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Q5SVY2 · Q5SVY2_MOUSE

  • Protein
    Peptidyl-prolyl cis-trans isomerase
  • Gene
    Ppia
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

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

Catalytic activity

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 Componentcytoplasm
Cellular Componentextracellular region
Cellular Componentnucleus
Cellular Componentprotein-containing complex
Molecular Functionheparan sulfate binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Biological Processactivation of protein kinase B activity
Biological Processapoptotic process
Biological Processcell adhesion molecule production
Biological Processcellular response to oxidative stress
Biological Processendothelial cell activation
Biological Processlipid droplet organization
Biological Processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
Biological Processnegative regulation of protein K48-linked ubiquitination
Biological Processnegative regulation of protein kinase activity
Biological Processnegative regulation of stress-activated MAPK cascade
Biological Processnegative regulation of viral life cycle
Biological Processneutrophil chemotaxis
Biological Processpositive regulation of MAPK cascade
Biological Processpositive regulation of NF-kappaB transcription factor activity
Biological Processpositive regulation of protein dephosphorylation
Biological Processpositive regulation of protein secretion
Biological Processpositive regulation of viral genome replication
Biological Processprotein folding
Biological Processprotein peptidyl-prolyl isomerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase
  • EC number
  • Short names
    PPIase

Gene names

    • Name
      Ppia

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • C57BL/6J
    • DBA/2
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q5SVY2

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Proteomic databases

Expression

Gene expression databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-163PPIase cyclophilin-type

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    164
  • Mass (Da)
    17,971
  • Last updated
    2005-05-10 v1
  • MD5 Checksum
    86D840EA27B9DD381720F76B6DAAAB50
MVNPTVFFDITADDEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC087928
EMBL· GenBank· DDBJ
AAH87928.1
EMBL· GenBank· DDBJ
mRNA
BC094272
EMBL· GenBank· DDBJ
AAH94272.1
EMBL· GenBank· DDBJ
mRNA
BC094632
EMBL· GenBank· DDBJ
AAH94632.1
EMBL· GenBank· DDBJ
mRNA
BC099478
EMBL· GenBank· DDBJ
AAH99478.1
EMBL· GenBank· DDBJ
mRNA
DQ985731
EMBL· GenBank· DDBJ
ABL77398.1
EMBL· GenBank· DDBJ
mRNA
AK131942
EMBL· GenBank· DDBJ
BAE20888.1
EMBL· GenBank· DDBJ
mRNA
AK136788
EMBL· GenBank· DDBJ
BAE23129.1
EMBL· GenBank· DDBJ
mRNA
AK151583
EMBL· GenBank· DDBJ
BAE30523.1
EMBL· GenBank· DDBJ
mRNA
AK153030
EMBL· GenBank· DDBJ
BAE31662.1
EMBL· GenBank· DDBJ
mRNA
AK160631
EMBL· GenBank· DDBJ
BAE35927.1
EMBL· GenBank· DDBJ
mRNA
AK160780
EMBL· GenBank· DDBJ
BAE36004.1
EMBL· GenBank· DDBJ
mRNA
AK168035
EMBL· GenBank· DDBJ
BAE40018.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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