ID   CYP3_CAEEL              Reviewed;         173 AA.
AC   P52011;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 3;
DE            Short=PPIase 3;
DE            EC=5.2.1.8 {ECO:0000269|PubMed:10574961, ECO:0000269|PubMed:8694762};
DE   AltName: Full=Cyclophilin-3 {ECO:0000303|PubMed:10574961};
DE            Short=CYP-3 {ECO:0000303|PubMed:10574961, ECO:0000303|PubMed:8694762};
DE   AltName: Full=Rotamase 3;
GN   Name=cyn-3; Synonyms=cyp-3; ORFNames=Y75B12B.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], FUNCTION, AND CATALYTIC ACTIVITY.
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   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10574961; DOI=10.1074/jbc.274.49.34877;
RA   Dornan J., Page A.P., Taylor P., Wu S., Winter A.D., Husi H.,
RA   Walkinshaw M.D.;
RT   "Biochemical and structural characterization of a divergent loop
RT   cyclophilin from Caenorhabditis elegans.";
RL   J. Biol. Chem. 274:34877-34883(1999).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN A COMPLEX WITH GOLD.
RX   PubMed=11028014;
RX   DOI=10.1002/1521-3773(20000818)39:16<2931::aid-anie2931>3.0.co;2-w;
RA   Zou J., Taylor P., Dornan J., Robinson S.P., Walkinshaw M.D., Sadler P.J.;
RT   "First crystal structure of a medicinally relevant gold protein complex:
RT   unexpected binding of [Au(PEt3)]+ to histidine.";
RL   Angew. Chem. Int. Ed. 39:2931-2934(2000).
CC   -!- FUNCTION: Catalyzes the cis-trans isomerization of proline imidic
CC       peptide bonds in oligopeptides (PubMed:8694762, PubMed:10574961). Plays
CC       a role in protein folding, transport and assembly (PubMed:8694762,
CC       PubMed:10574961). {ECO:0000269|PubMed:10574961,
CC       ECO:0000269|PubMed:8694762, ECO:0000303|PubMed:10574961,
CC       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; Evidence={ECO:0000269|PubMed:10574961,
CC         ECO:0000269|PubMed:8694762};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16239;
CC         Evidence={ECO:0000269|PubMed:10574961, ECO:0000269|PubMed:8694762};
CC   -!- INTERACTION:
CC       P52011; Q9NAP8: CELE_K09E4.1; NbExp=4; IntAct=EBI-2419150, EBI-2419154;
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in the single anterior
CC       excretory cell. {ECO:0000269|PubMed:10574961}.
CC   -!- DEVELOPMENTAL STAGE: During early larval development, peaking at the
CC       second larval stage, and dropping off in later development.
CC       {ECO:0000269|PubMed:10574961}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; U31077; AAC47129.1; -; mRNA.
DR   EMBL; AL032663; CAA21762.1; -; Genomic_DNA.
DR   PIR; T27373; T27373.
DR   RefSeq; NP_506751.1; NM_074350.6.
DR   PDB; 1DYW; X-ray; 1.80 A; A=1-173.
DR   PDB; 1E3B; X-ray; 1.85 A; A=1-173.
DR   PDB; 1E8K; X-ray; 1.90 A; A=1-173.
DR   PDB; 2IGV; X-ray; 1.67 A; A=1-173.
DR   PDB; 2IGW; X-ray; 1.78 A; A=1-173.
DR   PDBsum; 1DYW; -.
DR   PDBsum; 1E3B; -.
DR   PDBsum; 1E8K; -.
DR   PDBsum; 2IGV; -.
DR   PDBsum; 2IGW; -.
DR   AlphaFoldDB; P52011; -.
DR   SMR; P52011; -.
DR   BioGRID; 45023; 59.
DR   IntAct; P52011; 1.
DR   STRING; 6239.Y75B12B.5.1; -.
DR   EPD; P52011; -.
DR   PaxDb; 6239-Y75B12B-5; -.
DR   PeptideAtlas; P52011; -.
DR   EnsemblMetazoa; Y75B12B.5.1; Y75B12B.5.1; WBGene00000879.
DR   GeneID; 180028; -.
DR   KEGG; cel:CELE_Y75B12B.5; -.
DR   UCSC; Y75B12B.5.1; c. elegans.
DR   AGR; WB:WBGene00000879; -.
DR   WormBase; Y75B12B.5; CE20374; WBGene00000879; cyn-3.
DR   eggNOG; KOG0865; Eukaryota.
DR   GeneTree; ENSGT00940000168914; -.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   InParanoid; P52011; -.
DR   OMA; KEIEMIG; -.
DR   OrthoDB; 339082at2759; -.
DR   PhylomeDB; P52011; -.
DR   EvolutionaryTrace; P52011; -.
DR   PRO; PR:P52011; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000879; Expressed in germ line (C elegans) and 4 other cell types or 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; IDA:WormBase.
DR   GO; GO:0006457; P:protein folding; ISS:WormBase.
DR   CDD; cd01926; cyclophilin_ABH_like; 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:SF578; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 3-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   3D-structure; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..173
FT                   /note="Peptidyl-prolyl cis-trans isomerase 3"
FT                   /id="PRO_0000064192"
FT   DOMAIN          7..170
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   STRAND          5..12
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          15..24
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   HELIX           30..41
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   TURN            130..132
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          135..141
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   HELIX           143..150
FT                   /evidence="ECO:0007829|PDB:2IGV"
FT   STRAND          163..171
FT                   /evidence="ECO:0007829|PDB:2IGV"
SQ   SEQUENCE   173 AA;  18550 MW;  39994FEF4941DEC3 CRC64;
     MSRSKVFFDI TIGGKASGRI VMELYDDVVP KTAGNFRALC TGENGIGKSG KPLHFKGSKF
     HRIIPNFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT GPGVLSMANA GPNTNGSQFF
     LCTVKTEWLD GKHVVFGRVV EGLDVVKAVE SNGSQSGKPV KDCMIADCGQ LKA
//