P25334 (CYPR_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase CPR4
Short name=PPIase CPR4
EC=5.2.1.8

Alternative name(s):
Rotamase

Gene names

Name:	CPR4
Synonyms:	CYP4, SCC3
Ordered Locus Names:	YCR069W
ORF Names:	YCR69W/YCR70W

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	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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	Membrane; Single-pass membrane protein Potential.
Sequence similarities	Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Isomerase Rotamase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 – 20	20	Potential
	Chain	21 – 318	298	Peptidyl-prolyl cis-trans isomerase CPR4		PRO_0000025494
Regions
	Transmembrane	286 – 303	18	Helical; Potential
	Domain	55 – 225	171	PPIase cyclophilin-type
Amino acid modifications
	Glycosylation	166	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P25334 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: E23AE2763BF5DEE4	FASTA	318	35,780
	10 20 30 40 50 60 MWLKSLLLCL YSLVLCQVHA APSSGKQITS KDVDLQKKYE PSPPATHRGI ITIEYFDPVS 70 80 90 100 110 120 KSMKEADLTF ELYGTVVPKT VNNFAMLAHG VKAVIEGKDP NDIHTYSYRK TKINKVYPNK 130 140 150 160 170 180 YIQGGVVAPD VGPFTVYGPK FDDENFYLKH DRPERLAMAY FGPDSNTSEF IITTKADGNE 190 200 210 220 230 240 ELDGKSVVFG QITSGLDQLM DAIQYTETDE YGKPQHELRF LYFVLEILKI SNILDLHAAY 250 260 270 280 290 300 TEKVEKFRNG DVSVGSTLEN IFRNDKAYTP LTTSTGTTAY DLNHPISRAL MCLTVLGLCF 310 IAYKGMHEKP HTVSLRHK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of a third cyclophilin-homologous gene from Saccharomyces cerevisiae." Franco L., Jimenez A., Demolder J., Molemans F., Contreras R. Yeast 7:971-979(1991) [PubMed: 1803821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59720 Genomic DNA. Translation: CAA42275.1. AY558152 Genomic DNA. Translation: AAS56478.1. BK006937 Genomic DNA. Translation: DAA07541.1.
PIR	CSBYC3. S26658.
RefSeq	NP_009995.1. NM_001178780.1.
3D structure databases
ProteinModelPortal	P25334.
SMR	P25334. Positions 52-223.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25334. 10 interactions.
MINT	MINT-4478613.
STRING	P25334.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCR069W; YCR069W; YCR069W.
GeneID	850433.
KEGG	sce:YCR069W.
NMPDR	fig|4932.3.peg.722.
Organism-specific databases
CYGD	YCR069w.
SGD	S000000665. CPR4.
Phylogenomic databases
eggNOG	fuNOG10026.
GeneTree	EFGT00050000000590.
OMA	KHDRPGR.
OrthoDB	EOG4C5GTX.
Gene expression databases
ArrayExpress	P25334.
Genevestigator	P25334.
GermOnline	YCR069W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K01802.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. False negative. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	966021.

Entry information

Entry name

CYPR_YEAST

Accession

Primary (citable) accession number: P25334
Secondary accession number(s): D6VR72, P25658

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program