CYPH_BRANA
ID CYPH_BRANA Reviewed; 171 AA.
AC P24525;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 91.
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;
GN Name=CYP; Synonyms=ROT1;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Westar;
RX PubMed=1702215; DOI=10.1073/pnas.87.24.9519;
RA Gasser C.S., Gunning D.A., Budelier K.A., Brown S.M.;
RT "Structure and expression of cytosolic cyclophilin/peptidyl-prolyl cis-
RT trans isomerase of higher plants and production of active tomato
RT cyclophilin in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9519-9523(1990).
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.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M55018; AAA62706.1; -; mRNA.
DR PIR; B39252; CSRP.
DR AlphaFoldDB; P24525; -.
DR SMR; P24525; -.
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..171
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064142"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 171 AA; 18516 MW; 4F79D3E382B57F52 CRC64;
MVNPKVYFDM TVGDKAAGRI VMELYADTVP ETAENFRALC TGERGIGKSG KPLHYKGSAF
HRVIPKFMCQ GGDFTAGNGT GGESIYGMKF KDENFVKKHT GPGILSMRNA GSNTNGSQFF
ICTEKTSWLD GKHVVFGQVV EGMDVVRDIE KVGSDSGRTS KKVVTCDCGQ L
