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Protein

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

Gene

PPP3CA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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+Note: Binds 1 Fe3+ ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901Iron1 Publication
Metal bindingi92 – 921Iron1 Publication
Metal bindingi118 – 1181Iron1 Publication
Metal bindingi118 – 1181Zinc1 Publication
Metal bindingi150 – 1501Zinc1 Publication
Active sitei151 – 1511Proton donorBy similarity
Metal bindingi199 – 1991Zinc1 Publication
Metal bindingi281 – 2811Zinc1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.3.16. 908.
ReactomeiREACT_301041. DARPP-32 events.
REACT_340538. FCERI mediated Ca+2 mobilization.
REACT_342659. Ca2+ pathway.
REACT_361859. CLEC7A (Dectin-1) induces NFAT activation.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

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_0000058821Add
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

PRIDEiP48452.

Expressioni

Gene expression databases

ExpressionAtlasiP48452. baseline.

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

Protein-protein interaction databases

IntActiP48452. 1 interaction.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 344Combined sources
Helixi43 – 519Combined sources
Helixi58 – 7417Combined 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 – 1698Combined sources
Helixi172 – 18211Combined sources
Beta strandi188 – 1914Combined sources
Turni192 – 1943Combined sources
Beta strandi195 – 1973Combined sources
Helixi209 – 2135Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2253Combined sources
Helixi226 – 2327Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi247 – 2504Combined sources
Turni252 – 2554Combined sources
Beta strandi256 – 2605Combined sources
Helixi262 – 27211Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi295 – 30511Combined sources
Helixi311 – 3133Combined sources
Beta strandi319 – 3257Combined sources
Beta strandi328 – 3347Combined sources
Helixi344 – 3463Combined sources
Helixi349 – 36921Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TCOX-ray2.50A18-392[»]
2F2OX-ray2.17A/B389-413[»]
2F2PX-ray2.60A/B389-413[»]
ProteinModelPortaliP48452.
SMRiP48452. Positions 21-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48452.

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.
InParanoidiP48452.
KOiK04348.
OMAiELICEGD.
OrthoDBiEOG7BZVSC.
TreeFamiTF105557.

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. AlignAdd to basket

Isoform 1 (identifier: P48452-1) [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
MKEGRLEETV 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 SYPAVCEFLQ 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):58,672
Last modified:February 1, 1996 - v1
Checksum:iF3F153F22AB56BDF
GO
Isoform 2 (identifier: P48452-2) [UniParc]FASTAAdd to basket

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

Show »
Length:511
Mass (Da):57,643
Checksum:iC383F9EF7B41D775
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti367 – 3671N → D in ABB22788 (PubMed:15967565).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei448 – 45710Missing in isoform 2. 1 PublicationVSP_018561

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33868 mRNA. Translation: AAC48473.1.
DQ231569 mRNA. Translation: ABB22788.1.
BC123668 mRNA. Translation: AAI23669.1.
PIRiA56968.
RefSeqiNP_777212.1. NM_174787.2. [P48452-1]
XP_005207750.1. XM_005207693.2. [P48452-2]
UniGeneiBt.3966.

Genome annotation databases

EnsembliENSBTAT00000021305; ENSBTAP00000021305; ENSBTAG00000016005. [P48452-1]
ENSBTAT00000056385; ENSBTAP00000047848; ENSBTAG00000016005. [P48452-2]
GeneIDi286852.
KEGGibta:286852.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33868 mRNA. Translation: AAC48473.1.
DQ231569 mRNA. Translation: ABB22788.1.
BC123668 mRNA. Translation: AAI23669.1.
PIRiA56968.
RefSeqiNP_777212.1. NM_174787.2. [P48452-1]
XP_005207750.1. XM_005207693.2. [P48452-2]
UniGeneiBt.3966.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TCOX-ray2.50A18-392[»]
2F2OX-ray2.17A/B389-413[»]
2F2PX-ray2.60A/B389-413[»]
ProteinModelPortaliP48452.
SMRiP48452. Positions 21-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48452. 1 interaction.

Proteomic databases

PRIDEiP48452.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000021305; ENSBTAP00000021305; ENSBTAG00000016005. [P48452-1]
ENSBTAT00000056385; ENSBTAP00000047848; ENSBTAG00000016005. [P48452-2]
GeneIDi286852.
KEGGibta:286852.

Organism-specific databases

CTDi5530.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP48452.
KOiK04348.
OMAiELICEGD.
OrthoDBiEOG7BZVSC.
TreeFamiTF105557.

Enzyme and pathway databases

BRENDAi3.1.3.16. 908.
ReactomeiREACT_301041. DARPP-32 events.
REACT_340538. FCERI mediated Ca+2 mobilization.
REACT_342659. Ca2+ pathway.
REACT_361859. CLEC7A (Dectin-1) induces NFAT activation.

Miscellaneous databases

EvolutionaryTraceiP48452.
NextBioi20806501.

Gene expression databases

ExpressionAtlasiP48452. baseline.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON AND ZINC.
    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] [Europe PMC] [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.

Entry informationi

Entry nameiPP2BA_BOVIN
AccessioniPrimary (citable) accession number: P48452
Secondary accession number(s): Q08DM4, Q309F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 27, 2015
This is version 128 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, 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.