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P20651 (PP2BB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 beta isoform
EC=3.1.3.16
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform
Gene names
Name:Ppp3cb
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

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.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 525524Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
PRO_0000058827

Regions

Region2 – 310309Catalytic
Region256 – 2627Calcineurin B binding-site 1 Potential
Region305 – 3106Calcineurin B binding-site 2 Potential
Region402 – 42423Calmodulin-binding Potential
Region475 – 49723Inhibitory domain
Compositional bias11 – 2010Poly-Pro

Sites

Active site1601Proton donor By similarity
Metal binding991Iron By similarity
Metal binding1011Iron By similarity
Metal binding1271Iron By similarity
Metal binding1271Zinc By similarity
Metal binding1591Zinc By similarity
Metal binding2081Zinc By similarity
Metal binding2901Zinc By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
P20651 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 5E66AF3100BE3987

FASTA52559,113
        10         20         30         40         50         60 
MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP RVDVLKNHLV 

        70         80         90        100        110        120 
KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI HGQFFDLMKL FEVGGSPANT 

       130        140        150        160        170        180 
RYLFLGDYVD RGYFSIECVL YLWVLKILYP STLFLLRGNH ECRHLTEYFT FKQECKIKYS 

       190        200        210        220        230        240 
ERVYEACMEA FDSLPLAALL NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL 

       250        260        270        280        290        300 
WSDPSEDFGN EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY 

       310        320        330        340        350        360 
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY WLPNFMDVFT 

       370        380        390        400        410        420 
WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDVGSAA ARKEIIRNKI RAIGKMARVF 

       430        440        450        460        470        480 
SVLREESESV LTLKGLTPTG MLPSGVLAGG RQTLQSATVE AIEAEKAIRG SSPPHRICSF 

       490        500        510        520 
EEAKGLDRIN ERMPPRKDAV QQDGFNSLNT AHTTENHGTG NHSAQ

« Hide

References

[1]"Evidence for a second isoform of the catalytic subunit of calmodulin-dependent protein phosphatase (calcineurin A)."
Kuno T., Takeda T., Hirai M., Ito A., Mukai H., Tanaka C.
Biochem. Biophys. Res. Commun. 165:1352-1358(1989) [PubMed: 2558657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 2174876] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M31809 mRNA. Translation: AAA40848.1.
D90036 mRNA. Translation: BAA14084.1.
M58441 mRNA. Translation: AAA41915.1.
IPIIPI00201407.
PIRA33794.
RefSeqNP_058738.1. NM_017042.1.
UniGeneRn.11063.

3D structure databases

ProteinModelPortalP20651.
SMRP20651. Positions 24-381.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-66N.
STRINGP20651.

PTM databases

PhosphoSiteP20651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24675.
KEGGrno:24675.

Organism-specific databases

CTD5532.
RGD3383. Ppp3cb.

Phylogenomic databases

eggNOGroNOG04245.
GeneTreeENSGT00530000063087.
HOVERGENHBG002819.
InParanoidP20651.
OrthoDBEOG4PVNZK.
PhylomeDBP20651.

Gene expression databases

ArrayExpressP20651.
GenevestigatorP20651.
GermOnlineENSRNOG00000007757. Rattus norvegicus.

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...

Other

NextBio604059.

Entry information

Entry namePP2BB_RAT
AccessionPrimary (citable) accession number: P20651
Secondary accession number(s): Q6LDJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 16, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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