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P81531 (CYPH_BETPN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Pollen allergen Bet v 7
Rotamase
Allergen=Bet v 7
OrganismBetula pendula (European white birch) (Betula verrucosa)
Taxonomic identifier3505 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFagalesBetulaceaeBetula

Protein attributes

Sequence length42 AA.
Sequence statusFragments.
Protein existenceEvidence 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. Ref.1

Catalytic activity

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

Enzyme regulation

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase. Do not bind FK506. Ref.1

Subcellular location

Cytoplasm.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DiseaseAllergen
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

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

Chain‹1 – ›42›42Peptidyl-prolyl cis-trans isomerase
PRO_0000064141

Regions

Domain‹1 – ›42›42PPIase cyclophilin-type

Experimental info

Non-adjacent residues17 – 182
Non-terminal residue11
Non-terminal residue421

Sequences

Sequence LengthMass (Da)Tools
P81531 [UniParc].

Last modified March 1, 2001. Version 2.
Checksum: 9C893DF3F18B37B9

FASTA424,036
        10         20         30         40 
DFTAGNGTGG ESIYGAKDXX XXXXXTGPGI LSMANAGPGT NG 

« Hide

References

[1]"Purification and characterization of an 18-kd allergen of birch (Betula verrucosa) pollen: identification as a cyclophilin."
Cadot P., Diaz J., Proost P., Van Damme J., Engelborghs Y., Stevens E.A.M., Ceuppens J.L.
J. Allergy Clin. Immunol. 105:286-291(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION.
Tissue: Pollen.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome134. Bet v 7.
3139. Bet v 7.0101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PROSITEPS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYPH_BETPN
AccessionPrimary (citable) accession number: P81531
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Allergens

Nomenclature of allergens and list of entries