ID   PPIB_SCHJA              Reviewed;         213 AA.
AC   Q27774;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin B;
DE   AltName: Full=Rotamase B;
DE   AltName: Full=S-cyclophilin;
DE   Flags: Precursor;
OS   Schistosoma japonicum (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Chinese;
RX   PubMed=8898338; DOI=10.1016/0166-6851(96)02692-8;
RA   Klinkert M.-Q., Bugli F., Cruz J., Engels B., Cioli D.;
RT   "Sequence conservation of schistosome cyclophilins.";
RL   Mol. Biochem. Parasitol. 81:239-242(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: Inhibited by cyclosporin A (CsA).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U50389; AAC47316.1; -; mRNA.
DR   AlphaFoldDB; Q27774; -.
DR   SMR; Q27774; -.
DR   PRIDE; Q27774; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 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   Endoplasmic reticulum; Isomerase; Rotamase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..213
FT                   /note="Peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000025483"
FT   DOMAIN          35..197
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOTIF           210..213
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  23238 MW;  D4986CDF7EDB8368 CRC64;
     MAVLRVLCGL LLVSILFLGF VLSEGNGPKV TEKVFFDIEV DEQPLGRIII GLFGKTVPKT
     VENFKQLSIG TTLKDGRTAA YKGSTFHRVI KSFMIQGGDF TNHDGTGGFS IYGERFPDEN
     FKLKHVGAGW LSMANAGPNT NGAQFFITTT QNPWLDGKHV VFGKVVEGMS VVRQIENMQT
     DSRDRPVKSV KIANCGHIPV DVPFSVSNTD AAE