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Q39613 (CYPH_CATRO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase

Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Rotamase
Gene names
Name:PCKR1
OrganismCatharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Taxonomic identifier4058 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeCatharanthus

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
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).

Enzyme regulation

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-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

Chain1 – 172172Peptidyl-prolyl cis-trans isomerase
PRO_0000064143

Regions

Domain7 – 170164PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
Q39613 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EA6EC51886A50A81

FASTA17218,285
        10         20         30         40         50         60 
MPNPRVFFDM SVGGQPAGRI VMELFADTTP RTAENFRALC TGEKGTGRSG KPLHYKDSSF 

        70         80         90        100        110        120 
HRVIPGFMCQ GGDFTAGNGT GGESIYGAKF ADENFIKKHT GPGILSMANA GPNTNGSQFF 

       130        140        150        160        170 
ICTAKTEWLD GKHVVFGQVV EGMDVVKAIE KVGSSSGRTA KKVVVEDCGQ LS 

« Hide

References

[1]"Isolation of a full-length cDNA encoding a cytosolic cyclophilin from Periwinkle (Catharanthus roseus)."
Clastre M., Maaroufi H., Andreu F., Chenieux J.-C., Rideau M., Hamdi S.
Plant Gene Register PGR95-100
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85185 mRNA. Translation: CAA59468.1.
PIRT10056.

3D structure databases

ProteinModelPortalQ39613.
SMRQ39613. Positions 1-172.
ModBaseSearch...

Protein family/group databases

Allergome2900. Cat r 1.
3181. Cat r 1.0101.

Proteomic databases

PRIDEQ39613.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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...

Entry information

Entry nameCYPH_CATRO
AccessionPrimary (citable) accession number: Q39613
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families