ID   CYP8_CAEEL              Reviewed;         447 AA.
AC   P52016; Q95QQ0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 8;
DE            Short=PPIase 8;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-8 {ECO:0000303|PubMed:8694762};
DE            Short=CYP-8 {ECO:0000303|PubMed:8694762};
DE   AltName: Full=Rotamase 8;
GN   Name=cyn-8 {ECO:0000312|WormBase:D1009.2};
GN   Synonyms=cyp-8 {ECO:0000312|WormBase:D1009.2};
GN   ORFNames=D1009.2 {ECO:0000312|WormBase:D1009.2};
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], AND FUNCTION.
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: May catalyze the cis-trans isomerization of proline imidic
CC       peptide bonds in oligopeptides (PubMed:8694762). May play a role in the
CC       protein folding, transport and assembly (PubMed:8694762).
CC       {ECO:0000269|PubMed:8694762, ECO:0000303|PubMed:8694762}.
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; U31078; AAC47130.1; -; mRNA.
DR   EMBL; BX284606; CCD64414.1; -; Genomic_DNA.
DR   PIR; T18575; T18575.
DR   RefSeq; NP_509506.1; NM_077105.4.
DR   RefSeq; NP_509507.1; NM_077106.1.
DR   AlphaFoldDB; P52016; -.
DR   SMR; P52016; -.
DR   STRING; 6239.D1009.2a; -.
DR   iPTMnet; P52016; -.
DR   EPD; P52016; -.
DR   PaxDb; P52016; -.
DR   PeptideAtlas; P52016; -.
DR   PRIDE; P52016; -.
DR   EnsemblMetazoa; D1009.2.1; D1009.2.1; WBGene00000884.
DR   EnsemblMetazoa; D1009.2.2; D1009.2.2; WBGene00000884.
DR   GeneID; 181136; -.
DR   KEGG; cel:CELE_D1009.2; -.
DR   UCSC; D1009.2a; c. elegans.
DR   CTD; 181136; -.
DR   WormBase; D1009.2; CE27892; WBGene00000884; cyn-8.
DR   eggNOG; KOG0546; Eukaryota.
DR   InParanoid; P52016; -.
DR   OrthoDB; 1403619at2759; -.
DR   PRO; PR:P52016; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00000884; 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:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:WormBase.
DR   GO; GO:0006457; P:protein folding; ISS:WormBase.
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; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 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   Coiled coil; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..447
FT                   /note="Peptidyl-prolyl cis-trans isomerase 8"
FT                   /id="PRO_0000064195"
FT   DOMAIN          12..175
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          186..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          326..401
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        196..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..426
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        293
FT                   /note="S -> SSAPVNVKKKTQMKSPNFVH (in Ref. 1; AAC47130)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  51443 MW;  A246463F9A40AB42 CRC64;
     MPPEVRGNKR AFFDISINGE PAGRIVFSLW NHCCPRTVEN FRAFCTGELG KMNGHYASYQ
     GSVFHRVIKG FMIQGGDITH GNGTGGYSIY GRTFDDENLA LKHKKPYLLS MANRGPDTNG
     SQFFITSEEV PHLDGKHCVF GEVIKGVEVV KAIENLETGN EDKPVCKVEI THCGEMVRKG
     DVVGNAGAAA SEPEPTGVKM EDEPKTRNWL MRYSKSPESR EEKKKDKHGR EEKRDRRRRS
     NDRHGRDRRS RSRSQSRDRN RRRDDRSGRD GRVGRNERDD RSGRDERRDD RRSAPTKDGI
     KVRGRGKLTF LGGRTRSTTP PHWKREESKK LTLEAHQKRQ EELEERQKRA AQREKEEAER
     NARLEKERVE RQNQRELERQ KQEAERELKR QQENEESGNR RRRRSSRSGS ENDESELEEP
     KNRSASPRKR SSSSSSSSSS GHSSDSD