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P48452 (PP2BA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1 By similarity.

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 1 Fe3+ ion per subunit.

Binds 1 zinc ion per subunit.

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.

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
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalmodulin binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48452-1)

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: P48452-2)

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

Chain1 – 521521Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
PRO_0000058821

Regions

Region1 – 301301Catalytic
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 Ref.1
Metal binding921Iron
Metal binding1181Iron
Metal binding1181Zinc
Metal binding1501Zinc Ref.1
Metal binding1991Zinc Ref.1
Metal binding2811Zinc Ref.1

Amino acid modifications

Modified residue4691Phosphoserine By similarity

Natural variations

Alternative sequence448 – 45710Missing in isoform 2.
VSP_018561

Experimental info

Sequence conflict3671N → D in ABB22788. Ref.2

Secondary structure

1 .................................................................. 521
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1996. Version 1.
Checksum: F3F153F22AB56BDF

FASTA52158,672
        10         20         30         40         50         60 
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEETV 

        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 SYPAVCEFLQ 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: C383F9EF7B41D775
Show »

FASTA51157,643

References

« Hide 'large scale' references
[1]"X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex."
Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A., Fitzgibbon M.J., Fleming M.A., Caron P.R., Hsiao K., Navia M.A.
Cell 82:507-522(1995) [PubMed: 7543369] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Tissue: Brain.
[2]"Molecular cloning, expression, purification and characterization of calcineurin from bovine cardiac muscle."
Selvakumar P., Lakshmikuttyamma A., Anderson D.H., Sharma R.K.
Biochimie 87:975-983(2005) [PubMed: 15967565] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Heart muscle.
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: Hereford.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U33868 mRNA. Translation: AAC48473.1.
DQ231569 mRNA. Translation: ABB22788.1.
BC123668 mRNA. Translation: AAI23669.1.
IPIIPI00704314.
IPI00759423.
PIRA56968.
RefSeqNP_777212.1. NM_174787.2.
UniGeneBt.3966.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TCOX-ray2.50A18-392[»]
2F2OX-ray2.17A/B389-413[»]
2F2PX-ray2.60A/B389-413[»]
ProteinModelPortalP48452.
SMRP48452. Positions 21-372.
ModBaseSearch...

Protein-protein interaction databases

STRINGP48452.

Proteomic databases

PRIDEP48452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000021305; ENSBTAP00000021305; ENSBTAG00000016005.
ENSBTAT00000056385; ENSBTAP00000047848; ENSBTAG00000016005.
GeneID286852.
KEGGbta:286852.

Organism-specific databases

CTD5530.

Phylogenomic databases

eggNOGmaNOG05615.
GeneTreeENSGT00530000063087.
HOVERGENHBG002819.
InParanoidP48452.
OMASVWPAGP.
OrthoDBEOG4PVNZK.
PhylomeDBP48452.

Family and domain databases

InterProIPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
KOK04348.
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP2BA_BOVIN
AccessionPrimary (citable) accession number: P48452
Secondary accession number(s): Q08DM4, Q309F2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 16, 2011
This is version 97 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

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