ID   PPIA_PENGL              Reviewed;          11 AA.
AC   P85444;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=Rotamase;
DE   Flags: Fragment;
OS   Penicillium glabrum (Penicillium frequentans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69773;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND ALLERGEN.
RC   STRAIN=B7;
RA   Raquel H., Jeno P., Moita C., Cardoso C., Sao Jose H., San-Romao V.,
RA   Pinto Ricardo C., Oliveira M.M.;
RT   "Identification of putative allergens from Penicillium glabrum using two-
RT   dimensional (2-D) gel electrophoresis immunoblotting approach.";
RL   Submitted (FEB-2008) to UniProtKB.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250|UniProtKB:Q8LDP4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000250|UniProtKB:Q8LDP4};
CC   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase (By similarity).
CC       {ECO:0000250|UniProtKB:Q8LDP4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000255}.
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DR   PRIDE; P85444; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Allergen; Cytoplasm; Direct protein sequencing; Isomerase; Rotamase.
FT   CHAIN           <1..>11
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000324676"
FT   DOMAIN          <1..>11
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   NON_TER         1
FT   NON_TER         11
SQ   SEQUENCE   11 AA;  1377 MW;  85B0B191D9C44B1A CRC64;
     KFADENFQLK H