ID   CYPH_LUPLU              Reviewed;         172 AA.
AC   O49886;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
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;
OS   Lupinus luteus (European yellow lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3873;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Ventus; TISSUE=Seedling;
RX   PubMed=11768533; DOI=10.1094/mpmi.2001.14.12.1384;
RA   Nuc K., Nuc P., Slomski R.;
RT   "Yellow lupine cyclophilin transcripts are highly accumulated in the nodule
RT   meristem zone.";
RL   Mol. Plant Microbe Interact. 14:1384-1394(2001).
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   -!- TISSUE SPECIFICITY: Expressed in meristematic tissues, with higher
CC       levels in nodules. {ECO:0000269|PubMed:11768533}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; Y16088; CAA76054.1; -; mRNA.
DR   EMBL; AF178458; AAF00471.1; -; Genomic_DNA.
DR   AlphaFoldDB; O49886; -.
DR   SMR; O49886; -.
DR   PRIDE; O49886; -.
DR   BRENDA; 5.2.1.8; 3093.
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..172
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064144"
FT   DOMAIN          7..170
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   172 AA;  18287 MW;  DD8351276CBEEF1F CRC64;
     MSNPKVFFDM AIAGNPAGRI VMELYADTTP RTAENFRALC TGEKGVGRSG KPLHYKGSTF
     HRVIPNFMCQ GGDFTAGNGT GAESIYGAKF ADENFIKRHT GPGILSMANA GAGTNGSQFF
     ICTEKTEWLD GKHVVFGKVI EGMNVVRDIE KVGSGSGKTS RPVTIADCGQ LS