CYP2_CAEEL
ID CYP2_CAEEL Reviewed; 172 AA.
AC P52010; O46022;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase 2;
DE Short=PPIase 2;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-2;
DE AltName: Full=Rotamase 2;
GN Name=cyn-2; Synonyms=cyp-2; ORFNames=ZK520.5;
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; U34354; AAC47127.1; -; mRNA.
DR EMBL; Z92822; CAB07303.1; -; Genomic_DNA.
DR PIR; T27882; T27882.
DR RefSeq; NP_499828.1; NM_067427.5.
DR AlphaFoldDB; P52010; -.
DR SMR; P52010; -.
DR BioGRID; 41973; 2.
DR IntAct; P52010; 1.
DR STRING; 6239.ZK520.5; -.
DR EPD; P52010; -.
DR PaxDb; P52010; -.
DR PeptideAtlas; P52010; -.
DR PRIDE; P52010; -.
DR EnsemblMetazoa; ZK520.5.1; ZK520.5.1; WBGene00000878.
DR GeneID; 176807; -.
DR KEGG; cel:CELE_ZK520.5; -.
DR UCSC; ZK520.5.1; c. elegans.
DR CTD; 176807; -.
DR WormBase; ZK520.5; CE16730; WBGene00000878; cyn-2.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00940000168914; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P52010; -.
DR OMA; NTANNEF; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P52010; -.
DR PRO; PR:P52010; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000878; Expressed in adult organism 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..172
FT /note="Peptidyl-prolyl cis-trans isomerase 2"
FT /id="PRO_0000064191"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CONFLICT 8
FT /note="F -> I (in Ref. 1; AAC47127)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="V -> A (in Ref. 1; AAC47127)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="Missing (in Ref. 1; AAC47127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 18535 MW; 87CB148261CAC2B5 CRC64;
MPRVKVFFDI TIGGKKGGRI VMELYNDIVP KTAENFRALC TGEKGKGKSG KKLHFKGSKF
HRIIPEFMIQ GGDFTEGNGT GGESIHGEKF DDENFKEKHT GPGVLSMANC GANTNGSQFF
LCTVKTTWLD GKHVVFGKVI EGMDVVKAIE SKGSEDGAPS APCVIADCGE MK
