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Reviewed, UniProtKB/Swiss-Prot P35627 (CYPX_USEUD)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin
    Cyclosporin A-binding protein
OrganismUnspecified eudicot DB-1992
Taxonomic identifier323200 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledons

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 Probable.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Caution

Was originally (Ref.1) reported to be isolated from an A.thaliana cDNA library. Ref.2 authors have assigned that the sequence has been amplified from an other contaminating organism.

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 – 169169Peptidyl-prolyl cis-trans isomerase
PRO_0000064139

Regions

Domain5 – 168164PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
P35627-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: B6077FC139864931

FASTA16918,161
        10         20         30         40         50         60 
MAHCFFDMTI GGQPAGRIIM ELFPDVPKTA ENFRALCTGE KGIGPSGKKM TYEGSVFHRV 

        70         80         90        100        110        120 
IPKFMLQGGD FTLGNGRGGE SIYGAKFADE NFIHKHTTPG LLSMANAGPG TNGSQFFITT 

       130        140        150        160 
VATPHLDGKH VVFGKVVEGM DVVRKIEATQ TDRGDKPLSE VKIAKCGQL 

« Hide

References

[1]"Nucleotide sequence of a cDNA encoding an Arabidopsis cyclophilin-like protein."
Bartling D., Heese A., Weiler E.W.
Plant Mol. Biol. 19:529-530(1992) [PubMed: 1623198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
[2]"Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins."
Chou I.T., Gasser C.S.
Plant Mol. Biol. 35:873-892(1997) [PubMed: 9426607] [Abstract]
Cited for: DISCUSSION OF ORIGIN OF SEQUENCE.

Cross-references

Sequence databases

X63616 mRNA. Translation: CAA45161.1.
PIRS22496.

3D structure databases

HSSPHSSP built from PDB template 1E3B based on UniProtKB P52011.
ModBaseSearch...

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYPX_USEUD
AccessionPrimary (citable) accession number: P35627
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents