Q6C4W6 (PPIB_YARLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Rotamase B

Gene names

Name:	CPR2
Ordered Locus Names:	YALI0E23155g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia › Yarrowia lipolytica

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by cyclosporin A (CsA) By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity.
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
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 – 24	24	Potential
	Chain	25 – 228	204	Peptidyl-prolyl cis-trans isomerase B		PRO_0000233051
Regions
	Domain	35 – 192	158	PPIase cyclophilin-type
	Motif	225 – 228	4	Prevents secretion from ER
Amino acid modifications
	Glycosylation	136	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6C4W6 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: D89D2EA3BD7BDB6D	FASTA	228	24,946
	10 20 30 40 50 60 MKLFATIGVL LVALLAFFVQ PAQAEPDAEI THKVYFDIKQ GEESLGKIVM GLYGDVVPKT 70 80 90 100 110 120 VENFRALCTG ETGKGYKGSK FHRVIKNFMI QGGDFTRGDG TGGESIYGRK FPDENFQLKH 130 140 150 160 170 180 TKPYKLSMAN AGRDTNGSQF FITTVVTSWL DGKHVVFGEV LEGQDIVDAI ENAPTGARSN 190 200 210 220 PKVDITIADA GEIPVEKSET KEAEPAKEDA KEPKEDVKKK GKSDKDEL

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382131 Genomic DNA. Translation: CAG79895.1.
RefSeq	XP_504296.1. XM_504296.1.
3D structure databases
ProteinModelPortal	Q6C4W6.
SMR	Q6C4W6. Positions 29-197.
ModBase	Search...
Protein-protein interaction databases
STRING	4952.Q6C4W6.
Proteomic databases
PRIDE	Q6C4W6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2912927.
KEGG	yli:YALI0E23155g.
Phylogenomic databases
eggNOG	COG0652.
HOGENOM	HOG000065981.
KO	K03768.
OMA	ENFADEN.
OrthoDB	EOG4DZ54P.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPIB_YARLI

Accession

Primary (citable) accession number: Q6C4W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program