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O81108 (ACA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 124. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-transporting ATPase 2, plasma membrane-type
EC=3.6.3.8
Alternative name(s):
Ca(2+)-ATPase isoform 2
Gene names
Name:ACA2
Ordered Locus Names:At4g37640
ORF Names:F19F18.130
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length1014 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Activated by calmodulin.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Domain

The N-terminus contains an autoinhibitory calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion. Ref.1

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10141014Calcium-transporting ATPase 2, plasma membrane-type
PRO_0000046411

Regions

Topological domain1 – 160160Cytoplasmic Potential
Transmembrane161 – 18121Helical; Potential
Topological domain182 – 19918Lumenal Potential
Transmembrane200 – 22021Helical; Potential
Topological domain221 – 348128Cytoplasmic Potential
Transmembrane349 – 36820Helical; Potential
Topological domain369 – 39830Lumenal Potential
Transmembrane399 – 41618Helical; Potential
Topological domain417 – 810394Cytoplasmic Potential
Transmembrane811 – 82919Helical; Potential
Topological domain830 – 84011Lumenal Potential
Transmembrane841 – 86121Helical; Potential
Topological domain862 – 88120Cytoplasmic Potential
Transmembrane882 – 90423Helical; Potential
Topological domain905 – 91612Lumenal Potential
Transmembrane917 – 93822Helical; Potential
Topological domain939 – 95618Cytoplasmic Potential
Transmembrane957 – 97822Helical; Potential
Topological domain979 – 98810Lumenal Potential
Transmembrane989 – 101022Helical; Potential
Topological domain1011 – 10144Cytoplasmic Potential
Region20 – 3112Interaction with calmodulin

Sites

Active site45414-aspartylphosphate intermediate By similarity
Metal binding7551Magnesium By similarity
Metal binding7591Magnesium By similarity

Amino acid modifications

Modified residue451Phosphoserine; by CPK1 Ref.5

Sequences

Sequence LengthMass (Da)Tools
O81108 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 996DEFD26AFE9F03

FASTA1,014110,439
        10         20         30         40         50         60 
MESYLNENFD VKAKHSSEEV LEKWRNLCGV VKNPKRRFRF TANLSKRYEA AAMRRTNQEK 

        70         80         90        100        110        120 
LRIAVLVSKA AFQFISGVSP SDYTVPEDVK AAGFEICADE LGSIVESHDV KKLKFHGGVD 

       130        140        150        160        170        180 
GLAGKLKASP TDGLSTEAAQ LSQRQELFGI NKFAESEMRG FWVFVWEALQ DMTLMILGVC 

       190        200        210        220        230        240 
AFVSLIVGIA TEGWPKGSHD GLGIAASILL VVFVTATSDY RQSLQFRDLD KEKKKITVQV 

       250        260        270        280        290        300 
TRNGFRQKLS IYDLLPGDIV HLAIGDQVPA DGLFLSGFSV VIDESSLTGE SEPVMVNAQN 

       310        320        330        340        350        360 
PFLMSGTKVQ DGSCKMMITT VGMRTQWGKL MATLTEGGDD ETPLQVKLNG VATIIGKIGL 

       370        380        390        400        410        420 
FFAVVTFAVL VQGMFMRKLS TGTHWVWSGD EALELLEYFA IAVTIVVVAV PEGLPLAVTL 

       430        440        450        460        470        480 
SLAFAMKKMM NDKALVRHLA ACETMGSATT ICSDKTGTLT TNHMTVVKSC ICMNVQDVAN 

       490        500        510        520        530        540 
KGSSLQSEIP ESAVKLLIQS IFNNTGGEVV VNKHGKTELL GTPTETAILE LGLSLGGKFQ 

       550        560        570        580        590        600 
EERKSYKVIK VEPFNSTKKR MGVVIELPEG GRMRAHTKGA SEIVLAACDK VVNSSGEVVP 

       610        620        630        640        650        660 
LDEESIKYLN VTINEFANEA LRTLCLAYMD IEGGFSPDDA IPASGFTCVG IVGIKDPVRP 

       670        680        690        700        710        720 
GVKESVELCR RAGITVRMVT GDNINTAKAI ARECGILTDD GIAIEGPVFR EKNQEELLEL 

       730        740        750        760        770        780 
IPKIQVMARS SPMDKHTLVK QLRTTFDEVV AVTGDGTNDA PALHEADIGL AMGIAGTEVA 

       790        800        810        820        830        840 
KESADVIILD DNFSTIVTVA KWGRSVYINI QKFVQFQLTV NVVALVVNFS SACLTGSAPL 

       850        860        870        880        890        900 
TAVQLLWVNM IMDTLGALAL ATEPPNDELM KRLPVGRRGN FITNAMWRNI LGQAVYQFIV 

       910        920        930        940        950        960 
IWILQAKGKA MFGLDGPDST LMLNTLIFNC FVFCQVFNEI SSREMEEIDV FKGILDNYVF 

       970        980        990       1000       1010 
VVVIGATVFF QIIIIEFLGT FASTTPLTIT QWIFSIFIGF LGMPIAAGLK TIPV

« Hide

References

« Hide 'large scale' references
[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. 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.
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00544002.
PIRT04721.
RefSeqNP_195479.1. NM_119927.2.
UniGeneAt.24252.

3D structure databases

ProteinModelPortalO81108.
SMRO81108. Positions 16-76, 118-1012.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-8066261.

Protein family/group databases

TCDB3.A.3.2.12. P-type ATPase (P-ATPase) superfamily.

Proteomic databases

PaxDbO81108.
PRIDEO81108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G37640.1; AT4G37640.1; AT4G37640.
GeneID829918.
KEGGath:AT4G37640.

Organism-specific databases

TAIRAt4g37640.

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000265623.
InParanoidO81108.
KOK01537.
OMAGFEICAD.
PhylomeDBO81108.
ProtClustDBCLSN2683872.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14659.

Gene expression databases

ArrayExpressO81108.
GenevestigatorO81108.
GermOnlineAT4G37640. Arabidopsis thaliana.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR006408. ATPase_P-typ_Ca-transp_plasma.
IPR006068. 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.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERPTHR24093. PTHR24093. 1 hit.
PfamPF12515. CaATP_NAI. 1 hit.
PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACA2_ARATH
AccessionPrimary (citable) accession number: O81108
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: May 29, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents