ID   CYP7_CAEEL              Reviewed;         171 AA.
AC   P52015;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 7;
DE            Short=PPIase 7;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-7;
DE   AltName: Full=Rotamase 7;
GN   Name=cyn-7; Synonyms=cyp-7; ORFNames=Y75B12B.2;
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-13.
RC   STRAIN=Bristol N2;
RX   PubMed=9150941; DOI=10.1002/elps.1150180337;
RA   Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.;
RT   "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates
RT   and identification of protein spots by microsequencing.";
RL   Electrophoresis 18:557-562(1997).
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; U27559; AAC47125.1; -; mRNA.
DR   EMBL; AL032663; CAA21760.1; -; Genomic_DNA.
DR   PIR; T27371; T27371.
DR   RefSeq; NP_506749.1; NM_074348.11.
DR   AlphaFoldDB; P52015; -.
DR   SMR; P52015; -.
DR   BioGRID; 45022; 62.
DR   DIP; DIP-24704N; -.
DR   FunCoup; P52015; 1404.
DR   STRING; 6239.Y75B12B.2.2; -.
DR   PaxDb; 6239-Y75B12B.2.2; -.
DR   PeptideAtlas; P52015; -.
DR   EnsemblMetazoa; Y75B12B.2.1; Y75B12B.2.1; WBGene00000883.
DR   GeneID; 180027; -.
DR   KEGG; cel:CELE_Y75B12B.2; -.
DR   UCSC; Y75B12B.2.1; c. elegans.
DR   AGR; WB:WBGene00000883; -.
DR   CTD; 180027; -.
DR   WormBase; Y75B12B.2; CE20371; WBGene00000883; cyn-7.
DR   eggNOG; KOG0865; Eukaryota.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   InParanoid; P52015; -.
DR   OMA; FKSIVPR; -.
DR   OrthoDB; 193499at2759; -.
DR   PhylomeDB; P52015; -.
DR   PRO; PR:P52015; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000883; Expressed in adult organism and 4 other cell types or tissues.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd01926; cyclophilin_ABH_like; 1.
DR   FunFam; 2.40.100.10:FF:000002; Peptidyl-prolyl cis-trans isomerase; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 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   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D-RELATED; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..171
FT                   /note="Peptidyl-prolyl cis-trans isomerase 7"
FT                   /id="PRO_0000064194"
FT   DOMAIN          7..170
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        12
FT                   /note="I -> T (in Ref. 1; AAC47125)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   171 AA;  18401 MW;  D5BD5E32A32942A7 CRC64;
     MSRPRVFFDI TIAGKPTGRI VMELYNDIVP KTAENFRALC TGEKGVGKSG KPLHFKGSKF
     HRIIPEFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT GPGVLSMANA GPNTNGSQFF
     LCTVKTAWLD GKHVVFGRVV EGLDIVSKVE GNGSSSGTPK SECLIADCGQ L
//