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P63329

- PP2BA_RAT

UniProt

P63329 - PP2BA_RAT

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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform

Gene

Ppp3ca

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901IronBy similarity
Metal bindingi92 – 921IronBy similarity
Metal bindingi118 – 1181IronBy similarity
Metal bindingi118 – 1181ZincBy similarity
Metal bindingi150 – 1501ZincBy similarity
Active sitei151 – 1511Proton donorBy similarity
Metal bindingi199 – 1991ZincBy similarity
Metal bindingi281 – 2811ZincBy similarity

GO - Molecular functioni

  1. calcium-dependent protein serine/threonine phosphatase activity Source: RGD
  2. calmodulin binding Source: RGD
  3. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  4. drug binding Source: Ensembl
  5. metal ion binding Source: UniProtKB-KW
  6. phosphoprotein phosphatase activity Source: RGD
  7. protein heterodimerization activity Source: RGD
  8. protein serine/threonine phosphatase activity Source: RGD

GO - Biological processi

  1. calcineurin-NFAT signaling cascade Source: Ensembl
  2. calcium ion transport Source: Ensembl
  3. cellular response to drug Source: Ensembl
  4. cellular response to glucose stimulus Source: BHF-UCL
  5. G1/S transition of mitotic cell cycle Source: Ensembl
  6. multicellular organismal response to stress Source: Ensembl
  7. negative regulation of calcium ion-dependent exocytosis Source: BHF-UCL
  8. negative regulation of insulin secretion Source: BHF-UCL
  9. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  10. protein dephosphorylation Source: RGD
  11. protein import into nucleus Source: Ensembl
  12. regulation of excitatory postsynaptic membrane potential Source: Ensembl
  13. regulation of synaptic transmission Source: Ensembl
  14. response to amphetamine Source: RGD
  15. response to calcium ion Source: UniProtKB
  16. skeletal muscle fiber development Source: Ensembl
  17. transition between fast and slow fiber Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_194690. Ca2+ pathway.
REACT_203734. FCERI mediated Ca+2 mobilization.
REACT_242934. DARPP-32 events.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ppp3ca
Synonyms:Calna
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi3382. Ppp3ca.

Subcellular locationi

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

GO - Cellular componenti

  1. calcineurin complex Source: RGD
  2. cytosol Source: RGD
  3. membrane Source: RGD
  4. mitochondrion Source: Ensembl
  5. nucleus Source: UniProtKB-SubCell
  6. sarcolemma Source: UniProtKB-SubCell
  7. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 521520Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoformPRO_0000058824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei224 – 2241Nitrated tyrosineBy similarity

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

PaxDbiP63329.
PRIDEiP63329.

PTM databases

PhosphoSiteiP63329.

Expressioni

Gene expression databases

GenevestigatoriP63329.

Interactioni

Subunit structurei

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. Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy. Interacts with CMYA5; this interaction represses calcineurin activity in muscle (By similarity). Interacts with CHP1 and CHP2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cacna1cP220025EBI-7022944,EBI-1185084
Cacng8Q8VHW56EBI-7022944,EBI-9086576

