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Protein

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

Gene

Ppp3cb

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

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca2+-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32.By similarity

Miscellaneous

Unlike for protein substrates, PPP3CB activity towards synthetic phosphatase substrate p-nitrophenyl phosphate (pNPP) is increased in presence of the immunosuppressant complex FKBP12-FK506.By similarity

Catalytic activityi

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

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

Enzyme regulationi

Activated by Ca2+-bound calmodulin following an increase in intracellular Ca2+. At low Ca2+ concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca2+. In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca2+ causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A. The subsequent binding of Ca2+-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi99IronBy similarity1
Metal bindingi101Iron; via tele nitrogenBy similarity1
Metal bindingi127IronBy similarity1
Metal bindingi127ZincBy similarity1
Metal bindingi159ZincBy similarity1
Active sitei160Proton donorBy similarity1
Metal bindingi208Zinc; via tele nitrogenBy similarity1
Metal bindingi290Zinc; via pros nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • calcium ion regulated exocytosis Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • muscle cell cellular homeostasis Source: RGD
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • protein dephosphorylation Source: RGD
  • protein phosphorylation Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • response to amphetamine Source: RGD

Keywordsi

Molecular functionCalmodulin-binding, Hydrolase, Protein phosphatase
LigandIron, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC:3.1.3.16By similarity)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform
Short name:
CNA betaBy similarity
Gene namesi
Name:Ppp3cb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3383 Ppp3cb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000588272 – 525Serine/threonine-protein phosphatase 2B catalytic subunit beta isoformAdd BLAST524

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei479PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP20651
PRIDEiP20651

PTM databases

iPTMnetiP20651
PhosphoSitePlusiP20651

Interactioni

Subunit structurei

Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca2+-binding subunit (also known as calcineurin B). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). In response to an increase in Ca2+ intracellular levels, forms a complex composed of PPP3CB/calcineurin A, calcineurin B and calmodulin. Interacts (via calcineurin B binding domain) with regulatory subunit PPP3R1/calcineurin B. Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca2+.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Akap6Q9WVC72EBI-7400670,EBI-7559840

GO - Molecular functioni

  • calmodulin binding Source: RGD
  • enzyme binding Source: UniProtKB
  • protein heterodimerization activity Source: RGD
  • protein phosphatase 2B binding Source: UniProtKB

Protein-protein interaction databases

BioGridi246807, 1 interactor
CORUMiP20651
DIPiDIP-66N
IntActiP20651, 4 interactors
MINTiP20651
STRINGi10116.ENSRNOP00000010476

Structurei

3D structure databases

ProteinModelPortaliP20651
SMRiP20651
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni65 – 356CatalyticBy similarityAdd BLAST292
Regioni357 – 379Calcineurin B bindingBy similarityAdd BLAST23
Regioni402 – 416Calmodulin-bindingBy similarityAdd BLAST15
Regioni417 – 424Autoinhibitory segmentBy similarity8
Regioni475 – 497Autoinhibitory domainBy similarityAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi316 – 320SAPNY motifBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 20Poly-ProSequence analysis10

Domaini

The poly-Pro domain may confer substrate specificity.By similarity
The autoinhibitory domain prevents access to the catalytic site.By similarity
The autoinhibitory segment prevents access to the substrate binding site.By similarity
Possible isomerization of Pro-318 within the SAPNY motif triggers a conformation switch which affects the organization and thus accessibility of the active site and the substrate binding region (PxIxIF motif). The trans- to cis-transition may favor calcineurin A activation and substrate binding. The reverse cis- to trans-transition may be enhanced by peptidyl-prolyl isomerases such as PPIA.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0375 Eukaryota
COG0639 LUCA
HOGENOMiHOG000172699
HOVERGENiHBG002819
InParanoidiP20651
KOiK04348
PhylomeDBiP20651

Family and domain databases

Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR006186 Ser/Thr-sp_prot-phosphatase
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

P20651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP
60 70 80 90 100
RVDVLKNHLV KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI
110 120 130 140 150
HGQFFDLMKL FEVGGSPANT RYLFLGDYVD RGYFSIECVL YLWVLKILYP
160 170 180 190 200
STLFLLRGNH ECRHLTEYFT FKQECKIKYS ERVYEACMEA FDSLPLAALL
210 220 230 240 250
NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL WSDPSEDFGN
260 270 280 290 300
EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
310 320 330 340 350
RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY
360 370 380 390 400
WLPNFMDVFT WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDVGSAA
410 420 430 440 450
ARKEIIRNKI RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLAGG
460 470 480 490 500
RQTLQSATVE AIEAEKAIRG SSPPHRICSF EEAKGLDRIN ERMPPRKDAV
510 520
QQDGFNSLNT AHTTENHGTG NHSAQ
Length:525
Mass (Da):59,113
Last modified:February 1, 1991 - v1
Checksum:i5E66AF3100BE3987
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31809 mRNA Translation: AAA40848.1
D90036 mRNA Translation: BAA14084.1
M58441 mRNA Translation: AAA41915.1
PIRiA33794
RefSeqiNP_058738.1, NM_017042.2
UniGeneiRn.11063

Genome annotation databases

GeneIDi24675
KEGGirno:24675
UCSCiRGD:3383 rat

Similar proteinsi

Entry informationi

Entry nameiPP2BB_RAT
AccessioniPrimary (citable) accession number: P20651
Secondary accession number(s): Q6LDJ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 20, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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