ID   CYP10_CAEEL             Reviewed;         161 AA.
AC   P52017; Q95ZZ8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 10;
DE            Short=PPIase 10;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-10;
DE   AltName: Full=Rotamase 10;
GN   Name=cyn-10; Synonyms=cyp-10; ORFNames=B0252.4;
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] (ISOFORM A).
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], AND ALTERNATIVE SPLICING.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b;
CC         IsoId=P52017-1; Sequence=Displayed;
CC       Name=a;
CC         IsoId=P52017-2; Sequence=VSP_005183;
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U34954; AAC47114.1; -; mRNA.
DR   EMBL; FO080139; CCD61541.1; -; Genomic_DNA.
DR   EMBL; FO080139; CCD61542.1; -; Genomic_DNA.
DR   PIR; T18577; T18577.
DR   RefSeq; NP_001021890.1; NM_001026719.4. [P52017-1]
DR   RefSeq; NP_495416.2; NM_063015.3. [P52017-2]
DR   AlphaFoldDB; P52017; -.
DR   SMR; P52017; -.
DR   BioGRID; 39470; 1.
DR   STRING; 6239.B0252.4b; -.
DR   EPD; P52017; -.
DR   PaxDb; P52017; -.
DR   PeptideAtlas; P52017; -.
DR   EnsemblMetazoa; B0252.4a.1; B0252.4a.1; WBGene00000886. [P52017-2]
DR   EnsemblMetazoa; B0252.4b.1; B0252.4b.1; WBGene00000886. [P52017-1]
DR   GeneID; 174132; -.
DR   KEGG; cel:CELE_B0252.4; -.
DR   UCSC; B0252.4b; c. elegans. [P52017-1]
DR   CTD; 174132; -.
DR   WormBase; B0252.4a; CE02420; WBGene00000886; cyn-10. [P52017-2]
DR   WormBase; B0252.4b; CE27567; WBGene00000886; cyn-10. [P52017-1]
DR   eggNOG; KOG0884; Eukaryota.
DR   GeneTree; ENSGT00940000153189; -.
DR   InParanoid; P52017; -.
DR   OMA; VPFHRVM; -.
DR   OrthoDB; 1392223at2759; -.
DR   PhylomeDB; P52017; -.
DR   Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:P52017; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000886; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 1.
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   Alternative splicing; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..161
FT                   /note="Peptidyl-prolyl cis-trans isomerase 10"
FT                   /id="PRO_0000064197"
FT   DOMAIN          1..153
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   VAR_SEQ         148..161
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000303|PubMed:8694762"
FT                   /id="VSP_005183"
SQ   SEQUENCE   161 AA;  17960 MW;  D7D18CA11572DF72 CRC64;
     MSVTLHTTSG DIKIELYVDD APKACENFLA LCASDYYNGC IFHRNIKDFM VQTGDPTHSG
     KGGESIWGGP FEDEFVSALK HDSRGCVSMA NNGPDSNRSQ FFITYAKQAH LDMKYTLFGK
     VIDGFDTLEE IETIKVDNKY RPLVQQKIQN VTIHANPMAA D