Protein-protein interaction databases

BioGridi246806. 3 interactions.
IntActiP63329. 4 interactions.
MINTiMINT-4106043.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 344Combined sources
Helixi43 – 519Combined sources
Helixi58 – 7215Combined sources
Beta strandi77 – 815Combined sources
Beta strandi83 – 886Combined sources
Helixi95 – 10511Combined sources
Turni108 – 1103Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi120 – 1234Combined sources
Helixi126 – 13914Combined sources
Turni141 – 1433Combined sources
Beta strandi144 – 1463Combined sources
Helixi154 – 1596Combined sources
Helixi162 – 1687Combined sources
Helixi172 – 18413Combined sources
Beta strandi188 – 1914Combined sources
Turni192 – 1943Combined sources
Beta strandi195 – 2006Combined sources
Helixi209 – 2135Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2253Combined sources
Helixi226 – 2327Combined sources
Turni237 – 2404Combined sources
Beta strandi247 – 2504Combined sources
Turni252 – 2554Combined sources
Beta strandi256 – 2605Combined sources
Helixi262 – 27110Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi287 – 2904Combined sources
Turni295 – 2973Combined sources
Beta strandi299 – 3068Combined sources
Helixi311 – 3133Combined sources
Beta strandi319 – 3257Combined sources
Beta strandi328 – 3347Combined sources
Helixi344 – 3463Combined sources
Helixi349 – 36618Combined sources
Helixi473 – 4764Combined sources
Helixi478 – 4814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IL1X-ray3.00A/B/C/D1-492[»]
ProteinModelPortaliP63329.
SMRiP63329. Positions 1-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 301300CatalyticAdd
BLAST
Regioni247 – 2537Calcineurin B binding-site 1Sequence Analysis
Regioni296 – 3016Calcineurin B binding-site 2Sequence Analysis
Regioni392 – 41423Calmodulin-bindingSequence AnalysisAdd
BLAST
Regioni465 – 48723Inhibitory domainAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP63329.
KOiK04348.
OMAiELICEGD.
OrthoDBiEOG7BZVSC.
PhylomeDBiP63329.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P63329-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL 
        60         70         80         90        100
MKEGRLEESV ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK 
       110        120        130        140        150
LFEVGGSPAN TRYLFLGDYV DRGYFSIECV LYLWALKILY PKTLFLLRGN 
       160        170        180        190        200
HECRHLTEYF TFKQECKIKY SERVYDACMD AFDCLPLAAL MNQQFLCVHG 
       210        220        230        240        250
GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG NEKTQEHFTH 
       260        270        280        290        300
NTVRGCSYFY SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 
       310        320        330        340        350
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF 
       360        370        380        390        400
TWSLPFVGEK VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI 
       410        420        430        440        450
RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLSGG KQTLQSATVE 
       460        470        480        490        500
AIEADEAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM PSDANLNSIN 
       510        520 
KALASETNGT DSNGSNSSNI Q
Length:521
Mass (Da):58,644
Last modified:October 11, 2004 - v1
Checksum:i16530C27DDBF1F05
GO
Isoform 2 (identifier: P63329-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:511
Mass (Da):57,615
Checksum:i01428D70D67450BD
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei448 – 45710Missing in isoform 2. 1 PublicationVSP_018564

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA33264.
RefSeqiNP_058737.1. NM_017041.1. [P63329-1]
XP_006233425.1. XM_006233363.2. [P63329-2]
UniGeneiRn.228648.
Rn.6866.

Genome annotation databases

EnsembliENSRNOT00000047975; ENSRNOP00000049674; ENSRNOG00000009882. [P63329-2]
GeneIDi24674.
KEGGirno:24674.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 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 .
PIRi A33264.
RefSeqi NP_058737.1. NM_017041.1. [P63329-1 ]
XP_006233425.1. XM_006233363.2. [P63329-2 ]
UniGenei Rn.228648.
Rn.6866.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IL1 X-ray 3.00 A/B/C/D 1-492 [» ]
ProteinModelPortali P63329.
SMRi P63329. Positions 1-411.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246806. 3 interactions.
IntActi P63329. 4 interactions.
MINTi MINT-4106043.

PTM databases

PhosphoSitei P63329.

Proteomic databases

PaxDbi P63329.
PRIDEi P63329.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000047975 ; ENSRNOP00000049674 ; ENSRNOG00000009882 . [P63329-2 ]
GeneIDi 24674.
KEGGi rno:24674.

Organism-specific databases

CTDi 5530.
RGDi 3382. Ppp3ca.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000063087.
HOGENOMi HOG000172699.
HOVERGENi HBG002819.
InParanoidi P63329.
KOi K04348.
OMAi ELICEGD.
OrthoDBi EOG7BZVSC.
PhylomeDBi P63329.

Enzyme and pathway databases

Reactomei REACT_194690. Ca2+ pathway.
REACT_203734. FCERI mediated Ca+2 mobilization.
REACT_242934. DARPP-32 events.

Miscellaneous databases

NextBioi 295542.

Gene expression databases

Genevestigatori P63329.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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, IDENTIFICATION BY 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.

Entry informationi

Entry nameiPP2BA_RAT
AccessioniPrimary (citable) accession number: P63329
Secondary accession number(s): P12816
, P20652, Q6LDJ8, Q9WUV7, Q9Z1I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 7, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.
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