P38657 · PDIA3_BOVIN

  • Protein
    Protein disulfide-isomerase A3
  • Gene
    PDIA3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone. Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity.

Caution

Was originally thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha).

Catalytic activity

  • Catalyzes the rearrangement of -S-S- bonds in proteins.
    EC:5.3.4.1 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, site.

150550100150200250300350400450500
TypeIDPosition(s)Description
Active site57Nucleophile
Site58Contributes to redox potential value
Site59Contributes to redox potential value
Active site60Nucleophile
Site119Lowers pKa of C-terminal Cys of first active site
Active site406Nucleophile
Site407Contributes to redox potential value
Site408Contributes to redox potential value
Active site409Nucleophile
Site471Lowers pKa of C-terminal Cys of second active site

GO annotations

AspectTerm
Cellular Componentcell surface
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum lumen
Cellular Componentmelanosome
Molecular Functionprotein disulfide isomerase activity
Biological Processadaptive immune response
Biological Processpositive regulation of apoptotic process
Biological Processprotein folding
Biological Processresponse to endoplasmic reticulum stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein disulfide-isomerase A3
  • EC number
  • Alternative names
    • 58 kDa glucose-regulated protein
    • 58 kDa microsomal protein (p58)
    • Disulfide isomerase ER-60
    • Endoplasmic reticulum resident protein 57 (ER protein 57; ERp57)
    • Endoplasmic reticulum resident protein 60 (ER protein 60; ERp60)

Gene names

    • Name
      PDIA3
    • Synonyms
      GRP58

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P38657

Proteomes

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_000003422425-505Protein disulfide-isomerase A3
Disulfide bond57Interchain (with TAPBP); in linked form; reversible
Disulfide bond57↔60Redox-active; reversible
Modified residue61N6-methyllysine
Disulfide bond85↔92
Modified residue129N6-succinyllysine
Modified residue152N6-acetyllysine
Modified residue218N6-succinyllysine
Modified residue252N6-acetyllysine
Modified residue319Phosphothreonine
Modified residue362N6-acetyllysine
Disulfide bond406↔409Redox-active
Modified residue494N6-acetyllysine

Post-translational modification

Within the major histocompatibility complex class I (MHC I) peptide loading complex forms reversible disulfide-linked heterodimers with TAPBP as part of its protein folding chaperone activity. This is essential to assist the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum.
Phosphorylated.

Keywords

Proteomic databases

Interaction

Subunit

Part of the major histocompatibility complex class I (MHC I) peptide loading complex composed of TAP1, TAP2, B2M, MHC heavy chain, TAPBP, PDIA3, and CALR. Interacts with ERP27 and CANX. Interacts with SERPINA2 and with SERPINA1 (By similarity).
Interacts with ATP2A2 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Domain25-133Thioredoxin 1
Domain343-485Thioredoxin 2
Region484-505Disordered
Compositional bias487-505Basic and acidic residues
Motif502-505Prevents 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
    505
  • Mass (Da)
    56,930
  • Last updated
    1995-02-01 v1
  • Checksum
    A85911748DC70A23
MRLRRLALFPGLALLLAAARLAAASDVLELTDDNFESRITDTGSSGLMLVEFFAPWCGHCKKLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEESGAYDGPRTADGIVSHLKKQAGPASVPLKSEEEFEKFISDKDASVVGFFKDLFSEAHSEFLKAASNLRDNYRFAHTNVESLVNKYDDDGEGITLFRPSHLTNKFEDKTVAYTEQKMTSGKIKRFIQENIFGICPHMTEDNKDLLQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGQKLHFAVASRKTFSHELSDFGLESTTGEIPVVAVRTAKGEKFVMQEEFSRDGKALERFLEDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLRKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKQNPKKYEGGRELSDFISYLKREATNPPVIQEEKPKKKKKAQEDL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias487-505Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D16235
EMBL· GenBank· DDBJ
BAA03760.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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