ID   CYPX_USEUD              Reviewed;         169 AA.
AC   P35627;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Rotamase;
OS   Unspecified eudicot DB-1992.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons.
OX   NCBI_TaxID=323200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=1623198; DOI=10.1007/bf00023405;
RA   Bartling D., Heese A., Weiler E.W.;
RT   "Nucleotide sequence of a cDNA encoding an Arabidopsis cyclophilin-like
RT   protein.";
RL   Plant Mol. Biol. 19:529-530(1992).
RN   [2]
RP   DISCUSSION OF ORIGIN OF SEQUENCE.
RX   PubMed=9426607; DOI=10.1023/a:1005930024796;
RA   Chou I.T., Gasser C.S.;
RT   "Characterization of the cyclophilin gene family of Arabidopsis thaliana
RT   and phylogenetic analysis of known cyclophilin proteins.";
RL   Plant Mol. Biol. 35:873-892(1997).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:1623198) reported to be isolated from
CC       an A.thaliana cDNA library. PubMed:9426607 authors have assigned that
CC       the sequence has been amplified from an other contaminating organism.
CC       {ECO:0000305|PubMed:1623198}.
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DR   EMBL; X63616; CAA45161.1; -; mRNA.
DR   PIR; S22496; S22496.
DR   AlphaFoldDB; P35627; -.
DR   SMR; P35627; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Rotamase.
FT   CHAIN           1..169
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064139"
FT   DOMAIN          5..168
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   169 AA;  18161 MW;  B6077FC139864931 CRC64;
     MAHCFFDMTI GGQPAGRIIM ELFPDVPKTA ENFRALCTGE KGIGPSGKKM TYEGSVFHRV
     IPKFMLQGGD FTLGNGRGGE SIYGAKFADE NFIHKHTTPG LLSMANAGPG TNGSQFFITT
     VATPHLDGKH VVFGKVVEGM DVVRKIEATQ TDRGDKPLSE VKIAKCGQL