P09102 · PDIA1_CHICK
- ProteinProtein disulfide-isomerase
- GeneP4HB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids515 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 58 | Nucleophile | ||||
Sequence: C | ||||||
Site | 59 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 60 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 61 | Nucleophile | ||||
Sequence: C | ||||||
Site | 125 | Lowers pKa of C-terminal Cys of first active site | ||||
Sequence: R | ||||||
Active site | 402 | Nucleophile | ||||
Sequence: C | ||||||
Site | 403 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 404 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 405 | Nucleophile | ||||
Sequence: C | ||||||
Site | 466 | Lowers pKa of C-terminal Cys of second active site | ||||
Sequence: R |
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 | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | external side of plasma membrane | |
Molecular Function | protein disulfide isomerase activity | |
Biological Process | protein folding | |
Biological Process | response to endoplasmic reticulum stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein disulfide-isomerase
- EC number
- Short namesPDI
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionP09102
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MAVVRVRAIVALLCLVAALGLA | ||||||
Chain | PRO_0000034200 | 23-515 | Protein disulfide-isomerase | |||
Sequence: EPLEEEDGVLVLRAANFEQALAAHRHLLVEFYAPWCGHCKALAPEYAKAAAQLKAEGSEIRLAKVDATEEAELAQQFGVRGYPTIKFFRNGDKAAPREYTAGREADDIVSWLKKRTGPAATTLTDAAAAETLVDSSEVVVIGFFKDVTSDAAKEFLLAAESVDDIPFGISSSADVFSKYQLSQDGVVLFKKFDEGRNNFEGDLTKDNLLNFIKSNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYEGKLDNFKTAAGNFKGKILFIFIDSDHSDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDDLTADKIKEFCNKFLEGKIKPHLMSQDLPEDWDKQPVKVLVGKNFEEVAFDENKNVFVEFYAPWCGHCKQLAPIWDKLGETYRDHENIVIAKMDSTANEVEAVKIHSFPTLKFFPAGSGRNVIDYNGERTLEGFKKFLESGGQDGAAADDDLEDLETDEETDLEEGDDDEQKIQKDEL | ||||||
Disulfide bond | 58↔61 | Redox-active | ||||
Sequence: CGHC | ||||||
Disulfide bond | 402↔405 | Redox-active | ||||
Sequence: CGHC |
Keywords
- PTM
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-139 | Thioredoxin 1 | ||||
Sequence: EPLEEEDGVLVLRAANFEQALAAHRHLLVEFYAPWCGHCKALAPEYAKAAAQLKAEGSEIRLAKVDATEEAELAQQFGVRGYPTIKFFRNGDKAAPREYTAGREADDIVSWLKKRTG | ||||||
Domain | 351-480 | Thioredoxin 2 | ||||
Sequence: FLEGKIKPHLMSQDLPEDWDKQPVKVLVGKNFEEVAFDENKNVFVEFYAPWCGHCKQLAPIWDKLGETYRDHENIVIAKMDSTANEVEAVKIHSFPTLKFFPAGSGRNVIDYNGERTLEGFKKFLESGGQ | ||||||
Region | 477-515 | Disordered | ||||
Sequence: SGGQDGAAADDDLEDLETDEETDLEEGDDDEQKIQKDEL | ||||||
Compositional bias | 483-515 | Acidic residues | ||||
Sequence: AAADDDLEDLETDEETDLEEGDDDEQKIQKDEL | ||||||
Motif | 512-515 | Prevents secretion from ER | ||||
Sequence: KDEL |
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.
- Length515
- Mass (Da)57,410
- Last updated2003-05-16 v3
- ChecksumE7CC978A5109C2CE
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 23 | in Ref. 1 and 3 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 94-95 | in Ref. 3 | ||||
Sequence: EL → DV | ||||||
Sequence conflict | 359 | in Ref. 3 | ||||
Sequence: H → Q | ||||||
Sequence conflict | 447 | in Ref. 5; CAB57801 | ||||
Sequence: T → M | ||||||
Compositional bias | 483-515 | Acidic residues | ||||
Sequence: AAADDDLEDLETDEETDLEEGDDDEQKIQKDEL |
Keywords
- Technical term