CYP11_CAEEL
ID CYP11_CAEEL Reviewed; 183 AA.
AC P52018;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase 11;
DE Short=PPIase 11;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-11;
DE AltName: Full=Rotamase 11;
GN Name=cyn-11; Synonyms=cyp-11; ORFNames=T01B7.4;
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. PPIase H
CC subfamily. {ECO:0000305}.
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DR EMBL; U34955; AAC47115.1; -; mRNA.
DR EMBL; Z66499; CAA91297.1; -; Genomic_DNA.
DR PIR; T18578; T18578.
DR RefSeq; NP_495855.1; NM_063454.5.
DR AlphaFoldDB; P52018; -.
DR SMR; P52018; -.
DR BioGRID; 39721; 1.
DR STRING; 6239.T01B7.4; -.
DR EPD; P52018; -.
DR PaxDb; P52018; -.
DR PeptideAtlas; P52018; -.
DR EnsemblMetazoa; T01B7.4.1; T01B7.4.1; WBGene00000887.
DR GeneID; 174394; -.
DR KEGG; cel:CELE_T01B7.4; -.
DR UCSC; T01B7.4; c. elegans.
DR CTD; 174394; -.
DR WormBase; T01B7.4; CE03588; WBGene00000887; cyn-11.
DR eggNOG; KOG0879; Eukaryota.
DR GeneTree; ENSGT00940000154721; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; P52018; -.
DR OMA; RHPNNPV; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P52018; -.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:P52018; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000887; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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..183
FT /note="Peptidyl-prolyl cis-trans isomerase 11"
FT /id="PRO_0000064198"
FT DOMAIN 20..182
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 183 AA; 20193 MW; 23549C922828C533 CRC64;
MTEYDKFAEQ LRHPDNPIVF LEVTAGGAPI GTIVIELFAD VTPRTAENFR QFCTGEYKKD
GVPNGYKNCT FHRVIKDFMI QGGDFCNGDG TGLMSIYGSK FRDENFELKH IGPGMLSMAN
AGSDTNGCQF FITCAKTDFL DNKHVVFGRV LDGMLTVRKI ENVPTGANNK PKLPIVVVQC
GQL