PPIE_SCHJA
ID PPIE_SCHJA Reviewed; 179 AA.
AC Q26516;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E;
DE Short=PPIase E;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin E;
DE AltName: Full=Rotamase E;
DE Flags: Fragment;
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=Philippines;
RX PubMed=1635025; DOI=10.2307/3283541;
RA Argaet V.P., Mitchell G.F.;
RT "Cyclophilin of Schistosoma japonicum.";
RL J. Parasitol. 78:660-664(1992).
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.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000305}.
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DR EMBL; M93420; AAA29863.1; -; mRNA.
DR AlphaFoldDB; Q26516; -.
DR SMR; Q26516; -.
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..179
FT /note="Peptidyl-prolyl cis-trans isomerase E"
FT /id="PRO_0000064160"
FT DOMAIN 21..177
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT NON_TER 1
SQ SEQUENCE 179 AA; 20050 MW; 4ADA71B386175DAC CRC64;
EDVSDDEMRT KKQKRNLPRV FFDIRIGNAD RGRIVMELRS DIVPRTAENF RALCTGDRGF
GYHNCCFHRV IPQFMCQGGD FVKGDGTGGK SIYGRKFDDE NFQLRHEGFG VLSMANSGPN
TNGSQFFICT TKCDWLDGKH VVFGRVVDGQ NVVKKMESVG SKSGKVKEPV TISRCGELI