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P63329 (PP2BA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 84. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
EC=3.1.3.16
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit alpha isoform
Gene names
Name:Ppp3ca
Synonyms:Calna
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. Many of the substrates contain a PxIxIT motif. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1 By similarity. Ref.2

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 1 Fe3+ ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity. Interacts with CRTC2, MYOZ1, MYOZ2 and MYOZ3 Interacts with DNM1L; the interaction dephosphorylates DNM1L and regulates its translocation to mitochondria By similarity. Interacts with CHP1 and CHP2. Interacts with CMYA5; this interaction represses calcineurin activity in muscle By similarity. Ref.6 Ref.7

Subcellular location

Nucleus By similarity. Note: Colocalizes with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
Iron
Metal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Nitration
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

calcineurin-NFAT signaling cascade

Inferred from electronic annotation. Source: Ensembl

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 19965390. Source: BHF-UCL

negative regulation of calcium ion-dependent exocytosis

Inferred by curator PubMed 19965390. Source: BHF-UCL

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 19965390. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay PubMed 12135494Ref.2. Source: RGD

protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic transmission

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from expression pattern PubMed 11954050. Source: RGD

response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

response to stress

Inferred from electronic annotation. Source: Ensembl

skeletal muscle fiber development

Inferred from electronic annotation. Source: Ensembl

transition between fast and slow fiber

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

calcineurin complex

Inferred from direct assay PubMed 12135494. Source: RGD

cytosol

Inferred from direct assay PubMed 16150427. Source: RGD

membrane

Inferred from direct assay PubMed 16150427. Source: RGD

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalmodulin binding

Inferred from direct assay PubMed 12135494. Source: RGD

calmodulin-dependent protein phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterodimerization activity

Inferred from direct assay PubMed 12135494. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cacna1cP220025EBI-7022944,EBI-1185084

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P63329-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P63329-2)

The sequence of this isoform differs from the canonical sequence as follows:
     448-457: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 521520Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
PRO_0000058824

Regions

Region2 – 301300Catalytic
Region247 – 2537Calcineurin B binding-site 1 Potential
Region296 – 3016Calcineurin B binding-site 2 Potential
Region392 – 41423Calmodulin-binding Potential
Region465 – 48723Inhibitory domain

Sites

Active site1511Proton donor By similarity
Metal binding901Iron By similarity
Metal binding921Iron By similarity
Metal binding1181Iron By similarity
Metal binding1181Zinc By similarity
Metal binding1501Zinc By similarity
Metal binding1991Zinc By similarity
Metal binding2811Zinc By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue2241Nitrated tyrosine By similarity

Natural variations

Alternative sequence448 – 45710Missing in isoform 2.
VSP_018564

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 16530C27DDBF1F05

FASTA52158,644
        10         20         30         40         50         60 
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV 

        70         80         90        100        110        120 
ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV 

       130        140        150        160        170        180 
DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD 

       190        200        210        220        230        240 
AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG 

       250        260        270        280        290        300 
NEKTQEHFTH NTVRGCSYFY SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 

       310        320        330        340        350        360 
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK 

       370        380        390        400        410        420 
VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV 

       430        440        450        460        470        480 
LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN 

       490        500        510        520 
ERMPPRRDAM PSDANLNSIN KALASETNGT DSNGSNSSNI Q

« Hide

Isoform 2 [UniParc].

Checksum: 01428D70D67450BD
Show »

FASTA51157,615

References

[1]"The complete primary structure of calcineurin A, a calmodulin binding protein homologous with protein phosphatases 1 and 2A."
Ito A., Hashimoto T., Hirai M., Takeda T., Shuntoh H., Kuno T., Tanaka C.
Biochem. Biophys. Res. Commun. 163:1492-1497(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of the phosphatase activity of a baculovirus-expressed calcineurin A isoform."
Perrino B.A., Fong Y.L., Brickey D.A., Saitoh Y., Ushio Y., Fukunaga K., Miyamoto E., Soderling T.R.
J. Biol. Chem. 267:15965-15969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
[3]"Molecular cloning and characterization of the promoter region of the calcineurin A alpha gene."
Chang C., Takeda T., Mukai H., Shuntoh H., Kuno T., Tanaka C.
Biochem. J. 288:801-805(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
Tissue: Liver.
[4]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 143-148, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[5]"Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells."
Wadzinski B.E., Heasley L.E., Johnson G.L.
J. Biol. Chem. 265:21504-21508(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 236-306.
[6]"Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein."
Lin X., Sikkink R.A., Rusnak F., Barber D.L.
J. Biol. Chem. 274:36125-36131(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHP1.
[7]"CHP2 activates the calcineurin/nuclear factor of activated T cells signaling pathway and enhances the oncogenic potential of HEK293 cells."
Li G.D., Zhang X., Li R., Wang Y.D., Wang Y.L., Han K.J., Qian X.P., Yang C.G., Liu P., Wei Q., Chen W.F., Zhang J., Zhang Y.
J. Biol. Chem. 283:32660-32668(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHP2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D90035 mRNA. Translation: BAA14083.1.
M29275 mRNA. Translation: AAA40940.1.
X57115 mRNA. Translation: CAA40398.2.
D10480 Genomic DNA. Translation: BAA01283.1.
M58440 mRNA. Translation: AAA41914.1.
IPIIPI00201410.
IPI00559849.
PIRA33264.
RefSeqNP_058737.1. NM_017041.1.
UniGeneRn.6866.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IL1X-ray3.00A/B/C/D1-492[»]
ProteinModelPortalP63329.
SMRP63329. Positions 1-411.
ModBaseSearch...

Protein-protein interaction databases

IntActP63329. 1 interaction.
MINTMINT-4106043.

PTM databases

PhosphoSiteP63329.

Proteomic databases

PaxDbP63329.
PRIDEP63329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000047975; ENSRNOP00000049674; ENSRNOG00000009882.
GeneID24674.
KEGGrno:24674.

Organism-specific databases

CTD5530.
RGD3382. Ppp3ca.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063087.
HOGENOMHOG000172699.
HOVERGENHBG002819.
InParanoidP63329.
KOK04348.
OMARTKPNIQ.
OrthoDBEOG7BZVSC.

Enzyme and pathway databases

ReactomeREACT_111984. Signal Transduction.

Gene expression databases

GenevestigatorP63329.

Family and domain databases

InterProIPR004843. PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295542.

Entry information

Entry namePP2BA_RAT
AccessionPrimary (citable) accession number: P63329
Secondary accession number(s): P12816 expand/collapse secondary AC list , P20652, Q6LDJ8, Q9WUV7, Q9Z1I5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 13, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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