ID   PPIA_SCHMA              Reviewed;         161 AA.
AC   Q26565;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
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;
DE   AltName: Full=Smp17.7;
DE   AltName: Full=p17.7;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=NMRI;
RX   PubMed=8919996; DOI=10.1016/0166-6851(95)02542-1;
RA   Kiang D., El Ghazalie N.E., Medhat A.M., Abdel-Fattah M., Karim A.M.,
RA   Loverde P.T.;
RT   "Identification and characterization of Schistosoma mansoni p17.7, a
RT   cyclophilin.";
RL   Mol. Biochem. Parasitol. 76:73-82(1996).
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   -!- TISSUE SPECIFICITY: Found mainly in the tegument, gut epithelium, and
CC       muscle layers. Also found in the interior of the parasite.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L46884; AAB41257.1; -; mRNA.
DR   RefSeq; XP_018652799.1; XM_018797792.1.
DR   AlphaFoldDB; Q26565; -.
DR   SMR; Q26565; -.
DR   STRING; 6183.Smp_040130.1; -.
DR   EnsemblMetazoa; Smp_040130.1; Smp_040130.1; Smp_040130.
DR   GeneID; 8347523; -.
DR   KEGG; smm:Smp_040130; -.
DR   WBParaSite; Smp_040130.1; Smp_040130.1; Smp_040130.
DR   CTD; 8347523; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   HOGENOM; CLU_012062_4_3_1; -.
DR   OMA; VESMGSN; -.
DR   OrthoDB; 1403619at2759; -.
DR   PhylomeDB; Q26565; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   ExpressionAtlas; Q26565; differential.
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   1: Evidence at protein level;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..161
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064127"
FT   DOMAIN          6..160
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   161 AA;  17671 MW;  BB3D3C4EF874F527 CRC64;
     MAAKAFFDIK AGDERLGRII FELFNDVPDT TRNFRELCTH KNNFGYKGSV FHRIIPGFMC
     QGGDFTNGDG TGGKSIYGNK FKDENFNHKH EAFSLSMANA GPNTNGSQFF ITTVPCSWLD
     GKHVVFGKVV SGIDVVKKME SLGSTSGKPS KKIIIEDCGE C