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P48578 (PP2A3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. 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:
Serine/threonine-protein phosphatase PP2A-3 catalytic subunit

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 2A isoform 3
Gene names
Name:PP2A3
Synonyms:EP7, PP2A4
Ordered Locus Names:At3g58500
ORF Names:F14P22.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (subunit A), that associates with a variety of regulatory subunits such as subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the PPP phosphatase family. PP-2A subfamily.

Sequence caution

The sequence CAB68188.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Serine/threonine-protein phosphatase PP2A-3 catalytic subunit
PRO_0000058855

Sites

Active site1221Proton donor By similarity
Metal binding611Manganese 1 By similarity
Metal binding631Manganese 1 By similarity
Metal binding891Manganese 1 By similarity
Metal binding891Manganese 2 By similarity
Metal binding1211Manganese 2 By similarity
Metal binding1711Manganese 2 By similarity
Metal binding2451Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P48578 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 0636FF10832B1B00

FASTA31335,767
        10         20         30         40         50         60 
MGANSLPTDA TLDLDEQISQ LMQCKPLSEQ QVRALCEKAK EILMDESNVQ PVKSPVTICG 

        70         80         90        100        110        120 
DIHGQFHDLA ELFRIGGKCP DTNYLFMGDY VDRGYYSVET VTLLVGLKVR YPQRITILRG 

       130        140        150        160        170        180 
NHESRQITQV YGFYDECLRK YGNANVWKIF TDLFDYFPLT ALVESEIFCL HGGLSPSIET 

       190        200        210        220        230        240 
LDNIRNFDRV QEVPHEGPMC DLLWSDPDDR CGWGISPRGA GYTFGQDISE QFNHTNNLKL 

       250        260        270        280        290        300 
IARAHQLVMD GFNWAHEQKV VTIFSAPNYC YRCGNMASIL EVDDCRNHTF IQFEPAPRRG 

       310 
EPDVTRRTPD YFL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of a fourth isoform of the catalytic subunit of protein phosphatase 2A from Arabidopsis thaliana."
Casamayor A., Perez-Callejon E., Pujol G., Arino J., Ferrer A.
Plant Mol. Biol. 26:523-528(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia GL1.
Tissue: Leaf.
[2]"Molecular cloning and characterization of two phosphatase 2A catalytic subunit genes from Arabidopsis thaliana."
Perez-Callejon E., Casamayor A., Pujol G., Camps M., Ferrer A., Arino J.
Gene 209:105-112(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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.
[6]"Arabidopsis PPP family of serine/threonine phosphatases."
Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.
Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08047 mRNA. Translation: AAA64941.1.
U60136 Genomic DNA. Translation: AAD10855.1.
AL137082 Genomic DNA. Translation: CAB68188.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79790.1.
AY057604 mRNA. Translation: AAL14399.1.
AY056222 mRNA. Translation: AAL07071.1.
AY113023 mRNA. Translation: AAM47331.1.
PIRS52660.
RefSeqNP_567066.1. NM_115712.3.
UniGeneAt.25267.

3D structure databases

ProteinModelPortalP48578.
SMRP48578. Positions 11-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid10334. 2 interactions.
IntActP48578. 1 interaction.

Proteomic databases

PaxDbP48578.
PRIDEP48578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G58500.1; AT3G58500.1; AT3G58500.
GeneID825019.
KEGGath:AT3G58500.

Organism-specific databases

TAIRAT3G58500.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
InParanoidP48578.
KOK04382.
OMADPANDSK.
PhylomeDBP48578.

Enzyme and pathway databases

BioCycARA:AT3G58500-MONOMER.

Gene expression databases

GenevestigatorP48578.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP2A3_ARATH
AccessionPrimary (citable) accession number: P48578
Secondary accession number(s): Q9M2G6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 109 of the entry and version 1 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