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Protein

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

Gene

Ppp3ca

Organism
Rattus norvegicus (Rat)
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 similarity1 Publication

Catalytic activityi

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi90IronBy similarity1
Metal bindingi92IronBy similarity1
Metal bindingi118IronBy similarity1
Metal bindingi118ZincBy similarity1
Metal bindingi150ZincBy similarity1
Active sitei151Proton donorBy similarity1
Metal bindingi199ZincBy similarity1
Metal bindingi281ZincBy similarity1

GO - Molecular functioni

  • calcium-dependent protein serine/threonine phosphatase activity Source: RGD
  • calmodulin binding Source: RGD
  • calmodulin-dependent protein phosphatase activity Source: UniProtKB
  • drug binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • phosphoprotein phosphatase activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein serine/threonine phosphatase activity Source: RGD

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. 5301.
ReactomeiR-RNO-180024. DARPP-32 events.
R-RNO-2871809. FCERI mediated Ca+2 mobilization.
R-RNO-4086398. Ca2+ pathway.
R-RNO-5607763. CLEC7A (Dectin-1) induces NFAT activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC:3.1.3.16)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit alpha isoform
Gene namesi
Name:Ppp3ca
Synonyms:Calna
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi3382. Ppp3ca.

Subcellular locationi

GO - Cellular componenti

  • calcineurin complex Source: RGD
  • cytosol Source: RGD
  • membrane Source: RGD
  • mitochondrion Source: Ensembl
  • nucleoplasm Source: Ensembl
  • postsynapse Source: GOC
  • sarcolemma Source: UniProtKB-SubCell
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000588242 – 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 residuei469PhosphoserineCombined sources1
Modified residuei492PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP63329.
PRIDEiP63329.

PTM databases

iPTMnetiP63329.
PhosphoSitePlusiP63329.
SwissPalmiP63329.

Expressioni

Gene expression databases

BgeeiENSRNOG00000009882.
GenevisibleiP63329. RN.

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 CIB1; the interaction increases upon cardiomyocytes hypertrophy. Interacts with CMYA5; this interaction represses calcineurin activity in muscle (By similarity). Interacts with CHP1 and CHP2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cacna1cP220025EBI-7022944,EBI-1185084
Cacng8Q8VHW56EBI-7022944,EBI-9086576

GO - Molecular functioni

  • calmodulin binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi246806. 3 interactors.
IntActiP63329. 4 interactors.
MINTiMINT-4106043.
STRINGi10116.ENSRNOP00000049674.

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 – 72Combined sources15
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 – 168Combined sources7
Helixi172 – 184Combined sources13
Beta strandi188 – 191Combined sources4
Turni192 – 194Combined sources3
Beta strandi195 – 200Combined sources6
Helixi209 – 213Combined sources5
Beta strandi218 – 220Combined sources3
Beta strandi223 – 225Combined sources3
Helixi226 – 232Combined sources7
Turni237 – 240Combined sources4
Beta strandi247 – 250Combined sources4
Turni252 – 255Combined sources4
Beta strandi256 – 260Combined sources5
Helixi262 – 271Combined sources10
Beta strandi275 – 279Combined sources5
Beta strandi287 – 290Combined sources4
Turni295 – 297Combined sources3
Beta strandi299 – 306Combined sources8
Helixi311 – 313Combined sources3
Beta strandi319 – 325Combined sources7
Beta strandi328 – 334Combined sources7
Helixi344 – 346Combined sources3
Helixi349 – 366Combined sources18
Helixi473 – 476Combined sources4
Helixi478 – 481Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IL1X-ray3.00A/B/C/D1-492[»]
ProteinModelPortaliP63329.
SMRiP63329.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiP63329.
KOiK04348.
OMAiELICEGD.
OrthoDBiEOG091G094R.
PhylomeDBiP63329.

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: P63329-1) [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
MKEGRLEESV 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 SYPAVCDFLQ 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):58,644
Last modified:October 11, 2004 - v1
Checksum:i16530C27DDBF1F05
GO
Isoform 2 (identifier: P63329-2) [UniParc]FASTAAdd to basket

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

Show »
Length:511
Mass (Da):57,615
Checksum:i01428D70D67450BD
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_018564448 – 457Missing in isoform 2. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90035 mRNA. Translation: BAA14083.1.
M29275 mRNA. Translation: AAA40940.1.
X57115 mRNA. Translation: CAA40398.2.
D10480 Genomic DNA. Translation: BAA01283.1.
M58440 mRNA. Translation: AAA41914.1.
PIRiA33264.
RefSeqiNP_058737.1. NM_017041.1. [P63329-1]
XP_006233425.1. XM_006233363.3. [P63329-2]
UniGeneiRn.228648.
Rn.6866.

Genome annotation databases

EnsembliENSRNOT00000047975; ENSRNOP00000049674; ENSRNOG00000009882. [P63329-1]
GeneIDi24674.
KEGGirno:24674.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90035 mRNA. Translation: BAA14083.1.
M29275 mRNA. Translation: AAA40940.1.
X57115 mRNA. Translation: CAA40398.2.
D10480 Genomic DNA. Translation: BAA01283.1.
M58440 mRNA. Translation: AAA41914.1.
PIRiA33264.
RefSeqiNP_058737.1. NM_017041.1. [P63329-1]
XP_006233425.1. XM_006233363.3. [P63329-2]
UniGeneiRn.228648.
Rn.6866.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IL1X-ray3.00A/B/C/D1-492[»]
ProteinModelPortaliP63329.
SMRiP63329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246806. 3 interactors.
IntActiP63329. 4 interactors.
MINTiMINT-4106043.
STRINGi10116.ENSRNOP00000049674.

PTM databases

iPTMnetiP63329.
PhosphoSitePlusiP63329.
SwissPalmiP63329.

Proteomic databases

PaxDbiP63329.
PRIDEiP63329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000047975; ENSRNOP00000049674; ENSRNOG00000009882. [P63329-1]
GeneIDi24674.
KEGGirno:24674.

Organism-specific databases

CTDi5530.
RGDi3382. Ppp3ca.

Phylogenomic databases

eggNOGiKOG0375. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP63329.
KOiK04348.
OMAiELICEGD.
OrthoDBiEOG091G094R.
PhylomeDBiP63329.

Enzyme and pathway databases

BRENDAi3.1.3.16. 5301.
ReactomeiR-RNO-180024. DARPP-32 events.
R-RNO-2871809. FCERI mediated Ca+2 mobilization.
R-RNO-4086398. Ca2+ pathway.
R-RNO-5607763. CLEC7A (Dectin-1) induces NFAT activation.

Miscellaneous databases

PROiP63329.

Gene expression databases

BgeeiENSRNOG00000009882.
GenevisibleiP63329. RN.

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...

Entry informationi

Entry nameiPP2BA_RAT
AccessioniPrimary (citable) accession number: P63329
Secondary accession number(s): P12816
, P20652, Q6LDJ8, Q9WUV7, Q9Z1I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 116 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.