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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure 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

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure 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

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P48452 (PP2BA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·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

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Sequence length	521 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Function	Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1 By similarity.
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 1 Fe³⁺ ion per subunit. Binds 1 zinc ion per subunit.
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. Interacts with CHP1 and CHP2 By similarity. Interacts with CMYA5; this interaction represses calcineurin activity in muscle By similarity.
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	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara calcineurin-NFAT signaling cascade Inferred from electronic annotation. Source: Compara calcium ion transport Inferred from electronic annotation. Source: Compara cellular response to drug Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein import into nucleus Inferred from electronic annotation. Source: Compara regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: Compara regulation of synaptic transmission Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from sequence or structural similarity. Source: UniProtKB response to stress Inferred from electronic annotation. Source: Compara skeletal muscle fiber development Inferred from electronic annotation. Source: Compara transition between fast and slow fiber Inferred from electronic annotation. Source: Compara
Cellular_component	Z disc Inferred from electronic annotation. Source: Compara calcineurin complex Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calmodulin-dependent protein phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB drug binding Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 521

521

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

PRO_0000058821

Region

1 – 301

301

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 Ref.1

Metal binding

Iron

Metal binding

118

Iron

Metal binding

118

Zinc

Metal binding

150

Zinc Ref.1

Metal binding

199

Zinc Ref.1

Metal binding

281

Zinc Ref.1

Modified residue

469

Phosphoserine By similarity

Alternative sequence

448 – 457

Missing in isoform 2.

VSP_018561

Sequence conflict

367

N → D in ABB22788. Ref.2

521

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: F3F153F22AB56BDF Show »	FASTA	521	58,672
10 20 30 40 50 60 MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEETV 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 SYPAVCEFLQ 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: C383F9EF7B41D775 Show »	FASTA	511	57,643
10 20 30 40 50 60 MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEETV 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 SYPAVCEFLQ 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex." Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A., Fitzgibbon M.J., Fleming M.A., Caron P.R., Hsiao K., Navia M.A. Cell 82:507-522(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Tissue: Brain.
[2]	"Molecular cloning, expression, purification and characterization of calcineurin from bovine cardiac muscle." Selvakumar P., Lakshmikuttyamma A., Anderson D.H., Sharma R.K. Biochimie 87:975-983(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Heart muscle.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: Hereford. Tissue: Brain cortex.
+	Additional computationally mapped references.

EMBL
GenBank
DDBJ

U33868 mRNA. Translation: AAC48473.1.
DQ231569 mRNA. Translation: ABB22788.1.
BC123668 mRNA. Translation: AAI23669.1.

IPI

IPI00704314.
IPI00759423.

PIR

A56968.

RefSeq

NP_777212.1. NM_174787.2.

UniGene

Bt.3966.

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TCO	X-ray	2.50	A	18-392	[»]
2F2O	X-ray	2.17	A/B	389-413	[»]
2F2P	X-ray	2.60	A/B	389-413	[»]

ProteinModelPortal

P48452.

SMR

P48452. Positions 21-372.

ModBase

Search...

PRIDE

P48452.

StructuralBiologyKnowledgebase

Search...

Ensembl

ENSBTAT00000021305; ENSBTAP00000021305; ENSBTAG00000016005.
ENSBTAT00000056385; ENSBTAP00000047848; ENSBTAG00000016005.

GeneID

286852.

KEGG

bta:286852.

CTD

5530.

eggNOG

COG0639.

GeneTree

ENSGT00530000063087.

HOGENOM

HOG000172699.

HOVERGEN

HBG002819.

InParanoid

P48452.

K04348.

OMA

NKPNDEP.

OrthoDB

EOG4PVNZK.

Reactome

REACT_114534. Signal Transduction.

ArrayExpress

P48452.

InterPro

IPR004843. Metallo_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...

ChEMBL

CHEMBL5018.

EvolutionaryTrace

P48452.

NextBio

20806501.

Entry name

PP2BA_BOVIN

Accession

Primary (citable) accession number: P48452
Secondary accession number(s): Q08DM4, Q309F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·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: P48452-1)

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: P48452-2)

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