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P52013 (CYP5_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase 5
Short name=PPIase 5
EC=5.2.1.8
Alternative name(s):
Cyclophilin-5
Rotamase 5
Gene names
Name:cyn-5
Synonyms:cyp-5
ORF Names:F31C3.1
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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). Ref.3

Subcellular location

Cytoplasm Ref.3.

Tissue specificity

Embryonic, larval and adult gut cells. Ref.3

Developmental stage

Throughout development, highest in embryos. Ref.3

Induction

Inhibited by cyclosporin. Ref.3

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Mass spectrometry

Molecular mass is 20766 Da from positions 23 - 204. Determined by MALDI. Ref.3

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainSignal
   Molecular functionIsomerase
Rotamase
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from direct assay Ref.3. Source: WormBase

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.3
Chain23 – 204182Peptidyl-prolyl cis-trans isomerase 5
PRO_0000025495

Regions

Domain32 – 189158PPIase cyclophilin-type

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict4 – 1815LLVVA…GALAQ → FLLWRPCSLSELLLR in AAC47126. Ref.1

Secondary structure

1 .................................. 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52013 [UniParc].

Last modified June 20, 2003. Version 2.
Checksum: 6216192BFE1FB493

FASTA20421,927
        10         20         30         40         50         60 
MKSLLVVAAV LAVGALAQGD DAKGPKVTDK VYFDMEIGGK PIGRIVIGLF GKTVPKTATN 

        70         80         90        100        110        120 
FIELAKKPKG EGYPGSKFHR VIADFMIQGG DFTRGDGTGG RSIYGEKFAD ENFKLKHYGA 

       130        140        150        160        170        180 
GWLSMANAGA DTNGSQFFIT TVKTPWLDGR HVVFGKILEG MDVVRKIEQT EKLPGDRPKQ 

       190        200 
DVIIAASGHI AVDTPFSVER EAVV

« 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: 8694762] [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: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Structural and biological characterisation of the gut-associated cyclophilin B isoforms from Caenorhabditis elegans."
Picken N.C., Eschenlauer S., Taylor P., Page A.P., Walkinshaw M.D.
J. Mol. Biol. 322:15-25(2002) [PubMed: 12215411] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-27, X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 23-204, MASS SPECTROMETRY, ENZYME ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U31948 mRNA. Translation: AAC47126.1.
Z92784 Genomic DNA. Translation: CAB07192.1.
PIRT21587.
RefSeqNP_493624.1. NM_061223.4.
UniGeneCel.6652.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0PX-ray1.75A23-204[»]
ProteinModelPortalP52013.
SMRP52013. Positions 23-204.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-24378N.
MINTMINT-1065973.
STRINGP52013.

2D gel databases

World-2DPAGE0020:P52013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF31C3.1.1; F31C3.1.1; F31C3.1.
F31C3.1.2; F31C3.1.2; F31C3.1.
GeneID173374.
KEGGcel:F31C3.1.
UCSCF31C3.1.1. c. elegans.

Organism-specific databases

CTD173374.
WormBaseF31C3.1; CE17730; WBGene00000881; cyn-5.

Phylogenomic databases

eggNOGmeNOG10184.
GeneTreeEMGT00050000000009.
HOGENOMHBG610621.
InParanoidP52013.
OMASMANSGE.
PhylomeDBP52013.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KOK03768.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio879385.

Entry information

Entry nameCYP5_CAEEL
AccessionPrimary (citable) accession number: P52013
Secondary accession number(s): O62190
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 20, 2003
Last modified: January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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