Q12461 (PTPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2A activator 2
EC=5.2.1.8

Alternative name(s):
Peptidyl-prolyl cis-trans isomerase PTPA-2
Short name=PPIase PTPA-2
Short name=Rotamase PTPA-2
Phosphotyrosyl phosphatase activator 2

Gene names

Name:	RRD2
Synonyms:	NOH1, YPA2
Ordered Locus Names:	YPL152W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	358 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. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis. Ref.4 Ref.5 Ref.6 Ref.9 Ref.10 Ref.11
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with the phosphatase PP2A catalytic subunits PPH21 and PPH22. Forms a ternary complex with PPH21-TAP42. Ref.6 Ref.9 Ref.10
Subcellular location	Cytoplasm Ref.7.
Miscellaneous	Present with 2430 molecules/cell in log phase SD medium. Ref.8

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mitotic spindle organization in nucleus Inferred from mutant phenotype Ref.4. Source: SGD response to osmotic stress Inferred from genetic interaction. Source: SGD
Cellular component	cell fraction Inferred from direct assay. Source: SGD cytosol Traceable author statement. Source: SGD nucleus Inferred from mutant phenotype Ref.4. Source: GOC protein phosphatase type 2A complex Inferred from direct assay. 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.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 358

358

Serine/threonine-protein phosphatase 2A activator 2

PRO_0000226120

Secondary structure

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358

Helix Strand Turn

Details...

Turn

10 – 13

4

Helix

14 – 17

4

Helix

20 – 34

15

Turn

35 – 38

4

Helix

50 – 66

17

Helix

84 – 103

20

Helix

109 – 120

12

Turn

126 – 129

4

Helix

133 – 148

16

Helix

154 – 163

10

Helix

165 – 180

16

Beta strand

192 – 196

5

Helix

199 – 207

9

Turn

208 – 210

3

Helix

216 – 220

5

Helix

222 – 228

7

Turn

229 – 231

3

Helix

233 – 244

12

Turn

245 – 247

3

Helix

250 – 253

4

Helix

255 – 260

6

Helix

266 – 280

15

Turn

281 – 283

3

Helix

285 – 288

4

Beta strand

295 – 297

3

Sequences

	Sequence		Length	Mass (Da)
	Q12461 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E0BE8A7EDD54E306	FASTA	358	41,452
	10 20 30 40 50 60 MLPEKRLLTP DDMKLWEESP TRAHFTKFII DLAESVKGHE NSQYKEPISE SINSMMNLLS 70 80 90 100 110 120 QIKDITQKHP VIKDADSSRF GKVEFRDFYD EVSRNSRKIL RSEFPSLTDE QLEQLSIYLD 130 140 150 160 170 180 ESWGNKRRID YGSGHELNFM CLLYGLYSYG IFNLSNDSTN LVLKVFIEYL KIMRILETKY 190 200 210 220 230 240 WLEPAGSHGV WGLDDYHFLP FLFGAFQLTT HKHLKPISIH NNELVEMFAH RYLYFGCIAF 250 260 270 280 290 300 INKVKSSASL RWHSPMLDDI SGVKTWSKVA EGMIKMYKAE VLSKLPIMQH FYFSEFLPCP 310 320 330 340 350 DGVSPPRGHI HDGTDKDDEC NFEGHVHTTW GDCCGIKLPS AIAATEMNKK HHKPIPFD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators." Purnelle B., Coster F., Goffeau A. Yeast 12:1483-1492(1996) [PubMed: 8948103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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: 11262194] [Abstract] Cited for: FUNCTION.
[5]	"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: 11134337] [Abstract] Cited for: FUNCTION.
[6]	"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: 12952889] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPH21.
[7]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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: 15447631] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPH21 AND PPH22.
[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: 15689491] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPH21 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: 16380387] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X96770 Genomic DNA. Translation: CAA65569.1.
Z73508 Genomic DNA. Translation: CAA97857.1.
BK006949 Genomic DNA. Translation: DAA11283.1.

PIR

S65163.

RefSeq

NP_015173.1. NM_001183966.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IXN	X-ray	2.80	A/B	1-304	[»]

ProteinModelPortal

Q12461.

SMR

Q12461. Positions 3-299.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2558N.

IntAct

Q12461. 5 interactions.

MINT

MINT-556521.

STRING

Q12461.

Proteomic databases

PeptideAtlas

Q12461.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL152W; YPL152W; YPL152W.

GeneID

855951.

KEGG

sce:YPL152W.

NMPDR

fig|4932.3.peg.6303.

Organism-specific databases

CYGD

YPL152w.

SGD

S000006073. RRD2.

Phylogenomic databases

eggNOG

fuNOG05567.

GeneTree

EFGT00050000004419.

HOGENOM

HBG526297.

OMA

ISSAKNW.

OrthoDB

EOG4VHPGD.

Gene expression databases

ArrayExpress

Q12461.

Genevestigator

Q12461.

GermOnline

YPL152W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004327. Phstyr_phstse_ac.
[Graphical view]

KO

K01802.

PANTHER

PTHR10012. Phstyr_phstse_ac. 1 hit.

Pfam

PF03095. PTPA. 1 hit.
[Graphical view]

PIRSF

PIRSF016325. Phstyr_phstse_ac. 1 hit.

ProtoNet

Search...

Other

NextBio

980732.

Entry information

Entry name

PTPA2_YEAST

Accession

Primary (citable) accession number: Q12461
Secondary accession number(s): D6W3L7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program