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IID00069
 UniprotQ08209
ProteinSerine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
GenePPP3CA
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
521
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-370 Hetero trimer : IID00060Complex,IID00435Complex
 Evidence X-RAY 5sve A Reference
       Region 5sve A 1-10 disorder
       Region 5sve A 11-370 order
Seq 1-370 Hetero trimer : IID00060Complex,IID90028Complex
 Evidence X-RAY 4f0z A Reference
       Region 4f0z A 1-13 disorder
       Region 4f0z A 14-370 order
Seq 1-372 Hetero hexamer : IID00060Complex,P62937
 Evidence X-RAY 1m63 E Reference
       Region 1m63 E 1-13 disorder
       Region 1m63 E 14-372 order
 Evidence X-RAY 1m63 A Reference
       Region 1m63 A 1-372 order
Seq 1-380 Hetero pentamer : IID00060Complex
 Evidence X-RAY 2p6b C Reference
       Region 2p6b C 1-13 disorder
       Region 2p6b C 14-370 order
       Region 2p6b C 371-380 disorder
 Evidence X-RAY 2p6b A Reference
       Region 2p6b A 1-13 disorder
       Region 2p6b A 14-370 order
       Region 2p6b A 371-380 disorder
Seq 1-521 Hetero dimer : IID00060Complex
 Evidence X-RAY 3ll8 C Reference
       Region 3ll8 C 14-370 order
 Evidence X-RAY 1aui A Reference
       Region 1aui A 1-13 disorder
       Region 1aui A 14-373 order
       Region 1aui A 374-468 disorder
       Region 1aui A 469-486 order
       Region 1aui A 487-521 disorder
Seq 2-346 Monomer :
 Evidence X-RAY 5c1v B Reference
       Region 5c1v B 2-22 disorder
       Region 5c1v B 23-282 order
       Region 5c1v B 283-289 disorder
       Region 5c1v B 290-340 order
       Region 5c1v B 341-346 disorder
 Evidence X-RAY 5c1v A Reference
       Region 5c1v A 2-23 disorder
       Region 5c1v A 24-340 order
       Region 5c1v A 341-346 disorder
Seq 14-370 Hetero trimer : IID00060Complex,IID00233Complex
 Evidence X-RAY 3ll8 A Reference
       Region 3ll8 A 14-370 order
Seq 20-392 Hetero trimer : IID00060Complex,P62937
 Evidence X-RAY 1mf8 A Reference
       Region 1mf8 A 20-371 order
       Region 1mf8 A 372-392 disorder
Seq 21-347 Hetero dimer :
 Evidence NMR 2jog A Reference
       Region 2jog A 21-347 order
Seq 389-413 Hetero tetramer : IID00706Complex
 Evidence X-RAY 2r28 D Reference
       Region 2r28 D 389-392 disorder
       Region 2r28 D 393-411 order
       Region 2r28 D 412-413 disorder
 Evidence X-RAY 2r28 C Reference
       Region 2r28 C 389-395 disorder
       Region 2r28 C 396-410 order
       Region 2r28 C 411-413 disorder
Seq 391-414 Hetero dimer : IID00706Complex
 Evidence NMR 2jzi B Reference
       Region 2jzi B 391-414 order
 Evidence X-RAY 4q5u C Reference
       Region 4q5u C 391-414 order
Seq 395-411 Hetero octamer : IID00706Complex
 Evidence X-RAY 2w73 K Reference
       Region 2w73 K 395-411 order
 Evidence X-RAY 2w73 L Reference
       Region 2w73 L 395-411 order
 Evidence X-RAY 2w73 M Reference
       Region 2w73 M 395-411 order
 Evidence X-RAY 2w73 O Reference
       Region 2w73 O 395-411 order
SeqProS verified 391-414 Hetero octamer : IID00706Complex
       Region 2w73 K 395-411 order
       Region 2w73 L 395-411 order
       Region 2w73 M 395-411 order
       Region 2w73 O 395-411 order
       Region 1aui A 374-468 disorder
SeqProS verified 391-414 Hetero tetramer : IID00706Complex
       Region 2r28 C 396-410 order
       Region 2r28 D 393-411 order
       Region 1aui A 374-468 disorder
SeqProS verified 391-414 Hetero dimer : IID00706Complex
       Region 2jzi B 391-414 order
       Region 4q5u C 391-414 order
       Region 1aui A 374-468 disorder
Seqphosphorylation
    469-469 Phosphoserine
    492-492 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
 
Prediction
NeProc
Disorder 1-9,375-391,400-416,425-428,436-441,482-521
Order 10-374,392-399,417-424,429-435,442-481
ProS 400-416,425-428,436-441,482-487,518-521
AlphaFold
Disorder 1-8,372-389,425-433,454-465,487-521
Order 9-371,390-424,434-453,466-486
Pfam Hmmer
PF00149 83-285 2e-36
SEG 504-519
Function
Function in SwissProt
Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals (PubMed:15671020, PubMed:18838687, PubMed:19154138, PubMed:23468591). Many of the substrates contain a PxIxIT motif and/or a LxVP motif (PubMed:17498738, PubMed:17502104, PubMed:23468591, PubMed:27974827, PubMed:22343722). In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation (PubMed:15671020). In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion (PubMed:18838687). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 (PubMed:19154138). In response to increased Ca(2+) levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation (PubMed:26248042). Dephosphorylates and inactivates transcription factor ELK1 (PubMed:19154138). Dephosphorylates DARPP32 (PubMed:19154138). May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins (PubMed:30611118). Dephosphorylates transcription factor TFEB at 'Ser-211' following Coxsackievirus B3 infection, promoting nuclear translocation (PubMed:33691586).
Biological Process
Diagram with PDB data
PPP3CA/CALM1Structure of calmodulin bound to its recognition site from calcineurin
PPP3CA/RCAN1Structure of Calcineurin bound to RCAN1
See also
Diagram with PDB data
NFATC1/PPP3CA/PPP3R1Structure of Calcineurin in complex with NFATc1 LxVP peptide