Reviewed, UniProtKB/Swiss-Prot P35176 (CYPD_YEAST)

Names and origin

Protein names

Recommended name:
    Peptidyl-prolyl cis-trans isomerase D
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin D

Gene names

Name:	CPR5
Synonyms:	CYP5, CYPD
Ordered Locus Names:	YDR304C
ORF Names:	D9740.14

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	225 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.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Endoplasmic reticulum lumen.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 225	203	Peptidyl-prolyl cis-trans isomerase D		PRO_0000025488
Regions
	Domain	37 – 195	159	PPIase cyclophilin-type
	Motif	222 – 225	4	Prevents secretion from ER
Amino acid modifications
	Modified residue	218	1	Phosphoserine Ref.4
	Glycosylation	139	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P35176-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: F4861424C8443B58	FASTA	225	25,327
	10 20 30 40 50 60 MKLQFFSFIT LFACLFTTAI FAKEDTAEDP EITHKVYFDI NHGDKQIGRI VMGLYGLTTP 70 80 90 100 110 120 QTVENFYQLT ISRDPKMGYL NSIFHRVIPN FMIQGGDFTH RSGIGGKSIF GNTFKDENFD 130 140 150 160 170 180 VKHDKPGRLS MANRGKNTNG SQFFITTVPC PWLDGKHVVF GEVLDGMDVV HYIENVKTDS 190 200 210 220 RNMPVKEVII VESGELETVP LDNKDAAKLQ EEIKAEASEA AHDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum." Frigerio G., Pelham H.R.B. J. Mol. Biol. 233:183-188(1993) [PubMed: 8377189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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.
[3]	"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.
[4]	"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-218, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X73142 mRNA. Translation: CAA51658.1. U28374 Genomic DNA. Translation: AAB64740.1. AY557734 Genomic DNA. Translation: AAS56060.1.
PIR	S38324.
RefSeq	NP_010590.1.
3D structure databases
HSSP	HSSP built from PDB template 1CYN based on UniProtKB P23284.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5222N.
IntAct	P35176. 2 interactions.
STRING	P35176.
2-D gel databases
SWISS-2DPAGE	P35176.
Proteomic databases
PeptideAtlas	P35176.
Genome annotation databases
Ensembl	YDR304C; YDR304C; YDR304C; Saccharomyces cerevisiae. [Genome view]
GeneID	851898.
GenomeReviews	Gene locus YDR304C in contig Z71256_GR.
KEGG	sce:YDR304C.
NMPDR	fig|4932.3.peg.1352.
Organism-specific databases
CYGD	YDR304c.
SGD	S000002712. CPR5.
Phylogenomic databases
HOGENOM	P35176.
OMA	EEHEITH.
Enzyme and pathway databases
BRENDA	5.2.1.8. 250.
Gene expression databases
ArrayExpress	P35176.
Genevestigator	P35176.
GermOnline	YDR304C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000886. ER_target_seq_motif. 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. PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	969898.

Entry information

Entry name

CYPD_YEAST

Accession

Primary (citable) accession number: P35176

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 3, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)