P53043 (PPT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase T
Short name=PPT
EC=3.1.3.16

Gene names

Name:	PPT1
Ordered Locus Names:	YGR123C
ORF Names:	G6347

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery. Ref.10
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Enzyme regulation	Stimulated by arachidonic acid and other unsaturated fatty acids, and by arachidoyl coenzyme A. Ref.7
Subunit structure	Interacts (via TPR repeats) with HSP82 (via C-terminal MEEVD pentapeptide). Ref.10
Subcellular location	Nucleus Ref.7 Ref.8.
Induction	Expression peaks in early log phase and decreases dramatically during the stationary phase (at protein level). Ref.7
Domain	The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT1 phosphatase activity.
Miscellaneous	Present with 6990 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily. Contains 3 TPR repeats.
Biophysicochemical properties	Kinetic parameters: KM=34 mM for p-nitrophenylphosphate Ref.11 pH dependence: Optimum pH is 7.8.
Sequence caution	The sequence CAA61596.1 differs from that shown. Reason: Frameshift at position 381.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat TPR repeat
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein dephosphorylation Inferred from direct assay Ref.1. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.7. Source: SGD nucleus Inferred from direct assay Ref.7. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSC82	P15108	3	EBI-13796,EBI-8666
HSP82	P02829	5	EBI-13796,EBI-8659

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 513

513

Serine/threonine-protein phosphatase T

PRO_0000058898

Regions

Repeat

12 – 45

34

TPR 1

Repeat

46 – 79

34

TPR 2

Repeat

80 – 113

34

TPR 3

Region

188 – 513

326

Catalytic

Sites

Active site

311

1

Proton donor By similarity

Metal binding

249

1

Iron By similarity

Metal binding

251

1

Iron By similarity

Metal binding

278

1

Iron By similarity

Metal binding

278

1

Manganese By similarity

Metal binding

310

1

Manganese By similarity

Metal binding

359

1

Manganese By similarity

Metal binding

434

1

Manganese By similarity

Experimental info

Mutagenesis

311

1

H → A: Loss of phosphatase activity. Ref.10

Secondary structure

1

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513

Helix Strand Turn

Details...

