PPIA_ECHGR
ID PPIA_ECHGR Reviewed; 162 AA.
AC P14088; Q8ITN4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=EGCyP-1;
DE AltName: Full=Rotamase;
GN Name=CYP-1;
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12458833; DOI=10.1017/s0031182002002330;
RA Colebrook A.L., Jenkins D.D., Lightowlers M.W.;
RT "Anti-parasitic effect of cyclosporin A on Echinococcus granulosus and
RT characterization of the associated cyclophilin protein.";
RL Parasitology 125:485-493(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-162.
RX PubMed=2677720; DOI=10.1016/0166-6851(89)90177-1;
RA Lightowlers M.W., Haralambous A., Rickard M.D.;
RT "Amino acid sequence homology between cyclophilin and a cDNA-cloned antigen
RT of Echinococcus granulosus.";
RL Mol. Biochem. Parasitol. 36:287-290(1989).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000269|PubMed:12458833}.
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 -!- DEVELOPMENTAL STAGE: Expressed constitutively in all life-cycle stages
CC examined. {ECO:0000269|PubMed:12458833}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC subfamily. {ECO:0000305}.
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DR EMBL; AF431734; AAN63589.1; -; Genomic_DNA.
DR EMBL; AF430707; AAN62875.1; -; mRNA.
DR PIR; A45000; A45000.
DR AlphaFoldDB; P14088; -.
DR SMR; P14088; -.
DR WBParaSite; EgrG_000920600; EgrG_000920600; EgrG_000920600.
DR OrthoDB; 1403619at2759; -.
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..162
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064124"
FT DOMAIN 6..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 162 AA; 17355 MW; BD60E17A8FE6B60F CRC64;
MGVKCFFDIS IGGKPAGRIV FALFDDVPKT VENFRALCTG EKGFGYKGSK FHRIIPGFMC
QGGDFTAGNG TGGKSIYGSK FEDENFNHKH SKPMMLSMAN AGKNTNGSQF FITTAVTSWL
DGKHVVFGEV ESGEDVVKDM EAVGSSSGKT SQEVLITDCG QL
