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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Preferred order of sections

With

Entry

#Exp.

IntAct

Notes

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

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P63329 (PP2BA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Protein names

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 names

Name:	Ppp3ca
Synonyms:	Calna

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Sequence length	521 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Function	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. Ref.2
Catalytic activity	[a protein]-serine/threonine phosphate + H₂O = [a protein]-serine/threonine + phosphate.
Cofactor	Binds 1 Fe³⁺ ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	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 By similarity. Interacts with CHP1 and CHP2. Interacts with CMYA5; this interaction represses calcineurin activity in muscle By similarity. Ref.6 Ref.7
Subcellular location	Nucleus By similarity. Note: Colocalizes with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-2B subfamily.

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Calmodulin-binding Iron Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Nitration
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Ensembl calcineurin-NFAT signaling cascade Inferred from electronic annotation. Source: Ensembl calcium ion transport Inferred from electronic annotation. Source: Ensembl cellular response to drug Inferred from electronic annotation. Source: Ensembl cellular response to glucose stimulus Inferred from mutant phenotype PubMed 19965390. Source: BHF-UCL multicellular organismal response to stress Inferred from electronic annotation. Source: Ensembl negative regulation of calcium ion-dependent exocytosis Inferred by curator PubMed 19965390. Source: BHF-UCL negative regulation of insulin secretion Inferred from mutant phenotype PubMed 19965390. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Ensembl protein dephosphorylation Inferred from direct assay PubMed 12135494 Ref.2. Source: RGD protein import into nucleus Inferred from electronic annotation. Source: Ensembl regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: Ensembl regulation of synaptic transmission Inferred from electronic annotation. Source: Ensembl response to amphetamine Inferred from expression pattern PubMed 11954050. Source: RGD response to calcium ion Inferred from sequence or structural similarity. Source: UniProtKB skeletal muscle fiber development Inferred from electronic annotation. Source: Ensembl transition between fast and slow fiber Inferred from electronic annotation. Source: Ensembl
Cellular_component	Z disc Inferred from electronic annotation. Source: Ensembl calcineurin complex Inferred from direct assay PubMed 12135494. Source: RGD cytosol Inferred from direct assay PubMed 16150427. Source: RGD membrane Inferred from direct assay PubMed 16150427. Source: RGD mitochondrion Inferred from electronic annotation. Source: Ensembl nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calmodulin binding Inferred from direct assay PubMed 12135494. Source: RGD calmodulin-dependent protein phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB drug binding Inferred from electronic annotation. Source: Ensembl metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activity Inferred from direct assay PubMed 12135494. Source: RGD
Complete GO annotation...

With	Entry	#Exp.	IntAct	Notes
Cacna1c	P22002	5	EBI-7022944,EBI-1185084

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Initiator methionine

Removed By similarity

Chain

2 – 521

520

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

PRO_0000058824

Region

2 – 301

300

Catalytic

Region

247 – 253

Calcineurin B binding-site 1 Potential

Region

296 – 301

Calcineurin B binding-site 2 Potential

Region

392 – 414

Calmodulin-binding Potential

Region

465 – 487

Inhibitory domain

Active site

151

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

118

Iron By similarity

Metal binding

118

Zinc By similarity

Metal binding

150

Zinc By similarity

Metal binding

199

Zinc By similarity

Metal binding

281

Zinc By similarity

Modified residue

N-acetylserine By similarity

Modified residue

224

Nitrated tyrosine By similarity

Alternative sequence

448 – 457

Missing in isoform 2.