Helix

192 – 201

10

Helix

203 – 205

3

Helix

211 – 226

16

Beta strand

230 – 234

5

Beta strand

237 – 239

3

Beta strand

243 – 247

5

Helix

254 – 264

11

Beta strand

271 – 275

5

Beta strand

280 – 283

4

Helix

286 – 299

14

Turn

301 – 303

3

Beta strand

304 – 306

3

Helix

314 – 320

7

Helix

322 – 329

8

Helix

332 – 342

11

Beta strand

347 – 351

5

Turn

352 – 354

3

Beta strand

355 – 357

3

Helix

370 – 374

5

Beta strand

384 – 386

3

Helix

387 – 393

7

Beta strand

398 – 404

7

Beta strand

411 – 413

3

Helix

415 – 424

10

Beta strand

428 – 432

5

Beta strand

439 – 444

6

Helix

445 – 447

3

Beta strand

449 – 452

4

Helix

458 – 460

3

Beta strand

465 – 471

7

Turn

480 – 482

3

Beta strand

488 – 493

6

Turn

503 – 506

4

Sequences

	Sequence		Length	Mass (Da)
	P53043 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6966DA22340A5793	FASTA	513	57,995
	10 20 30 40 50 60 MSTPTAADRA KALERKNEGN VFVKEKHFLK AIEKYTEAID LDSTQSIYFS NRAFAHFKVD 70 80 90 100 110 120 NFQSALNDCD EAIKLDPKNI KAYHRRALSC MALLEFKKAR KDLNVLLKAK PNDPAATKAL 130 140 150 160 170 180 LTCDRFIREE RFRKAIGGAE NEAKISLCQT LNLSSFDANA DLANYEGPKL EFEQLYDDKN 190 200 210 220 230 240 AFKGAKIKNM SQEFISKMVN DLFLKGKYLP KKYVAAIISH ADTLFRQEPS MVELENNSTP 250 260 270 280 290 300 DVKISVCGDT HGQFYDVLNL FRKFGKVGPK HTYLFNGDFV DRGSWSCEVA LLFYCLKILH 310 320 330 340 350 360 PNNFFLNRGN HESDNMNKIY GFEDECKYKY SQRIFNMFAQ SFESLPLATL INNDYLVMHG 370 380 390 400 410 420 GLPSDPSATL SDFKNIDRFA QPPRDGAFME LLWADPQEAN GMGPSQRGLG HAFGPDITDR 430 440 450 460 470 480 FLRNNKLRKI FRSHELRMGG VQFEQKGKLM TVFSAPNYCD SQGNLGGVIH VVPGHGILQA 490 500 510 GRNDDQNLII ETFEAVEHPD IKPMAYSNGG FGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus." Chen M.X., McPartlin A.E., Brown L., Chen Y.H., Barker H.M., Cohen P.T.W. EMBO J. 13:4278-4290(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown open reading frames, the gene for an Asn synthase, remnants of Ty and three tRNA genes." van Dyck L., Tettelin H., Purnelle B., Goffeau A. Yeast 13:171-176(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases." Chen M.X., Chen Y.H., Cohen P.T.W. FEBS Lett. 306:54-58(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-277.
[7]	"Characterization of Saccharomyces cerevisiae protein Ser/Thr phosphatase T1 and comparison to its mammalian homolog PP5." Jeong J.-Y., Johns J., Sinclair C., Park J.-M., Rossie S. BMC Cell Biol. 4:3-3(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION.
[8]	"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].
[9]	"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].
[10]	"The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90." Wandinger S.K., Suhre M.H., Wegele H., Buchner J. EMBO J. 25:367-376(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP82, MUTAGENESIS OF HIS-311.
[11]	"Expression, purification and refolding of the phosphatase domain of protein phosphatase 1 (Ppt1) from Saccharomyces cerevisiae." Suhre M.H., Wegele H., Wandinger S.K. Int. J. Biol. Macromol. 39:23-28(2006) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X89417 Genomic DNA. Translation: CAA61596.1. Frameshift.
X83099 Genomic DNA. Translation: CAA58158.1.
Z72908 Genomic DNA. Translation: CAA97134.1.
AY558095 Genomic DNA. Translation: AAS56421.1.
S39959 Genomic DNA. Translation: AAB22462.1.
BK006941 Genomic DNA. Translation: DAA08216.1.

PIR

S52571.

RefSeq

NP_011639.3. NM_001181252.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ICF	X-ray	2.30	A/B	179-513	[»]

ProteinModelPortal

P53043.

SMR

P53043. Positions 11-508.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1525N.

IntAct

P53043. 10 interactions.

MINT

MINT-406578.

STRING

4932.YGR123C.

Proteomic databases

PaxDb

P53043.

PeptideAtlas

P53043.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR123C; YGR123C; YGR123C.

GeneID

853023.

KEGG

sce:YGR123C.
sce:YGR129W.

Organism-specific databases

CYGD

YGR123c.

SGD

S000003355. PPT1.

Phylogenomic databases

eggNOG

COG0639.

GeneTree

ENSGT00530000063173.

HOGENOM

HOG000172698.

KO

K04460.
K12868.

OMA

TVFAYKW.

OrthoDB

EOG4BZR9Z.

Gene expression databases

Genevestigator

P53043.

GermOnline

YGR123C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR004843. Metallo_PEstase_dom.
IPR013235. PPP_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR011236. Ser/Thr_PPase_5.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]

PANTHER

PTHR11668:SF12. PTHR11668:SF12. 1 hit.

Pfam

PF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]

PIRSF

PIRSF033096. PPPtase_5. 1 hit.

PRINTS

PR00114. STPHPHTASE.

SMART

SM00156. PP2Ac. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P53043.

NextBio

972897.

Entry information

Entry name

PPT1_YEAST

Accession

Primary (citable) accession number: P53043
Secondary accession number(s): D6VUQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program