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P52014 (CYP6_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase 6

Short name=PPIase 6
EC=5.2.1.8
Alternative name(s):
Cyclophilin-6
Rotamase 6
Gene names
Name:cyn-6
Synonyms:cyp-6
ORF Names:F42G9.2
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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).

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   DomainSignal
   Molecular functionIsomerase
Rotamase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 1616 Potential
Chain17 – 201185Peptidyl-prolyl cis-trans isomerase 6
PRO_0000025496

Regions

Domain29 – 186158PPIase cyclophilin-type

Amino acid modifications

Glycosylation1301N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P52014 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 084C5762917F958B

FASTA20121,864
        10         20         30         40         50         60 
MSRALLFFVL AILALSAEAR GPRVTDKVFF DMEIGGRPVG KIVIGLFGEV VPKTVKNFVE 

        70         80         90        100        110        120 
LAQRAEGEGY VGSKFHRVIE NFMIQGGDFT RGDGTGGRSI YGERFEDENF KLQHYGPGWL 

       130        140        150        160        170        180 
SMANAGEDTN GSQFFITTAK TSWLDGKHVV FGKILEGMDV VREIEATPKG AGDRPIEDVV 

       190        200 
IANAGHIPVE NPFTVARAGV N 

« 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27354 mRNA. Translation: AAC47124.1.
FO080196 Genomic DNA. Translation: CCD61884.1.
PIRT18573.
RefSeqNP_497257.1. NM_064856.5.
UniGeneCel.23333.

3D structure databases

ProteinModelPortalP52014.
SMRP52014. Positions 20-200.
ModBaseSearch...

Protein-protein interaction databases

IntActP52014. 1 interaction.
STRINGP52014.

Proteomic databases

PRIDEP52014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF42G9.2; F42G9.2; F42G9.2.
GeneID175231.
KEGGcel:F42G9.2.
UCSCF42G9.2. c. elegans.

Organism-specific databases

CTD175231.
WormBaseF42G9.2; CE01301; WBGene00000882; cyn-6.

Phylogenomic databases

eggNOGmeNOG10184.
GeneTreeEMGT00050000000009.
HOGENOMHBG610621.
InParanoidP52014.
OMAVGSKFHR.
PhylomeDBP52014.

Gene expression databases

ArrayExpressP52014.

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

NextBio887330.

Entry information

Entry nameCYP6_CAEEL
AccessionPrimary (citable) accession number: P52014
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 73 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families