Serine/threonine-protein phosphatase 2B catalytic subunit A1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P23287 (PP2B1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit A1
EC=3.1.3.16

Alternative name(s):
Calcineurin A1
Calmodulin-binding protein 1

Gene names

Name:	CNA1
Synonyms:	CMP1
Ordered Locus Names:	YLR433C
ORF Names:	L9753.6

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
Miscellaneous	Present with 7040 molecules/cell in log phase SD medium.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Inferred from mutant phenotype Ref.1. Source: SGD cellular ion homeostasis Inferred from mutant phenotype PubMed 8798496. Source: SGD fungal-type cell wall organization Inferred from genetic interaction PubMed 7530227. Source: SGD
Cellular_component	calcineurin complex Inferred from direct assay PubMed 1321337. Source: SGD cytoplasm Traceable author statement PubMed 9123967. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CMD1	P06787	4	EBI-12771,EBI-3976

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 553

553

Serine/threonine-protein phosphatase 2B catalytic subunit A1

PRO_0000058836

Sites

Active site

180

Proton donor By similarity

Metal binding

119

Iron By similarity

Metal binding

121

Iron By similarity

Metal binding

147

Iron By similarity

Metal binding

147

Zinc By similarity

Metal binding

179

Zinc By similarity

Metal binding

228

Zinc By similarity

Metal binding

317

Zinc By similarity

Natural variations

Natural variant

45 – 46

PI → SY in strain: S288c / GRF88.

Secondary structure

553

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23287 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: D5D6F91CC0BD277B
Show »

FASTA

553

63,002

        10         20         30         40         50         60 
MSKDLNSSRI KIIKPNDSYI KVDRKKDLTK YELENGKVIS TKDRPIASVP AITGKIPSDE 

        70         80         90        100        110        120 
EVFDSKTGLP NHSFLREHFF HEGRLSKEQA IKILNMSTVA LSKEPNLLKL KAPITICGDI 

       130        140        150        160        170        180 
HGQYYDLLKL FEVGGDPAEI DYLFLGDYVD RGAFSFECLI YLYSLKLNNL GRFWMLRGNH 

       190        200        210        220        230        240 
ECKHLTSYFT FKNEMLHKYD MEVYDACCRS FNVLPLAALM NGQYFCVHGG ISPELKSVED 

       250        260        270        280        290        300 
VNKINRFREI PSRGLMCDLL WADPVENYDD ARDGSEFDQS EDEFVPNSLR GCSFAFTFKA 

       310        320        330        340        350        360 
SCKFLKANGL LSIIRAHEAQ DAGYRMYKNN KVTGFPSLIT MFSAPNYLDT YHNKAAVLKY 

       370        380        390        400        410        420 
EENVMNIRQF HMSPHPYWLP DFMDVFTWSL PFVGEKVTSM LVSILNICSE QELDPESEPK 

       430        440        450        460        470        480 
AAEETVKARA NATKETGTPS DEKASSAILE DETRRKALRN KILAIAKVSR MFSVLREESE 

       490        500        510        520        530        540 
KVEYLKTMNA GVLPRGALAR GTEGLNETLS TFEKARKEDL INEKLPPSLS EVEQEKIKYY 

       550 
EKILKGAEKK PQL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase." Cyert M.S., Kunisawa R., Kaim D., Thorner J. Proc. Natl. Acad. Sci. U.S.A. 88:7376-7380(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[2]	"Identification and molecular characterization of the calmodulin-binding subunit gene (CMP1) of protein phosphatase 2B from Saccharomyces cerevisiae. An alpha-factor inducible gene." Ye R.R., Bretscher A. Eur. J. Biochem. 204:713-723(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 20B-12.
[3]	"The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B." Liu Y., Ishii S., Tokai M., Tsutsumi H., Ohki O., Akada R., Tanaka K., Tsuchiya E., Fukui S., Miyakawa T. Mol. Gen. Genet. 227:52-59(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M64839 Genomic DNA. Translation: AAA34465.1.
X66490 Genomic DNA. Translation: CAA47117.1.
X54963 Genomic DNA. Translation: CAA38711.1.
U21094 Genomic DNA. Translation: AAB67518.1.
AY693079 Genomic DNA. Translation: AAT93098.1.
BK006945 Genomic DNA. Translation: DAA09734.1.

PIR

S16809.

RefSeq

NP_013537.1. NM_001182321.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LHI	NMR	-	A	453-476	[»]

ProteinModelPortal

P23287.

SMR

P23287. Positions 60-408.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-662N.

IntAct

P23287. 24 interactions.

MINT

MINT-397444.

STRING

4932.YLR433C.

Proteomic databases

PaxDb

P23287.

PeptideAtlas

P23287.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR433C; YLR433C; YLR433C.

GeneID

851153.

KEGG

sce:YLR433C.

Organism-specific databases

CYGD

YLR433c.

SGD

S000004425. CNA1.

Phylogenomic databases

eggNOG

COG0639.

GeneTree

ENSGT00530000063087.

HOGENOM

HOG000172699.

K04348.

OMA

PRKDGVN.

OrthoDB

EOG45XC4G.

Gene expression databases

Genevestigator

P23287.

GermOnline

YLR433C. Saccharomyces cerevisiae.

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

967933.

Entry information

Entry name

PP2B1_YEAST

Accession

Primary (citable) accession number: P23287
Secondary accession number(s): D6VZ68

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents