ID   CYPH_BETPN              Reviewed;          42 AA.
AC   P81531;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=Cyclosporin A-binding protein;
DE   AltName: Full=Pollen allergen Bet v 7;
DE   AltName: Full=Rotamase;
DE   AltName: Allergen=Bet v 7;
DE   Flags: Fragments;
OS   Betula pendula (European white birch) (Betula verrucosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Betula.
OX   NCBI_TaxID=3505;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND ACTIVITY REGULATION.
RC   TISSUE=Pollen;
RX   PubMed=10669849; DOI=10.1016/s0091-6749(00)90078-2;
RA   Cadot P., Diaz J., Proost P., Van Damme J., Engelborghs Y., Stevens E.A.M.,
RA   Ceuppens J.L.;
RT   "Purification and characterization of an 18-kd allergen of birch (Betula
RT   verrucosa) pollen: identification as a cyclophilin.";
RL   J. Allergy Clin. Immunol. 105:286-291(2000).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000269|PubMed:10669849}.
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   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase. Do not bind FK506.
CC       {ECO:0000269|PubMed:10669849}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   Allergome; 134; Bet v 7.
DR   Allergome; 3139; Bet v 7.0101.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Cytoplasm; Direct protein sequencing; Isomerase; Rotamase.
FT   CHAIN           <1..>42
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064141"
FT   DOMAIN          <1..>42
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         42
SQ   SEQUENCE   42 AA;  4036 MW;  9C893DF3F18B37B9 CRC64;
     DFTAGNGTGG ESIYGAKDXX XXXXXTGPGI LSMANAGPGT NG
//