Gene expression databases

ExpressionAtlasiO81108. baseline and differential.
GenevisibleiO81108. AT.

Interactioni

GO - Molecular functioni

  • calmodulin binding Source: TAIR

Protein-protein interaction databases

BioGridi15199. 6 interactions.
MINTiMINT-8066261.
STRINGi3702.AT4G37640.1.

Structurei

Secondary structure

1
1014
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3110Combined sources
Turni34 – 363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M7ENMR-A20-45[»]
ProteinModelPortaliO81108.
SMRiO81108. Positions 20-45, 129-930.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 3112Interaction with calmodulinAdd
BLAST

Domaini

The N-terminus contains an autoinhibitory calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0204. Eukaryota.
ENOG410XNNC. LUCA.
HOGENOMiHOG000265623.
InParanoidiO81108.
KOiK01537.
OMAiPETEREH.
PhylomeDBiO81108.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
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.
IPR024750. Ca_ATPase_N_dom.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF12515. CaATP_NAI. 1 hit.
PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O81108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESYLNENFD VKAKHSSEEV LEKWRNLCGV VKNPKRRFRF TANLSKRYEA
60 70 80 90 100
AAMRRTNQEK LRIAVLVSKA AFQFISGVSP SDYTVPEDVK AAGFEICADE
110 120 130 140 150
LGSIVESHDV KKLKFHGGVD GLAGKLKASP TDGLSTEAAQ LSQRQELFGI
160 170 180 190 200
NKFAESEMRG FWVFVWEALQ DMTLMILGVC AFVSLIVGIA TEGWPKGSHD
210 220 230 240 250
GLGIAASILL VVFVTATSDY RQSLQFRDLD KEKKKITVQV TRNGFRQKLS
260 270 280 290 300
IYDLLPGDIV HLAIGDQVPA DGLFLSGFSV VIDESSLTGE SEPVMVNAQN
310 320 330 340 350
PFLMSGTKVQ DGSCKMMITT VGMRTQWGKL MATLTEGGDD ETPLQVKLNG
360 370 380 390 400
VATIIGKIGL FFAVVTFAVL VQGMFMRKLS TGTHWVWSGD EALELLEYFA
410 420 430 440 450
IAVTIVVVAV PEGLPLAVTL SLAFAMKKMM NDKALVRHLA ACETMGSATT
460 470 480 490 500
ICSDKTGTLT TNHMTVVKSC ICMNVQDVAN KGSSLQSEIP ESAVKLLIQS
510 520 530 540 550
IFNNTGGEVV VNKHGKTELL GTPTETAILE LGLSLGGKFQ EERKSYKVIK
560 570 580 590 600
VEPFNSTKKR MGVVIELPEG GRMRAHTKGA SEIVLAACDK VVNSSGEVVP
610 620 630 640 650
LDEESIKYLN VTINEFANEA LRTLCLAYMD IEGGFSPDDA IPASGFTCVG
660 670 680 690 700
IVGIKDPVRP GVKESVELCR RAGITVRMVT GDNINTAKAI ARECGILTDD
710 720 730 740 750
GIAIEGPVFR EKNQEELLEL IPKIQVMARS SPMDKHTLVK QLRTTFDEVV
760 770 780 790 800
AVTGDGTNDA PALHEADIGL AMGIAGTEVA KESADVIILD DNFSTIVTVA
810 820 830 840 850
KWGRSVYINI QKFVQFQLTV NVVALVVNFS SACLTGSAPL TAVQLLWVNM
860 870 880 890 900
IMDTLGALAL ATEPPNDELM KRLPVGRRGN FITNAMWRNI LGQAVYQFIV
910 920 930 940 950
IWILQAKGKA MFGLDGPDST LMLNTLIFNC FVFCQVFNEI SSREMEEIDV
960 970 980 990 1000
FKGILDNYVF VVVIGATVFF QIIIIEFLGT FASTTPLTIT QWIFSIFIGF
1010
LGMPIAAGLK TIPV
Length:1,014
Mass (Da):110,439
Last modified:November 1, 1998 - v1
Checksum:i996DEFD26AFE9F03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025842 mRNA. Translation: AAC26997.1.
AL035605 Genomic DNA. Translation: CAB38303.1.
AL161591 Genomic DNA. Translation: CAB80429.1.
CP002687 Genomic DNA. Translation: AEE86819.1.
AY062484 mRNA. Translation: AAL32562.1.
PIRiT04721.
RefSeqiNP_195479.1. NM_119927.2.
UniGeneiAt.24252.

Genome annotation databases

EnsemblPlantsiAT4G37640.1; AT4G37640.1; AT4G37640.
GeneIDi829918.
GrameneiAT4G37640.1; AT4G37640.1; AT4G37640.
KEGGiath:AT4G37640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025842 mRNA. Translation: AAC26997.1.
AL035605 Genomic DNA. Translation: CAB38303.1.
AL161591 Genomic DNA. Translation: CAB80429.1.
CP002687 Genomic DNA. Translation: AEE86819.1.
AY062484 mRNA. Translation: AAL32562.1.
PIRiT04721.
RefSeqiNP_195479.1. NM_119927.2.
UniGeneiAt.24252.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M7ENMR-A20-45[»]
ProteinModelPortaliO81108.
SMRiO81108. Positions 20-45, 129-930.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15199. 6 interactions.
MINTiMINT-8066261.
STRINGi3702.AT4G37640.1.

Protein family/group databases

TCDBi3.A.3.2.12. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiO81108.

Proteomic databases

PaxDbiO81108.
PRIDEiO81108.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G37640.1; AT4G37640.1; AT4G37640.
GeneIDi829918.
GrameneiAT4G37640.1; AT4G37640.1; AT4G37640.
KEGGiath:AT4G37640.

Organism-specific databases

TAIRiAT4G37640.

Phylogenomic databases

eggNOGiKOG0204. Eukaryota.
ENOG410XNNC. LUCA.
HOGENOMiHOG000265623.
InParanoidiO81108.
KOiK01537.
OMAiPETEREH.
PhylomeDBiO81108.

Enzyme and pathway databases

BioCyciARA:AT4G37640-MONOMER.
MetaCyc:MONOMER-14659.
ReactomeiR-ATH-418359. Reduction of cytosolic Ca++ levels.
R-ATH-5578775. Ion homeostasis.
R-ATH-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiO81108.

Gene expression databases

ExpressionAtlasiO81108. baseline and differential.
GenevisibleiO81108. AT.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
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.
IPR024750. Ca_ATPase_N_dom.
IPR023214. HAD-like_dom.
IPR006408. P-type_ATPase_IIB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF12515. CaATP_NAI. 1 hit.
PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel calmodulin-regulated Ca2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain."
    Harper J.F., Hong B., Hwang I., Guo H.Q., Stoddard R., Huang J.F., Palmgren M.G., Sze H.
    J. Biol. Chem. 273:1099-1106(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CALMODULIN-BINDING DOMAIN.
    Strain: cv. Columbia.
  2. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "A calcium-dependent protein kinase can inhibit a calmodulin-stimulated Ca2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis."
    Hwang I., Sze H., Harper J.F.
    Proc. Natl. Acad. Sci. U.S.A. 97:6224-6229(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-45 BY CPK1.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACA2_ARATH
AccessioniPrimary (citable) accession number: O81108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.