VSP_018564

521

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 16530C27DDBF1F05 Show »	FASTA	521	58,644
10 20 30 40 50 60 MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV 70 80 90 100 110 120 ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV 130 140 150 160 170 180 DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD 190 200 210 220 230 240 AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG 250 260 270 280 290 300 NEKTQEHFTH NTVRGCSYFY SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 310 320 330 340 350 360 SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK 370 380 390 400 410 420 VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV 430 440 450 460 470 480 LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN 490 500 510 520 ERMPPRRDAM PSDANLNSIN KALASETNGT DSNGSNSSNI Q « Hide
Isoform 2 [UniParc]. Checksum: 01428D70D67450BD Show »	FASTA	511	57,615
10 20 30 40 50 60 MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV 70 80 90 100 110 120 ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV 130 140 150 160 170 180 DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD 190 200 210 220 230 240 AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG 250 260 270 280 290 300 NEKTQEHFTH NTVRGCSYFY SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 310 320 330 340 350 360 SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK 370 380 390 400 410 420 VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV 430 440 450 460 470 480 LTLKGLTPTG MLPSGVLSGG KQTLQSAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM 490 500 510 PSDANLNSIN KALASETNGT DSNGSNSSNI Q « Hide

[1]	"The complete primary structure of calcineurin A, a calmodulin binding protein homologous with protein phosphatases 1 and 2A." Ito A., Hashimoto T., Hirai M., Takeda T., Shuntoh H., Kuno T., Tanaka C. Biochem. Biophys. Res. Commun. 163:1492-1497(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Characterization of the phosphatase activity of a baculovirus-expressed calcineurin A isoform." Perrino B.A., Fong Y.L., Brickey D.A., Saitoh Y., Ushio Y., Fukunaga K., Miyamoto E., Soderling T.R. J. Biol. Chem. 267:15965-15969(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
[3]	"Molecular cloning and characterization of the promoter region of the calcineurin A alpha gene." Chang C., Takeda T., Mukai H., Shuntoh H., Kuno T., Tanaka C. Biochem. J. 288:801-805(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19. Tissue: Liver.
[4]	Lubec G., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 143-148, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain.
[5]	"Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells." Wadzinski B.E., Heasley L.E., Johnson G.L. J. Biol. Chem. 265:21504-21508(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 236-306.
[6]	"Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein." Lin X., Sikkink R.A., Rusnak F., Barber D.L. J. Biol. Chem. 274:36125-36131(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHP1.
[7]	"CHP2 activates the calcineurin/nuclear factor of activated T cells signaling pathway and enhances the oncogenic potential of HEK293 cells." Li G.D., Zhang X., Li R., Wang Y.D., Wang Y.L., Han K.J., Qian X.P., Yang C.G., Liu P., Wei Q., Chen W.F., Zhang J., Zhang Y. J. Biol. Chem. 283:32660-32668(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHP2.
+	Additional computationally mapped references.

EMBL
GenBank
DDBJ

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.

PIR

A33264.

RefSeq

NP_058737.1. NM_017041.1.

UniGene

Rn.6866.

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4IL1	X-ray	3.00	A/B/C/D	1-492	[»]

ProteinModelPortal

P63329.

SMR

P63329. Positions 1-411.

ModBase

Search...

MobiDB

Search...

BioGrid

246806. 3 interactions.

IntAct

P63329. 1 interaction.

MINT

MINT-4106043.

PhosphoSite

P63329.

PaxDb

P63329.

PRIDE

P63329.

StructuralBiologyKnowledgebase

Search...

Ensembl

ENSRNOT00000047975; ENSRNOP00000049674; ENSRNOG00000009882.

GeneID

24674.

KEGG

rno:24674.

CTD

5530.

RGD

3382. Ppp3ca.

eggNOG

COG0639.

GeneTree

ENSGT00530000063087.

HOGENOM

HOG000172699.

HOVERGEN

HBG002819.

InParanoid

P63329.

K04348.

OMA

RTKPNIQ.

OrthoDB

EOG7BZVSC.

Reactome

REACT_111984. Signal Transduction.

Genevestigator

P63329.

InterPro

IPR004843. PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

PRINTS

PR00114. STPHPHTASE.

SMART

SM00156. PP2Ac. 1 hit.
[Graphical view]

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

NextBio

295542.

Entry name

PP2BA_RAT

Accession

Primary (citable) accession number: P63329
Secondary accession number(s): P12816

Q9Z1I5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	February 19, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P63329-1)

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.

Isoform 2 (identifier: P63329-2)

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