CYP3_CAEEL
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 03-AUG-2022, entry version 148.
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; 57.
DR IntAct; P52011; 1.
DR STRING; 6239.Y75B12B.5; -.
DR EPD; P52011; -.
DR PaxDb; P52011; -.
DR PeptideAtlas; P52011; -.
DR PRIDE; 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 CTD; 180028; -.
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; SIVSMRV; -.
DR OrthoDB; 1403619at2759; -.
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 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 GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:WormBase.
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 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
