A0A1S3A634 · A0A1S3A634_ERIEU
- ProteinProtein disulfide-isomerase A6
- GenePDIA6
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids440 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.
Catalytic activity
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Molecular Function | protein disulfide isomerase activity | |
Molecular Function | protein-disulfide reductase activity | |
Biological Process | response to endoplasmic reticulum stress |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein disulfide-isomerase A6
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Eulipotyphla > Erinaceidae > Erinaceinae > Erinaceus
Accessions
- Primary accessionA0A1S3A634
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MALPVIGLVACTFFLSVNG | ||||||
Chain | PRO_5010349651 | 20-440 | Protein disulfide-isomerase A6 | |||
Sequence: LYSSSDDVIELTPSNFNQEVIQSNSLWLVEFYAPWCGHCQRLTPEWKKAASALKGVVKVGAVNADKHQSLGGQYGVQGFPTIKIFGSNKNRAEDYQGGRTSEAIVDAALTALRQLVKDRLAGRDGGYSSGKQGRSESSSKKDVIELTDDNFDTNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAATEVKDQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPMDYDGGRTKSDIVSRALDLFSDNAPPPELLEIVNEDIAKKTCEEHQLCVVAVLPHILDTGATGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQSDLENALGIGGFGYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGTFPTISTREPWDGKDGELPVEDDIDLSDVELDDFENDEL |
Interaction
Subunit
Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with MICA on the surface of tumor cells, leading to MICA disulfide bond reduction which is required for its release from tumor cells. Interacts with ITGB3 following platelet stimulation. Interacts with ERN1; the interaction is direct. Interacts with EIF2AK3.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-133 | Thioredoxin | ||||
Sequence: PVIGLVACTFFLSVNGLYSSSDDVIELTPSNFNQEVIQSNSLWLVEFYAPWCGHCQRLTPEWKKAASALKGVVKVGAVNADKHQSLGGQYGVQGFPTIKIFGSNKNRAEDYQGGRTSEAIVDAALTALRQ | ||||||
Domain | 154-287 | Thioredoxin | ||||
Sequence: SESSSKKDVIELTDDNFDTNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAATEVKDQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPMDYDGGRTKSDIVSRALDLFSDNAPPPELLEIVNEDIA | ||||||
Region | 399-423 | Disordered | ||||
Sequence: GGGTFPTISTREPWDGKDGELPVED |
Sequence similarities
Belongs to the protein disulfide isomerase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length440
- Mass (Da)48,113
- Last updated2017-04-12 v1
- Checksum650948A8286109B1
Keywords
- Technical term