P20651 (PP2BB_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
EC=3.1.3.16

Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit beta isoform

Gene names

Name:

Ppp3cb

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Catalytic activity	A phosphoprotein + H2O = a protein + 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.
Sequence similarities	Belongs to the PPP phosphatase family. PP-2B subfamily.

Ontologies

Keywords
Ligand	Calmodulin-binding Iron Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	calcium ion-dependent exocytosis Inferred from sequence or structural similarity. Source: UniProtKB cellular response to drug Inferred from sequence or structural similarity. Source: UniProtKB muscle cell homeostasis Inferred from expression pattern PubMed 11997253. Source: RGD positive regulation of insulin secretion involved in cellular response to glucose stimulus Inferred from mutant phenotype PubMed 11978799. Source: UniProtKB protein dephosphorylation Inferred from direct assay PubMed 12135494. Source: RGD protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB response to amphetamine Inferred from expression pattern PubMed 11954050. Source: RGD
Cellular_component	calcineurin complex Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay PubMed 11978799. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB 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 sequence or structural similarity. Source: UniProtKB protein heterodimerization activity Inferred from direct assay PubMed 12135494. Source: RGD protein phosphatase 2B binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 525	525	Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform		PRO_0000058827
Regions
	Region	1 – 310	310	Catalytic
	Region	256 – 262	7	Calcineurin B binding-site 1 Potential
	Region	305 – 310	6	Calcineurin B binding-site 2 Potential
	Region	402 – 424	23	Calmodulin-binding Potential
	Region	475 – 497	23	Inhibitory domain
	Compositional bias	11 – 20	10	Poly-Pro
Sites
	Active site	160	1	Proton donor By similarity
	Metal binding	99	1	Iron By similarity
	Metal binding	101	1	Iron By similarity
	Metal binding	127	1	Iron By similarity
	Metal binding	127	1	Zinc By similarity
	Metal binding	159	1	Zinc By similarity
	Metal binding	208	1	Zinc By similarity
	Metal binding	290	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20651 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 5E66AF3100BE3987	FASTA	525	59,113
	10 20 30 40 50 60 MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP RVDVLKNHLV 70 80 90 100 110 120 KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI HGQFFDLMKL FEVGGSPANT 130 140 150 160 170 180 RYLFLGDYVD RGYFSIECVL YLWVLKILYP STLFLLRGNH ECRHLTEYFT FKQECKIKYS 190 200 210 220 230 240 ERVYEACMEA FDSLPLAALL NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL 250 260 270 280 290 300 WSDPSEDFGN EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY 310 320 330 340 350 360 RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY WLPNFMDVFT 370 380 390 400 410 420 WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDVGSAA ARKEIIRNKI RAIGKMARVF 430 440 450 460 470 480 SVLREESESV LTLKGLTPTG MLPSGVLAGG RQTLQSATVE AIEAEKAIRG SSPPHRICSF 490 500 510 520 EEAKGLDRIN ERMPPRKDAV QQDGFNSLNT AHTTENHGTG NHSAQ

References

[1]	"Evidence for a second isoform of the catalytic subunit of calmodulin-dependent protein phosphatase (calcineurin A)." Kuno T., Takeda T., Hirai M., Ito A., Mukai H., Tanaka C. Biochem. Biophys. Res. Commun. 165:1352-1358(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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 245-315.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M31809 mRNA. Translation: AAA40848.1. D90036 mRNA. Translation: BAA14084.1. M58441 mRNA. Translation: AAA41915.1.
IPI	IPI00201407.
PIR	A33794.
RefSeq	NP_058738.1. NM_017042.2.
UniGene	Rn.11063. Rn.136394.
3D structure databases
ProteinModelPortal	P20651.
SMR	P20651. Positions 24-381.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-66N.
STRING	10116.ENSRNOP00000010476.
PTM databases
PhosphoSite	P20651.
Proteomic databases
PaxDb	P20651.
PRIDE	P20651.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24675.
KEGG	rno:24675.
UCSC	RGD:3383. rat.
Organism-specific databases
CTD	5532.
RGD	3383. Ppp3cb.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172699.
HOVERGEN	HBG002819.
InParanoid	P20651.
KO	K04348.
OrthoDB	EOG4PVNZK.
Enzyme and pathway databases
Reactome	REACT_111984. Signal Transduction.
Gene expression databases
ArrayExpress	P20651.
Genevestigator	P20651.
GermOnline	ENSRNOG00000007757. Rattus norvegicus.
Family and domain databases
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...
Other
NextBio	604059.

Entry information

Entry name

PP2BB_RAT

Accession

Primary (citable) accession number: P20651
Secondary accession number(s): Q6LDJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program