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P52011 (CYP3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase 3

Short name=PPIase 3
EC=5.2.1.8
Alternative name(s):
Cyclophilin-3
Rotamase 3
Gene names
Name:cyn-3
Synonyms:cyp-3
ORF Names:Y75B12B.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Tissue specificity

Exclusively expressed in the single anterior excretory cell. Ref.3

Developmental stage

During early larval development, peaking at the second larval stage, and dropping off in later development. Ref.3

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CELE_K09E4.1Q9NAP84EBI-2419150,EBI-2419154

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 173173Peptidyl-prolyl cis-trans isomerase 3
PRO_0000064192

Regions

Domain7 – 170164PPIase cyclophilin-type

Secondary structure

.................................. 173
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52011 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 39994FEF4941DEC3

FASTA17318,550
        10         20         30         40         50         60 
MSRSKVFFDI TIGGKASGRI VMELYDDVVP KTAGNFRALC TGENGIGKSG KPLHFKGSKF 

        70         80         90        100        110        120 
HRIIPNFMIQ GGDFTRGNGT GGESIYGEKF PDENFKEKHT GPGVLSMANA GPNTNGSQFF 

       130        140        150        160        170 
LCTVKTEWLD GKHVVFGRVV EGLDVVKAVE SNGSQSGKPV KDCMIADCGQ LKA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans."
Page A.P., Macniven K., Hengartner M.O.
Biochem. J. 317:179-185(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Bristol N2.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans."
Dornan J., Page A.P., Taylor P., Wu S., Winter A.D., Husi H., Walkinshaw M.D.
J. Biol. Chem. 274:34877-34883(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]"First crystal structure of a medicinally relevant gold protein complex: unexpected binding of [Au(PEt3)]+ to histidine."
Zou J., Taylor P., Dornan J., Robinson S.P., Walkinshaw M.D., Sadler P.J.
Angew. Chem. Int. Ed. 39:2931-2934(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN A COMPLEX WITH GOLD.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31077 mRNA. Translation: AAC47129.1.
AL032663 Genomic DNA. Translation: CAA21762.1.
PIRT27373.
RefSeqNP_506751.1. NM_074350.6.
UniGeneCel.6363.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYWX-ray1.80A1-173[»]
1E3BX-ray1.85A1-173[»]
1E8KX-ray1.90A1-173[»]
2IGVX-ray1.67A1-173[»]
2IGWX-ray1.78A1-173[»]
ProteinModelPortalP52011.
SMRP52011. Positions 1-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP52011. 1 interaction.
STRING6239.Y75B12B.5.1.

Proteomic databases

PaxDbP52011.
PRIDEP52011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaY75B12B.5; Y75B12B.5; WBGene00000879.
GeneID180028.
KEGGcel:CELE_Y75B12B.5.
UCSCY75B12B.5.1. c. elegans.

Organism-specific databases

CTD180028.
WormBaseY75B12B.5; CE20374; WBGene00000879; cyn-3.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00750000117619.
HOGENOMHOG000065981.
InParanoidP52011.
KOK01802.
OMANFAKKHE.
OrthoDBEOG79GT7W.
PhylomeDBP52011.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52011.
NextBio907804.

Entry information

Entry nameCYP3_CAEEL
AccessionPrimary (citable) accession number: P52011
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase