P09102 · PDIA1_CHICK

  • Protein
    Protein disulfide-isomerase
  • Gene
    P4HB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase (By similarity).

Catalytic activity

Features

Showing features for active site, site.

151550100150200250300350400450500
TypeIDPosition(s)Description
Active site58Nucleophile
Site59Contributes to redox potential value
Site60Contributes to redox potential value
Active site61Nucleophile
Site125Lowers pKa of C-terminal Cys of first active site
Active site402Nucleophile
Site403Contributes to redox potential value
Site404Contributes to redox potential value
Active site405Nucleophile
Site466Lowers pKa of C-terminal Cys of second active site

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 Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum lumen
Cellular Componentexternal side of plasma membrane
Molecular Functionprotein disulfide isomerase activity
Biological Processprotein folding
Biological Processresponse to endoplasmic reticulum stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein disulfide-isomerase
  • EC number
  • Short names
    PDI
  • Alternative names
    • Cellular thyroid hormone-binding protein
    • Prolyl 4-hydroxylase subunit beta
    • Retina cognin (R-cognin)

Gene names

    • Name
      P4HB
    • Synonyms
      PDI, PDIA1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus

Accessions

  • Primary accession
    P09102
  • Secondary accessions
    • Q90969

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_000003420023-515Protein disulfide-isomerase
Disulfide bond58↔61Redox-active
Disulfide bond402↔405Redox-active

Keywords

Proteomic databases

Interaction

Subunit

Heterodimer; heterodimerizes with the protein microsomal triglyceride transfer MTTP. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase. Stabilizes this enzyme and retains it in the ER without contributing to the catalytic activity. Binds UBQLN1 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias, motif.

TypeIDPosition(s)Description
Domain23-139Thioredoxin 1
Domain351-480Thioredoxin 2
Region477-515Disordered
Compositional bias483-515Acidic residues
Motif512-515Prevents secretion from ER

Sequence similarities

Belongs to the protein disulfide isomerase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    515
  • Mass (Da)
    57,410
  • Last updated
    2003-05-16 v3
  • Checksum
    E7CC978A5109C2CE
MAVVRVRAIVALLCLVAALGLAEPLEEEDGVLVLRAANFEQALAAHRHLLVEFYAPWCGHCKALAPEYAKAAAQLKAEGSEIRLAKVDATEEAELAQQFGVRGYPTIKFFRNGDKAAPREYTAGREADDIVSWLKKRTGPAATTLTDAAAAETLVDSSEVVVIGFFKDVTSDAAKEFLLAAESVDDIPFGISSSADVFSKYQLSQDGVVLFKKFDEGRNNFEGDLTKDNLLNFIKSNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYEGKLDNFKTAAGNFKGKILFIFIDSDHSDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDDLTADKIKEFCNKFLEGKIKPHLMSQDLPEDWDKQPVKVLVGKNFEEVAFDENKNVFVEFYAPWCGHCKQLAPIWDKLGETYRDHENIVIAKMDSTANEVEAVKIHSFPTLKFFPAGSGRNVIDYNGERTLEGFKKFLESGGQDGAAADDDLEDLETDEETDLEEGDDDEQKIQKDEL

Sequence caution

The sequence AAA49054.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict23in Ref. 1 and 3
Sequence conflict94-95in Ref. 3
Sequence conflict359in Ref. 3
Sequence conflict447in Ref. 5; CAB57801
Compositional bias483-515Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L11147
EMBL· GenBank· DDBJ
AAA49054.2
EMBL· GenBank· DDBJ
mRNA Different initiation
X13110
EMBL· GenBank· DDBJ
CAA31502.1
EMBL· GenBank· DDBJ
mRNA
X06768
EMBL· GenBank· DDBJ
CAB57801.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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