Reviewed, UniProtKB/Swiss-Prot P14832 (CYPH_YEAST)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin
      Short name=CPH
    Cyclosporin A-binding protein
    PPI-II

Gene names

Name:	CPR1
Synonyms:	CPH1, CYP1, SCC1
Ordered Locus Names:	YDR155C
ORF Names:	YD8358.10C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	162 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degredation (Vid) vesicles. Ref.9
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Subunit structure	Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and SET3. Ref.7
Subcellular location	Cytoplasm.
Miscellaneous	Present with 86000 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ascospore formation Inferred from mutant phenotype. Source: SGD protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Set3 complex Ref.6 Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	cyclosporin A binding Inferred from mutant phenotype. Source: SGD peptidyl-prolyl cis-trans isomerase activity Ref.2 Inferred from direct assay. Source: SGD protein binding Ref.7 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC13	P32797	1	EBI-5463,EBI-4187
HSP12	P22943	1	EBI-5463,EBI-8548
RPD3	P32561	1	EBI-5463,EBI-15864
SAP30	P38429	1	EBI-5463,EBI-27570
SMT3	Q12306	1	EBI-5463,EBI-17490

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 162

161

Peptidyl-prolyl cis-trans isomerase

PRO_0000064132

Regions

Domain

5 – 161

157

PPIase cyclophilin-type

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.5

Modified residue

71

1

Phosphothreonine Ref.13

Modified residue

142

1

Phosphoserine Ref.13

Modified residue

145

1

Phosphoserine Ref.13 Ref.10 Ref.11 Ref.12

Secondary structure

1

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162

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Beta strand

13 – 22

10

Turn

24 – 26

3

Helix

28 – 39

12

Turn

40 – 42

3

Beta strand

53 – 55

3

Turn

56 – 58

3

Beta strand

59 – 62

4

Turn

65 – 67

3

Beta strand

68 – 71

4

Beta strand

92 – 98

7

Beta strand

110 – 115

6

Helix

118 – 120

3

Turn

121 – 123

3

Beta strand

126 – 132

7

Helix

134 – 141

8

Beta strand

154 – 161

8

Sequences

	Sequence		Length	Mass (Da)
	P14832-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 012D8E8E4D85B4B7	FASTA	162	17,391
	10 20 30 40 50 60 MSQVYFDVEA DGQPIGRVVF KLYNDIVPKT AENFRALCTG EKGFGYAGSP FHRVIPDFML 70 80 90 100 110 120 QGGDFTAGNG TGGKSIYGGK FPDENFKKHH DRPGLLSMAN AGPNTNGSQF FITTVPCPWL 130 140 150 160 DGKHVVFGEV VDGYDIVKKV ESLGSPSGAT KARIVVAKSG EL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a full-length cDNA coding for cyclophilin (peptidyl-prolyl cis-trans isomerase) of Saccharomyces cerevisiae." Dietmeier K., Tropschug M. Nucleic Acids Res. 18:373-373(1990) [PubMed: 2183184] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Yeast cyclophilin: isolation and characterization of the protein, cDNA and gene." Haendler B., Keller R., Hiestand P.C., Kocher H.P., Wegmann G., Movva N.R. Gene 83:39-46(1989) [PubMed: 2687115] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Purification and properties of multiple molecular forms of yeast peptidyl prolyl cis-trans isomerase." Hasumi H., Nishikawa T. Biochim. Biophys. Acta 1161:161-167(1993) [PubMed: 8431466] [Abstract] Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
[6]	"The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program." Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H., Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F. Genes Dev. 15:2991-3004(2001) [PubMed: 11711434] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; SIF2; YIL112W AND SET3.
[7]	"Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase." Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J. EMBO J. 19:3739-3749(2000) [PubMed: 10899127] [Abstract] Cited for: INTERACTION WITH RPD3.
[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]	"Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles." Brown C.R., Cui D.-Y., Hung G.G.-C., Chiang H.-L. J. Biol. Chem. 276:48017-48026(2001) [PubMed: 11641409] [Abstract] Cited for: FUNCTION.
[10]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, MASS SPECTROMETRY.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, MASS SPECTROMETRY.
[13]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-142 AND SER-145, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X17505 mRNA. Translation: CAA35545.1.
M30513 Genomic DNA. Translation: AAA34528.1.
Z50046 Genomic DNA. Translation: CAA90376.1.
AY557665 Genomic DNA. Translation: AAS55991.1.

PIR

CSBY. S25443.

RefSeq

NP_010439.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IST	X-ray	1.90	A/B	1-162	[»]
1VDN	X-ray	1.60	A	1-162	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5203N.

IntAct

P14832. 43 interactions.

Proteomic databases

PeptideAtlas

P14832.

PRIDE

P14832.

Genome annotation databases

Ensembl

YDR155C. Saccharomyces cerevisiae. [Contig view]

GeneID

851733.

GenomeReviews

Gene locus YDR155C in contig Z71256_GR.

KEGG

sce:YDR155C.

NMPDR

fig|4932.3.peg.1188.

Organism-specific databases

CYGD

YDR155c.

SGD

S000002562. CPR1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P14832.

OMA

P14832. DVEADGQ.

Enzyme and pathway databases

BRENDA

5.2.1.8. 250.

Gene expression databases

ArrayExpress

P14832.

GermOnline

YDR155C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002130. PPIase_cyclophilin.
[Graphical view]

Gene3D

G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

969457.

Entry information

Entry name

CYPH_YEAST

Accession

Primary (citable) accession number: P14832

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)