Reviewed, UniProtKB/Swiss-Prot P81531 (CYPH_BETVE)

Names and origin

Protein names	Recommended name:     Peptidyl-prolyl cis-trans isomerase       Short name=PPIase       Short name=Rotamase     EC=5.2.1.8 Alternative name(s):     Cyclophilin     Cyclosporin A-binding protein     Pollen allergen Bet v 7     Allergen=Bet v 7
Organism	Betula verrucosa (White birch) (Betula pendula)
Taxonomic identifier	3505 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fagales › Betulaceae › Betula

Protein attributes

Sequence length	42 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
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
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)
	P81531-1 [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: 10669849] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION. Tissue: Pollen.

Cross-references

3D structure databases
HSSP	HSSP built from PDB template 1E3B based on UniProtKB P52011.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.2.1.8. 228863.
Family and domain databases
InterPro	IPR002130. PPIase_cyclophilin. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PROSITE	PS00170. CSA_PPIASE_1. Partial match. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYPH_BETVE

Accession

Primary (citable) accession number: P81531

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)