UniProtKB - P63329 (PP2BA_RAT)
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Protein
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
Gene
Ppp3ca
Organism
Rattus norvegicus (Rat)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 90 | IronBy similarity | 1 | |
Metal bindingi | 92 | IronBy similarity | 1 | |
Metal bindingi | 118 | IronBy similarity | 1 | |
Metal bindingi | 118 | ZincBy similarity | 1 | |
Metal bindingi | 150 | ZincBy similarity | 1 | |
Active sitei | 151 | Proton donorBy similarity | 1 | |
Metal bindingi | 199 | ZincBy similarity | 1 | |
Metal bindingi | 281 | ZincBy similarity | 1 |
GO - Molecular functioni
- calcium-dependent protein serine/threonine phosphatase activity Source: RGD
- calmodulin binding Source: RGD
- calmodulin-dependent protein phosphatase activity Source: UniProtKB
- cyclosporin A binding Source: RGD
- drug binding Source: RGD
- enzyme binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- phosphoprotein phosphatase activity Source: RGD
- protein dimerization activity Source: RGD
- protein heterodimerization activity Source: RGD
- protein serine/threonine phosphatase activity Source: RGD
GO - Biological processi
- calcineurin-NFAT signaling cascade Source: RGD
- calcium ion transport Source: RGD
- calcium-mediated signaling Source: RGD
- cardiac muscle hypertrophy in response to stress Source: RGD
- cellular response to drug Source: RGD
- cellular response to glucose stimulus Source: BHF-UCL
- dephosphorylation Source: RGD
- excitatory postsynaptic potential Source: RGD
- G1/S transition of mitotic cell cycle Source: RGD
- modulation of chemical synaptic transmission Source: RGD
- multicellular organismal response to stress Source: RGD
- negative regulation of calcium ion-dependent exocytosis Source: BHF-UCL
- negative regulation of chromatin binding Source: RGD
- negative regulation of dendrite morphogenesis Source: RGD
- negative regulation of gene expression Source: RGD
- negative regulation of insulin secretion Source: BHF-UCL
- negative regulation of production of miRNAs involved in gene silencing by miRNA Source: RGD
- positive regulation of cardiac muscle hypertrophy Source: RGD
- positive regulation of cardiac muscle hypertrophy in response to stress Source: RGD
- positive regulation of connective tissue replacement Source: RGD
- positive regulation of DNA binding transcription factor activity Source: RGD
- positive regulation of endocytosis Source: RGD
- positive regulation of gene expression Source: RGD
- positive regulation of NFAT protein import into nucleus Source: RGD
- positive regulation of transcription by RNA polymerase II Source: RGD
- protein dephosphorylation Source: RGD
- protein import into nucleus Source: RGD
- response to amphetamine Source: RGD
- response to calcium ion Source: UniProtKB
- skeletal muscle fiber development Source: RGD
- transition between fast and slow fiber Source: RGD
Keywordsi
Molecular function | Calmodulin-binding, Hydrolase, Protein phosphatase |
Ligand | Iron, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.1.3.16. 5301. |
Reactomei | R-RNO-2025928. Calcineurin activates NFAT. 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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3382. Ppp3ca. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000058824 | 2 – 521 | Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoformAdd BLAST | 520 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineBy similarity | 1 | |
Modified residuei | 224 | Nitrated tyrosineBy similarity | 1 | |
Modified residuei | 469 | PhosphoserineCombined sources | 1 | |
Modified residuei | 492 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Acetylation, Nitration, PhosphoproteinProteomic databases
PaxDbi | P63329. |
PRIDEi | P63329. |
PTM databases
iPTMneti | P63329. |
PhosphoSitePlusi | P63329. |
SwissPalmi | P63329. |
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. Interacts (constitutively active form) with SYNPO2 (By similarity).By similarity2 Publications
Binary interactionsi
GO - Molecular functioni
- calmodulin binding Source: RGD
- enzyme binding Source: RGD
- protein dimerization activity Source: RGD
- protein heterodimerization activity Source: RGD
Protein-protein interaction databases
