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P81531

- CYPH_BETPN

UniProt

P81531 - CYPH_BETPN

Protein

Peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Betula pendula (European white birch) (Betula verrucosa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    1. peptide binding Source: UniProtKB-KW
    2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    Cyclosporin

    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

    1. cytoplasm Source: UniProtKB-SubCell

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›42›42Peptidyl-prolyl cis-trans isomerasePRO_0000064141Add
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini‹1 – ›42›42PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the cyclophilin-type PPIase family.Curated
    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragments.

    P81531-1 [UniParc]FASTAAdd to Basket

    « Hide

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-adjacent residuesi17 – 182Curated
    Non-terminal residuei42 – 421

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 134. Bet v 7.
    3139. Bet v 7.0101.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiCYPH_BETPN
    AccessioniPrimary (citable) accession number: P81531
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 66 of the entry and version 2 of the sequence. [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

    External Data

    Dasty 3