PPIB_SCHMA
ID PPIB_SCHMA Reviewed; 213 AA.
AC Q26551;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
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;
GN Name=CYP;
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].
RC STRAIN=Puerto Rican;
RX PubMed=8720179; DOI=10.1016/0166-6851(95)02509-x;
RA Klinkert M.-Q., Bugli F., Engels B., Carrasquillo E., Valle C., Cioli D.;
RT "Characterization of a Schistosoma mansoni cDNA encoding a B-like
RT cyclophilin and its expression in Escherichia coli.";
RL Mol. Biochem. Parasitol. 75:99-111(1995).
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 -!- DEVELOPMENTAL STAGE: This soluble protein is present in abundance in
CC the adult worm as well as in the schistosomula and the eggs.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
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DR EMBL; U30874; AAC46985.1; -; mRNA.
DR AlphaFoldDB; Q26551; -.
DR SMR; Q26551; -.
DR STRING; 6183.Smp_040790.1; -.
DR eggNOG; KOG0880; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
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; Reference proteome; 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_0000025484"
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; 23294 MW; 15FF6371E60B7415 CRC64;
MAVLKPLCPL LLLSIICFGL IRSEANGPKV TDKVFFDIEV DGKPLARIII GLFGKTVPKT
VENFKQLSIG TQLKDGRTAS YKGSTFHRVI KSFMIQGGDF TNHDGTGGFS IYGDRFPDEN
FKLRHVGAGW LSMANAGPDT NGSQFFITTV KTSWLDGKHV VFGKVVEGMN IVRQIESETT
DSRDRPVKSI KIASCGHIPV EIPFSVTNSD AVE
