Q6FKH7 · FKBP3_CANGA

Function

function

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

Activity regulation

Inhibited by both FK506 and rapamycin.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentnucleolus
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    FK506-binding protein 3
  • EC number
  • Alternative names
    • Peptidyl-prolyl cis-trans isomerase (PPIase)
    • Rotamase

Gene names

    • Name
      FPR3
    • Ordered locus names
      CAGL0L11484g

Organism names

Accessions

  • Primary accession
    Q6FKH7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002330771-437FK506-binding protein 3

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region42-146Disordered
Compositional bias65-93Acidic residues
Compositional bias94-111Basic and acidic residues
Compositional bias112-136Acidic residues
Region179-328Disordered
Compositional bias188-250Acidic residues
Compositional bias268-328Basic and acidic residues
Domain351-437PPIase FKBP-type

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    437
  • Mass (Da)
    49,671
  • Last updated
    2004-07-19 v1
  • Checksum
    DEAA67DE23626C91
MSDMLPLATYSLNVLPYIPTPAIDIEMPVTVRITMAALDPEALDDQKQPSTLRIVKRNPNFDDEEYDDLLNGDYDEDEMASDDEEEEEEEEEEEKPAKKSKKSKGKKKDESEDEEEEEESDSDLDEEDDDDEFEEYVLATLSPKTQYQQTLDLTIAPEEEIQFIVTGSYAISLVGNYIKHPFDTPMGDMDDSEDEDGSDYDDELSDSYYNDQYSDDDAEDSDEHDLTPDEDELAPAGSVEEIEASEEEESEEEEKKSKHKKHDHHHHHDHDHDHDHEHKSKNKKRKQEEEEPKKEHKDKKVKFKKDLEEGPTKKEKAESKKADKTPKRRTLEGGVVIEDRTVGDGPAAKKGDRVGMRYIGKLKNGKVFDKNTSGKPFVFKLGRGEVIKGWDVGVAGMSVGSERRIIIPAPYAYGKQALPGIPANSELTFDVKLVSIK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias65-93Acidic residues
Compositional bias94-111Basic and acidic residues
Compositional bias112-136Acidic residues
Compositional bias188-250Acidic residues
Compositional bias268-328Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CR380958
EMBL· GenBank· DDBJ
CAG62241.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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