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Protein

Peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Betula pendula (European white birch) (Betula verrucosa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.1 Publication

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Pollen allergen Bet v 7
Rotamase
Allergen: Bet v 7
OrganismiBetula pendula (European white birch) (Betula verrucosa)
Taxonomic identifieri3505 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFagalesBetulaceaeBetula

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei134. Bet v 7.
3139. Bet v 7.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000064141‹1 – ›42Peptidyl-prolyl cis-trans isomeraseAdd BLAST›42

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – ›42PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST›42

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.Curated

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiView protein in InterPro
IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR002130. Cyclophilin-type_PPIase_dom.
PANTHERiPTHR11071. PTHR11071. 1 hit.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiView protein in PROSITE
PS50072. CSA_PPIASE_2. 1 hit.

Sequencei

Sequence statusi: Fragments.

P81531-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
DFTAGNGTGG ESIYGAKDXX XXXXXTGPGI LSMANAGPGT NG
Length:42
Mass (Da):4,036
Last modified:March 1, 2001 - v2
Checksum:i9C893DF3F18B37B9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-adjacent residuesi17 – 18Curated2
Non-terminal residuei421

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei134. Bet v 7.
3139. Bet v 7.0101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiView protein in InterPro
IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR002130. Cyclophilin-type_PPIase_dom.
PANTHERiPTHR11071. PTHR11071. 1 hit.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiView protein in PROSITE
PS50072. CSA_PPIASE_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCYPH_BETPN
AccessioniPrimary (citable) accession number: P81531
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 1, 2001
Last modified: February 15, 2017
This is version 71 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.