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Q8X166 (PPIB_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase B

Short name=PPIase B
EC=5.2.1.8
Alternative name(s):
Rotamase B
Gene names
Name:cypB
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 componentEndoplasmic reticulum
   DomainSignal
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptide 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 212189Peptidyl-prolyl cis-trans isomerase B
PRO_0000233044

Regions

Domain38 – 195158PPIase cyclophilin-type
Motif209 – 2124Prevents secretion from ER

Amino acid modifications

Glycosylation1391N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8X166 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: FA00BA7D1E50019C

FASTA21223,302
        10         20         30         40         50         60 
MNFKNIFLSF FFVLAVGLAL VHAEDAQPRG PKITSKVFFD IEHGDKPLGR VVLGLYGKTV 

        70         80         90        100        110        120 
PKTAENFRAL ATGEKGFGYE GSTFHRVIKD FMIQGGDFTR GDGTGGKSIY GEKFADENFK 

       130        140        150        160        170        180 
LRHTRKGLLS MANAGKDTNG SQFFITTVPT PWLDGRHVVF GEVLEGYEIV AQIENVPKGR 

       190        200        210 
SDRPVETVKI VKSGELESED KAGEKGSSHE EL 

« Hide

References

[1]"The foldase CYPB is a component of the secretory pathway of Aspergillus niger and contains the endoplasmic reticulum retention signal HEEL."
Derkx P.M.F., Madrid S.M.
Mol. Gen. Genet. 266:537-545(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY005867 Genomic DNA. Translation: AAF98447.1.

3D structure databases

ProteinModelPortalQ8X166.
SMRQ8X166. Positions 30-199.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ8X166.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0652.

Family and domain databases

InterProIPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPIB_ASPNG
AccessionPrimary (citable) accession number: Q8X166
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families