Serine/threonine-protein phosphatase 2A activator 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40454 (PTPA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. 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 2A activator 1
EC=5.2.1.8

Alternative name(s):
Peptidyl-prolyl cis-trans isomerase PTPA-1
Short name=PPIase PTPA-1
Short name=Rotamase PTPA-1
Phosphotyrosyl phosphatase activator 1

Gene names

Name:	RRD1
Synonyms:	NCS1, YPA1
Ordered Locus Names:	YIL153W

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	393 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg²⁺ by dissociating the inactive form from the complex. Involved in the regulation of cell cycle progression, mitotic spindle formation, bud morphogenesis and DNA repair. Ref.3 Ref.4 Ref.5 Ref.8 Ref.10 Ref.11
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with the phosphatase PP2A-like catalytic subunits PPG1, PPH3 and SIT4. Forms a ternary complex with SIT4-TAP42. Ref.4 Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Nucleus Ref.6 Ref.8.
Miscellaneous	Present with 4590 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the PTPA-type PPIase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from mutant phenotype Ref.8 PubMed 9705277. Source: SGD G1/S transition of mitotic cell cycle Inferred from physical interaction Ref.4. Source: SGD mitotic spindle organization in nucleus Inferred from mutant phenotype Ref.3. Source: SGD protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter in response to stress Inferred from mutant phenotype PubMed 21129186. Source: SGD response to osmotic stress Inferred from genetic interaction PubMed 10660069. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: SGD nucleus Inferred from direct assay Ref.8. Source: SGD
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.11. Source: SGD phosphatase activator activity Inferred from electronic annotation. Source: InterPro protein phosphatase type 2A regulator activity Inferred from mutant phenotype Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSY2	P40164	3	EBI-25278,EBI-29107
SIT4	P20604	4	EBI-25278,EBI-13707

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 393

393

Serine/threonine-protein phosphatase 2A activator 1

PRO_0000202955

Amino acid modifications

Modified residue

341

Phosphoserine Ref.12

Experimental info

Mutagenesis

205

D → G: Abolishes PPIase activity and fails to activate PP2A phosphatases. Ref.11

Secondary structure

393

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40454 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 22F52B3359739B6E
Show »

FASTA

393

45,082

        10         20         30         40         50         60 
MSLDRVDWPH ATFSTPVKRI FDTQTTLDFQ SSLAIHRIKY HLHKYTTLIS HCSDPDPHAT 

        70         80         90        100        110        120 
ASSIAMVNGL MGVLDKLAHL IDETPPLPGP RRYGNLACRE WHHKLDERLP QWLQEMLPSE 

       130        140        150        160        170        180 
YHEVVPELQY YLGNSFGSST RLDYGTGHEL SFMATVAALD MLGMFPHMRG ADVFLLFNKY 

       190        200        210        220        230        240 
YTIMRRLILT YTLEPAGSHG VWGLDDHFHL VYILGSSQWQ LLDAQAPLQP REILDKSLVR 

       250        260        270        280        290        300 
EYKDTNFYCQ GINFINEVKM GPFEEHSPIL YDIAVTVPRW SKVCKGLLKM YSVEVLKKFP 

       310        320        330        340        350        360 
VVQHFWFGTG FFPWVNIQNG TDLPVFEEKE EESIEQANAG SPGREQTSTR FPTSTSMPPP 

       370        380        390 
GVPPSGNNIN YLLSHQNQSH RNQTSFSRDR LRR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations." Van Hoof C., Janssens V., De Baere I., Stark M.J.R., de Winde J.H., Winderickx J., Thevelein J.M., Merlevede W., Goris J. Exp. Cell Res. 264:372-387(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae." Mitchell D.A., Sprague G.F. Jr. Mol. Cell. Biol. 21:488-500(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SIT4.
[5]	"A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo." Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I., Zaragoza K., Juno C., Ogris E. Genes Dev. 17:2138-2150(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[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].
[8]	"The yeast phosphotyrosyl phosphatase activator protein, yPtpa1/Rrd1, interacts with Sit4 phosphatase to mediate resistance to 4-nitroquinoline-1-oxide and UVA." Douville J., David J., Fortier P.K., Ramotar D. Curr. Genet. 46:72-81(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIT4.
[9]	"Specific interactions of PP2A and PP2A-like phosphatases with the yeast PTPA homologues, Ypa1 and Ypa2." Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V., Goris J. Biochem. J. 386:93-102(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPG1; PPH3 AND SIT4.
[10]	"The yeast phosphotyrosyl phosphatase activator is part of the Tap42-phosphatase complexes." Zheng Y., Jiang Y. Mol. Biol. Cell 16:2119-2127(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SIT4 AND TAP42.
[11]	"The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/trans-isomerase." Jordens J., Janssens V., Longin S., Stevens I., Martens E., Bultynck G., Engelborghs Y., Lescrinier E., Waelkens E., Goris J., Van Hoof C. J. Biol. Chem. 281:6349-6357(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-205.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z38059 Genomic DNA. Translation: CAA86125.1.
BK006942 Genomic DNA. Translation: DAA08400.1.

PIR

S48381.

RefSeq

NP_012113.1. NM_001179501.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IXO	X-ray	2.60	A/B	1-317	[»]
2IXP	X-ray	2.80	A/B/C/D	1-317	[»]

ProteinModelPortal

P40454.

SMR

P40454. Positions 2-317.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5663N.

IntAct

P40454. 19 interactions.

MINT

MINT-520859.

STRING

4932.YIL153W.

Proteomic databases

PaxDb

P40454.

PeptideAtlas

P40454.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIL153W; YIL153W; YIL153W.

GeneID

854653.

KEGG

sce:YIL153W.

Organism-specific databases

CYGD

YIL153w.

SGD

S000001415. RRD1.

Phylogenomic databases

eggNOG

COG5057.

GeneTree

ENSGT00390000011500.

HOGENOM

HOG000205736.

OMA

QHIPLGG.

OrthoDB

EOG4G7G7J.

Gene expression databases

Genevestigator

P40454.

GermOnline

YIL153W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004327. Phstyr_phstse_ac.
[Graphical view]

PANTHER

PTHR10012. PTHR10012. 1 hit.

Pfam

PF03095. PTPA. 1 hit.
[Graphical view]

PIRSF

PIRSF016325. Phstyr_phstse_ac. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P40454.

NextBio

977208.

Entry information

Entry name

PTPA1_YEAST

Accession

Primary (citable) accession number: P40454
Secondary accession number(s): D6VVD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 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 IX

Yeast (Saccharomyces cerevisiae) chromosome IX: 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

Amino acid modifications

Experimental info

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