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Protein

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

Gene

Ppp3cc

Organism
Mus musculus (Mouse)
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

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 bindingi86IronBy similarity1
Metal bindingi88Iron; via tele nitrogenBy similarity1
Metal bindingi114IronBy similarity1
Metal bindingi114ZincBy similarity1
Metal bindingi146ZincBy similarity1
Active sitei147Proton donorBy similarity1
Metal bindingi195Zinc; via tele nitrogenBy similarity1
Metal bindingi277Zinc; via pros nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-111447 Activation of BAD and translocation to mitochondria

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (EC:3.1.3.16By similarity)
Alternative name(s):
CAM-PRP catalytic subunit
Calcineurin, testis-specific catalytic subunit
Calmodulin-dependent calcineurin A subunit gamma isoform
Gene namesi
Name:Ppp3cc
Synonyms:Calnc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:107162 Ppp3cc

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000588291 – 513Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoformAdd BLAST513

Proteomic databases

EPDiP48455
MaxQBiP48455
PaxDbiP48455
PeptideAtlasiP48455
PRIDEiP48455

PTM databases

iPTMnetiP48455
PhosphoSitePlusiP48455

Expressioni

Tissue specificityi

Testis.

Gene expression databases

BgeeiENSMUSG00000022092
ExpressionAtlasiP48455 baseline and differential
GenevisibleiP48455 MM

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 PPP3CC/calcineurin A, calcineurin B and calmodulin. Interacts (via calmodulin-binding domain) with calmodulin; the interaction depends on calmodulin binding to Ca2+.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202346, 3 interactors
ComplexPortaliCPX-1007 Calcineurin-Calmodulin complex, gamma-R1 variant
CPX-1051 Calcineurin-Calmodulin complex, gamma-R2 variant
IntActiP48455, 1 interactor
STRINGi10090.ENSMUSP00000077532

Structurei

3D structure databases

ProteinModelPortaliP48455
SMRiP48455
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni52 – 343CatalyticCuratedAdd BLAST292
Regioni344 – 366Calcineurin B bindingBy similarityAdd BLAST23
Regioni385 – 399Calmodulin-bindingBy similarityAdd BLAST15
Regioni400 – 407Autoinhibitory segmentBy similarity8
Regioni458 – 480Autoinhibitory domainBy similarityAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi303 – 307SAPNY motifBy similarity5

Domaini

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-305 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
GeneTreeiENSGT00530000063087
HOVERGENiHBG002819
InParanoidiP48455
KOiK04348
OMAiFSLQHKI
OrthoDBiEOG091G094R
PhylomeDBiP48455
TreeFamiTF105557

Family and domain databases

Gene3Di3.60.21.10, 2 hits
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.

P48455-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVRRPQFST TERVIKAVPF PPTRRLTLKE VFENGKPKMD LLKNHLVKEG
60 70 80 90 100
RVEEEVALKI INDGAAILKQ EKTMIEVEAP ITVCGDVHGQ FFDLMKLFEV
110 120 130 140 150
GGSPSNTRYL FLGDYVDRGY FSIECVLYLW SLKINHPKTL FLLRGNHECR
160 170 180 190 200
HLTEYFTFKQ ECRIKYSEMV YDACMHTFDC LPLAALLNQQ FLCVHGGMSP
210 220 230 240 250
EITCLEDIRK LDRFSEPPAF GPVCDLLWSD PLEDYGSEKT LEHYTHNTVR
260 270 280 290 300
GCSYFFSYPA VCEFLQNNSL LSIIRAHEAQ DAGYRMYRKN QATGFPSLIT
310 320 330 340 350
IFSAPNYLDV YNNKAAVLKY ENNVMNIRQF NCSPHPYWLP NFMDVFTWSL
360 370 380 390 400
PFVGEKVTEM LVNILNICSD EEMNVTDEEG ATTGRKEVIK NKIRAIGKMA
410 420 430 440 450
RVFTVLREES ENVLTLKGLT PTGTLPLGVL SGGKQTIETA KQEAAEEREA
460 470 480 490 500
IRGFTIAHRI RSFEEARGLD RINERMPPRK EASYHHDAGR MHSHSHPPHP
510
QASRRTDHGK KAL
Length:513
Mass (Da):58,699
Last modified:February 1, 1996 - v1
Checksum:i521CB2B1DD9E03A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81475 mRNA Translation: AAA39968.1
AK133393 mRNA Translation: BAE21630.1
CH466535 Genomic DNA Translation: EDL35914.1
BC141079 mRNA Translation: AAI41080.1
CCDSiCCDS36968.1
PIRiA38193
RefSeqiNP_032941.1, NM_008915.3
UniGeneiMm.439683

Genome annotation databases

EnsembliENSMUST00000078434; ENSMUSP00000077532; ENSMUSG00000022092
GeneIDi19057
KEGGimmu:19057
UCSCiuc007unp.2 mouse

Similar proteinsi

Entry informationi

Entry nameiPP2BC_MOUSE
AccessioniPrimary (citable) accession number: P48455
Secondary accession number(s): Q3V074
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 18, 2018
This is version 137 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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