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Protein

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

Gene

PPP3CA

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

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase (PubMed:7543369). 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 similarity1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi90Iron1 Publication1
Metal bindingi92Iron1 Publication1
Metal bindingi118Iron1 Publication1
Metal bindingi118Zinc1 Publication1
Metal bindingi150Zinc1 Publication1
Active sitei151Proton donorBy similarity1
Metal bindingi199Zinc1 Publication1
Metal bindingi281Zinc1 Publication1

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • calmodulin-dependent protein phosphatase activity Source: UniProtKB
  • cyclosporin A binding Source: Ensembl
  • enzyme binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • protein dimerization activity Source: Ensembl

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi3.1.3.16 908
ReactomeiR-BTA-2025928 Calcineurin activates NFAT
R-BTA-2871809 FCERI mediated Ca+2 mobilization
R-BTA-4086398 Ca2+ pathway
R-BTA-5607763 CLEC7A (Dectin-1) induces NFAT activation

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC:3.1.3.16By similarity)
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
Proteomesi
  • UP000009136 Componenti: Chromosome 6

Organism-specific databases

VGNCiVGNC:33265 PPP3CA

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

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000588212 – 521Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoformAdd BLAST520

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei224Nitrated tyrosineBy similarity1
Modified residuei469PhosphoserineBy similarity1
Modified residuei492PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP48452
PRIDEiP48452

PTM databases

iPTMnetiP48452

Expressioni

Gene expression databases

BgeeiENSBTAG00000016005

Interactioni

Subunit structurei

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity (PubMed:7543369). Interacts with CRTC2, MYOZ1, MYOZ2 and MYOZ3. Interacts with DNM1L; the interaction dephosphorylates DNM1L and regulates its translocation to mitochondria. Interacts with CMYA5; this interaction represses calcineurin activity in muscle (By similarity). Interacts (constitutively active form) with SYNPO2 (By similarity)Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy (By similarity). Interacts with CHP1 and CHP2 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • enzyme binding Source: Ensembl
  • protein dimerization activity Source: Ensembl

Protein-protein interaction databases

IntActiP48452, 1 interactor
MINTiP48452
STRINGi9913.ENSBTAP00000021305

Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 34Combined sources4
Helixi43 – 51Combined sources9
Helixi58 – 74Combined sources17
Beta strandi77 – 81Combined sources5
Beta strandi83 – 88Combined sources6
Helixi95 – 105Combined sources11
Turni108 – 110Combined sources3
Beta strandi113 – 115Combined sources3
Beta strandi120 – 123Combined sources4
Helixi126 – 139Combined sources14
Turni141 – 143Combined sources3
Beta strandi144 – 146Combined sources3
Helixi154 – 159Combined sources6
Helixi162 – 169Combined sources8
Helixi172 – 182Combined sources11
Beta strandi188 – 191Combined sources4
Turni192 – 194Combined sources3
Beta strandi195 – 197Combined sources3
Helixi209 – 213Combined sources5
Beta strandi218 – 220Combined sources3
Beta strandi223 – 225Combined sources3
Helixi226 – 232Combined sources7
Beta strandi239 – 241Combined sources3
Beta strandi247 – 250Combined sources4
Turni252 – 255Combined sources4
Beta strandi256 – 260Combined sources5
Helixi262 – 272Combined sources11
Beta strandi275 – 279Combined sources5
Beta strandi287 – 290Combined sources4
Beta strandi295 – 305Combined sources11
Helixi311 – 313Combined sources3
Beta strandi319 – 325Combined sources7
Beta strandi328 – 334Combined sources7
Helixi344 – 346Combined sources3
Helixi349 – 369Combined sources21

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP48452

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 301CatalyticAdd BLAST300
Regioni247 – 253Calcineurin B binding-site 1Sequence analysis7
Regioni296 – 301Calcineurin B binding-site 2Sequence analysis6
Regioni392 – 414Calmodulin-bindingSequence analysisAdd BLAST23
Regioni465 – 487Inhibitory domainAdd BLAST23

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0375 Eukaryota
COG0639 LUCA
GeneTreeiENSGT00530000063087
HOGENOMiHOG000172699
HOVERGENiHBG002819
InParanoidiP48452
KOiK04348
OMAiLWSLKIW
OrthoDBiEOG091G094R
TreeFamiTF105557

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

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)DescriptionActionsGraphical viewLength
Sequence conflicti367N → D in ABB22788 (PubMed:15967565).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_018561448 – 457Missing in isoform 2. 1 Publication10

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_005207693.3 [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

Similar proteinsi

Entry informationi

Entry nameiPP2BA_BOVIN
AccessioniPrimary (citable) accession number: P48452
Secondary accession number(s): Q08DM4, Q309F2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 25, 2018
This is version 156 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

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health