P38657 · PDIA3_BOVIN
- ProteinProtein disulfide-isomerase A3
- GenePDIA3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids505 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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.
Catalytic activity
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 57 | Nucleophile | ||||
Sequence: C | ||||||
Site | 58 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 59 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 60 | Nucleophile | ||||
Sequence: C | ||||||
Site | 119 | Lowers pKa of C-terminal Cys of first active site | ||||
Sequence: R | ||||||
Active site | 406 | Nucleophile | ||||
Sequence: C | ||||||
Site | 407 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 408 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 409 | Nucleophile | ||||
Sequence: C | ||||||
Site | 471 | Lowers pKa of C-terminal Cys of second active site | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | melanosome | |
Molecular Function | protein disulfide isomerase activity | |
Biological Process | adaptive immune response | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | protein folding | |
Biological Process | response to endoplasmic reticulum stress |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein disulfide-isomerase A3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP38657
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MRLRRLALFPGLALLLAAARLAAA | ||||||
Chain | PRO_0000034224 | 25-505 | Protein disulfide-isomerase A3 | |||
Sequence: SDVLELTDDNFESRITDTGSSGLMLVEFFAPWCGHCKKLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEESGAYDGPRTADGIVSHLKKQAGPASVPLKSEEEFEKFISDKDASVVGFFKDLFSEAHSEFLKAASNLRDNYRFAHTNVESLVNKYDDDGEGITLFRPSHLTNKFEDKTVAYTEQKMTSGKIKRFIQENIFGICPHMTEDNKDLLQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGQKLHFAVASRKTFSHELSDFGLESTTGEIPVVAVRTAKGEKFVMQEEFSRDGKALERFLEDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLRKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKQNPKKYEGGRELSDFISYLKREATNPPVIQEEKPKKKKKAQEDL | ||||||
Disulfide bond | 57 | Interchain (with TAPBP); in linked form; reversible | ||||
Sequence: C | ||||||
Disulfide bond | 57↔60 | Redox-active; reversible | ||||
Sequence: CGHC | ||||||
Modified residue | 61 | N6-methyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 85↔92 | |||||
Sequence: CTANTNTC | ||||||
Modified residue | 129 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 152 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 218 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 252 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 319 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 362 | N6-acetyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 406↔409 | Redox-active | ||||
Sequence: CGHC | ||||||
Modified residue | 494 | N6-acetyllysine | ||||
Sequence: K |
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
- PTM
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).
Interacts with ATP2A2 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-133 | Thioredoxin 1 | ||||
Sequence: SDVLELTDDNFESRITDTGSSGLMLVEFFAPWCGHCKKLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEESGAYDGPRTADGIVSHLKKQAG | ||||||
Domain | 343-485 | Thioredoxin 2 | ||||
Sequence: SRDGKALERFLEDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLRKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKQNPKKYEGGRELSDFISYLKREAT | ||||||
Region | 484-505 | Disordered | ||||
Sequence: ATNPPVIQEEKPKKKKKAQEDL | ||||||
Compositional bias | 487-505 | Basic and acidic residues | ||||
Sequence: PPVIQEEKPKKKKKAQEDL | ||||||
Motif | 502-505 | Prevents secretion from ER | ||||
Sequence: QEDL |
Sequence similarities
Belongs to the protein disulfide isomerase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length505
- Mass (Da)56,930
- Last updated1995-02-01 v1
- ChecksumA85911748DC70A23
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 487-505 | Basic and acidic residues | ||||
Sequence: PPVIQEEKPKKKKKAQEDL |
Keywords
- Technical term