P81531 (CYPH_BETPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended 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
Organism	Betula pendula (European white birch) (Betula verrucosa)
Taxonomic identifier	3505 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fagales › Betulaceae › Betula

Protein attributes

Sequence length	42 AA.
Sequence status	Fragments.
Protein existence	Evidence 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 component	Cytoplasm
Disease	Allergen
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Technical term	Direct protein sequencing
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	cytoplasm 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
	Chain	‹1 – ›42	›42	Peptidyl-prolyl cis-trans isomerase		PRO_0000064141
Regions
	Domain	‹1 – ›42	›42	PPIase cyclophilin-type
Experimental info
	Non-adjacent residues	17 – 18	2
	Non-terminal residue	1	1
	Non-terminal residue	42	1

Sequences

	Sequence		Length	Mass (Da)
	P81531 [UniParc]. Last modified March 1, 2001. Version 2. Checksum: 9C893DF3F18B37B9	FASTA	42	4,036
	10 20 30 40 DFTAGNGTGG ESIYGAKDXX XXXXXTGPGI LSMANAGPGT NG

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
ModBase	Search...
Protein family/group databases
Allergome	134. Bet v 7. 3139. Bet v 7.0101.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. [Graphical view]
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. Partial match. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYPH_BETPN

Accession

Primary (citable) accession number: P81531

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program