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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

CPR2

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by cyclosporin A (CsA).By similarity

GO - Molecular functioni

  1. peptide binding Source: UniProtKB-KW
  2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
Short name:
PPIase B
Alternative name(s):
Rotamase B
Gene namesi
Name:CPR2
Ordered Locus Names:YALI0E23155g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
ProteomesiUP000001300 Componenti: Chromosome E

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. Golgi apparatus Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 228204Peptidyl-prolyl cis-trans isomerase BPRO_0000233051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ6C4W6.

Interactioni

Protein-protein interaction databases

STRINGi4952.Q6C4W6.

Structurei

3D structure databases

ProteinModelPortaliQ6C4W6.
SMRiQ6C4W6. Positions 29-197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 192158PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi225 – 2284Prevents secretion from ER

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065981.
InParanoidiQ6C4W6.
KOiK03768.
OMAiCLWIVLV.
OrthoDBiEOG757D7G.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6C4W6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLFATIGVL LVALLAFFVQ PAQAEPDAEI THKVYFDIKQ GEESLGKIVM
60 70 80 90 100
GLYGDVVPKT VENFRALCTG ETGKGYKGSK FHRVIKNFMI QGGDFTRGDG
110 120 130 140 150
TGGESIYGRK FPDENFQLKH TKPYKLSMAN AGRDTNGSQF FITTVVTSWL
160 170 180 190 200
DGKHVVFGEV LEGQDIVDAI ENAPTGARSN PKVDITIADA GEIPVEKSET
210 220
KEAEPAKEDA KEPKEDVKKK GKSDKDEL
Length:228
Mass (Da):24,946
Last modified:August 15, 2004 - v1
Checksum:iD89D2EA3BD7BDB6D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382131 Genomic DNA. Translation: CAG79895.1.
RefSeqiXP_504296.1. XM_504296.1.

Genome annotation databases

EnsemblFungiiCAG79895; CAG79895; YALI0_E23155g.
GeneIDi2912927.
KEGGiyli:YALI0E23155g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382131 Genomic DNA. Translation: CAG79895.1.
RefSeqiXP_504296.1. XM_504296.1.

3D structure databases

ProteinModelPortaliQ6C4W6.
SMRiQ6C4W6. Positions 29-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4952.Q6C4W6.

Proteomic databases

PRIDEiQ6C4W6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG79895; CAG79895; YALI0_E23155g.
GeneIDi2912927.
KEGGiyli:YALI0E23155g.

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000065981.
InParanoidiQ6C4W6.
KOiK03768.
OMAiCLWIVLV.
OrthoDBiEOG757D7G.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPIB_YARLI
AccessioniPrimary (citable) accession number: Q6C4W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2006
Last sequence update: August 15, 2004
Last modified: March 31, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.