BioGridi | 246806. 4 interactors. |
CORUMi | P63329. |
IntActi | P63329. 4 interactors. |
MINTi | P63329. |
STRINGi | 10116.ENSRNOP00000049674. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 31 – 34 | Combined sources | 4 | |
Helixi | 43 – 51 | Combined sources | 9 | |
Helixi | 58 – 72 | Combined sources | 15 | |
Beta strandi | 77 – 81 | Combined sources | 5 | |
Beta strandi | 83 – 88 | Combined sources | 6 | |
Helixi | 95 – 105 | Combined sources | 11 | |
Turni | 108 – 110 | Combined sources | 3 | |
Beta strandi | 113 – 115 | Combined sources | 3 | |
Beta strandi | 120 – 123 | Combined sources | 4 | |
Helixi | 126 – 139 | Combined sources | 14 | |
Turni | 141 – 143 | Combined sources | 3 | |
Beta strandi | 144 – 146 | Combined sources | 3 | |
Helixi | 154 – 159 | Combined sources | 6 | |
Helixi | 162 – 168 | Combined sources | 7 | |
Helixi | 172 – 184 | Combined sources | 13 | |
Beta strandi | 188 – 191 | Combined sources | 4 | |
Turni | 192 – 194 | Combined sources | 3 | |
Beta strandi | 195 – 200 | Combined sources | 6 | |
Helixi | 209 – 213 | Combined sources | 5 | |
Beta strandi | 218 – 220 | Combined sources | 3 | |
Beta strandi | 223 – 225 | Combined sources | 3 | |
Helixi | 226 – 232 | Combined sources | 7 | |
Turni | 237 – 240 | Combined sources | 4 | |
Beta strandi | 247 – 250 | Combined sources | 4 | |
Turni | 252 – 255 | Combined sources | 4 | |
Beta strandi | 256 – 260 | Combined sources | 5 | |
Helixi | 262 – 271 | Combined sources | 10 | |
Beta strandi | 275 – 279 | Combined sources | 5 | |
Beta strandi | 287 – 290 | Combined sources | 4 | |
Turni | 295 – 297 | Combined sources | 3 | |
Beta strandi | 299 – 306 | Combined sources | 8 | |
Helixi | 311 – 313 | Combined sources | 3 | |
Beta strandi | 319 – 325 | Combined sources | 7 | |
Beta strandi | 328 – 334 | Combined sources | 7 | |
Helixi | 344 – 346 | Combined sources | 3 | |
Helixi | 349 – 366 | Combined sources | 18 | |
Helixi | 473 – 476 | Combined sources | 4 | |
Helixi | 478 – 481 | Combined sources | 4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4IL1 | X-ray | 3.00 | A/B/C/D | 1-492 | [»] | |
ProteinModelPortali | P63329. | |||||
SMRi | P63329. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 301 | CatalyticAdd BLAST | 300 | |
Regioni | 247 – 253 | Calcineurin B binding-site 1Sequence analysis | 7 | |
Regioni | 296 – 301 | Calcineurin B binding-site 2Sequence analysis | 6 | |
Regioni | 392 – 414 | Calmodulin-bindingSequence analysisAdd BLAST | 23 | |
Regioni | 465 – 487 | Inhibitory domainAdd BLAST | 23 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0375. Eukaryota. COG0639. LUCA. |
GeneTreei | ENSGT00530000063087. |
HOGENOMi | HOG000172699. |
HOVERGENi | HBG002819. |
InParanoidi | P63329. |
KOi | K04348. |
OMAi | LWSLKIW. |
OrthoDBi | EOG091G094R. |
PhylomeDBi | P63329. |
Family and domain databases
Gene3Di | 3.60.21.10. 1 hit. |
InterProi | View protein in InterPro IPR004843. Calcineurin-like_PHP_ApaH. IPR029052. Metallo-depent_PP-like. IPR006186. Ser/Thr-sp_prot-phosphatase. |
Pfami | View protein in Pfam PF00149. Metallophos. 1 hit. |
PRINTSi | PR00114. STPHPHTASE. |
SMARTi | View protein in SMART SM00156. PP2Ac. 1 hit. |
PROSITEi | View protein in PROSITE PS00125. SER_THR_PHOSPHATASE. 1 hit. |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative 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.
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
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_018564 | 448 – 457 | Missing in isoform 2. 1 Publication | 10 |
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. |
PIRi | A33264. |
RefSeqi | NP_058737.1. NM_017041.1. [P63329-1] XP_006233425.1. XM_006233363.3. [P63329-2] |
UniGenei | Rn.228648. Rn.6866. |
Genome annotation databases
Ensembli | ENSRNOT00000047975; ENSRNOP00000049674; ENSRNOG00000009882. [P63329-1] |
GeneIDi | 24674. |
KEGGi | rno:24674. |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | PP2BA_RAT | |
Accessioni | P63329Primary (citable) accession number: P63329 Secondary accession number(s): P12816 Q9Z1I5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 11, 2004 |
Last sequence update: | October 11, 2004 | |
Last modified: | March 28, 2018 | |
This is version 126 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |