Q11067 · PDIA6_CAEEL
- ProteinProtein disulfide-isomerase A6 homolog
- Genepdi-6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids440 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
May function as a chaperone that inhibits aggregation of misfolded proteins (By similarity).
May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors (PubMed:24508390).
May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors (PubMed:24508390).
Catalytic activity
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 54 | Nucleophile | ||||
Sequence: C | ||||||
Site | 55 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 56 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 57 | Nucleophile | ||||
Sequence: C | ||||||
Site | 117 | Lowers pKa of C-terminal Cys of first active site | ||||
Sequence: R | ||||||
Active site | 194 | Nucleophile | ||||
Sequence: C | ||||||
Site | 195 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 196 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 197 | Nucleophile | ||||
Sequence: C | ||||||
Site | 259 | Lowers pKa of C-terminal Cys of second active site | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Molecular Function | protein disulfide isomerase activity | |
Molecular Function | protein-disulfide reductase activity | |
Biological Process | endoplasmic reticulum unfolded protein response | |
Biological Process | response to endoplasmic reticulum stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein disulfide-isomerase A6 homolog
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ11067
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Lethal at the early stages of larval development. Arrested larvae are small and display molting defects. RNAi-mediated knockdown results in reduced fecundity, and in induction of the unfolded protein response.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MALIKLLLASLAITSVCG | ||||||
Chain | PRO_0000034241 | 19-440 | Protein disulfide-isomerase A6 homolog | |||
Sequence: MYSKKDDVVELTEANFQSKVINSDDIWIVEFYAPWCGHCKSLVPEYKKAASALKGVAKVGAVDMTQHQSVGGPYNVQGFPTLKIFGADKKKPTDYNGQRTAQAIADSVLAEAKKAVSARLGGKSSGSSSSGSGSGSGKRGGGGSGNEVVELTDANFEDLVLNSKDIWLVEFFAPWCGHCKSLEPQWKAAASELKGKVRLGALDATVHTVVANKFAIRGFPTIKYFAPGSDVSDAQDYDGGRQSSDIVAWASARAQENMPAPEVFEGINQQVVEDACKEKQLCIFAFLPHILDCQSECRNNYLAMLKEQSEKFKKNLWGWIWVEGAAQPALEESFEVGGFGYPAMTALNFRKNKYAVLKGSFGKDGIHEFLRDLSYGKGRTSSLRGDGFPKIQKTEKWDGKDGALPAEDDIDLSDIDLDKTEL | ||||||
Disulfide bond | 54↔57 | Redox-active | ||||
Sequence: CGHC | ||||||
Disulfide bond | 194↔197 | Redox-active | ||||
Sequence: CGHC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-131 | Thioredoxin 1 | ||||
Sequence: MYSKKDDVVELTEANFQSKVINSDDIWIVEFYAPWCGHCKSLVPEYKKAASALKGVAKVGAVDMTQHQSVGGPYNVQGFPTLKIFGADKKKPTDYNGQRTAQAIADSVLAEAK | ||||||
Domain | 127-273 | Thioredoxin 2 | ||||
Sequence: LAEAKKAVSARLGGKSSGSSSSGSGSGSGKRGGGGSGNEVVELTDANFEDLVLNSKDIWLVEFFAPWCGHCKSLEPQWKAAASELKGKVRLGALDATVHTVVANKFAIRGFPTIKYFAPGSDVSDAQDYDGGRQSSDIVAWASARAQ | ||||||
Region | 138-164 | Disordered | ||||
Sequence: LGGKSSGSSSSGSGSGSGKRGGGGSGN | ||||||
Compositional bias | 139-157 | Polar residues | ||||
Sequence: GGKSSGSSSSGSGSGSGKR | ||||||
Region | 404-426 | Disordered | ||||
Sequence: DGFPKIQKTEKWDGKDGALPAED | ||||||
Compositional bias | 407-425 | Basic and acidic residues | ||||
Sequence: PKIQKTEKWDGKDGALPAE | ||||||
Motif | 437-440 | Prevents secretion from ER | ||||
Sequence: KTEL |
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.
- Length440
- Mass (Da)47,728
- Last updated1997-11-01 v1
- Checksum608785076B159578
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 139-157 | Polar residues | ||||
Sequence: GGKSSGSSSSGSGSGSGKR | ||||||
Compositional bias | 407-425 | Basic and acidic residues | ||||
Sequence: PKIQKTEKWDGKDGALPAE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FO080188 EMBL· GenBank· DDBJ | CCD61843.1 EMBL· GenBank· DDBJ | Genomic DNA |