ID   CYP1_CAEEL              Reviewed;         192 AA.
AC   P52009;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 1;
DE            Short=PPIase 1;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-1;
DE   AltName: Full=Rotamase 1;
GN   Name=cyn-1; Synonyms=cyp-1; ORFNames=Y49A3A.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=8694762; DOI=10.1042/bj3170179;
RA   Page A.P., Macniven K., Hengartner M.O.;
RT   "Cloning and biochemical characterization of the cyclophilin homologues
RT   from the free-living nematode Caenorhabditis elegans.";
RL   Biochem. J. 317:179-185(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; U30943; AAC47116.1; -; mRNA.
DR   EMBL; AL033512; CAA22075.1; -; Genomic_DNA.
DR   PIR; T27034; T27034.
DR   RefSeq; NP_506561.1; NM_074160.5.
DR   AlphaFoldDB; P52009; -.
DR   SMR; P52009; -.
DR   BioGRID; 44940; 36.
DR   STRING; 6239.Y49A3A.5; -.
DR   EPD; P52009; -.
DR   PaxDb; P52009; -.
DR   PeptideAtlas; P52009; -.
DR   EnsemblMetazoa; Y49A3A.5.1; Y49A3A.5.1; WBGene00000877.
DR   GeneID; 179936; -.
DR   KEGG; cel:CELE_Y49A3A.5; -.
DR   UCSC; Y49A3A.5.1; c. elegans.
DR   CTD; 179936; -.
DR   WormBase; Y49A3A.5; CE22213; WBGene00000877; cyn-1.
DR   eggNOG; KOG0865; Eukaryota.
DR   GeneTree; ENSGT00940000168914; -.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   InParanoid; P52009; -.
DR   OMA; GDTHAGK; -.
DR   OrthoDB; 1403619at2759; -.
DR   PhylomeDB; P52009; -.
DR   PRO; PR:P52009; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000877; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..192
FT                   /note="Peptidyl-prolyl cis-trans isomerase 1"
FT                   /id="PRO_0000064190"
FT   DOMAIN          25..188
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   192 AA;  20711 MW;  C2094D91809ECE85 CRC64;
     MKFLLRASSL AGQSLRFASQ RPKVFFDVSI GEEPAGRVTM ELFNDVVPKT AENFRALCTG
     EKGVGEQGVA LHFKGSKFHR IIPEFMIQGG DFTRHNGTGG ESIYGNKFKD ENFDLKHTGP
     GCLSMANAGP NTNGSQFFIC TVDTPWLDGG HVVFGQVTDG MSVVKKIEKM GSRSGAPAKT
     VTIADCGELK SE