Reviewed,
UniProtKB/Swiss-Prot P38660 (PDIA6_MESAU)
Last modified
September 22, 2009.
Version 67.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Protein disulfide-isomerase A6 EC=5.3.4.1 Alternative name(s): Protein disulfide isomerase P5 | ||
| Gene names |
| ||
| Organism | Mesocricetus auratus (Golden hamster) | ||
| Taxonomic identifier | 10036 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus |
Protein attributes
| Sequence length | 439 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Catalyzes the rearrangement of -S-S- bonds in proteins. |
| Subcellular location | Endoplasmic reticulum lumen By similarity. Melanosome By similarity. |
| Tissue specificity | Expressed most abundantly in lung and kidney, followed by heart, liver and brain. |
| Sequence similarities | Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Redox-active center Repeat Signal |
| Molecular function | Isomerase |
| PTM | Disulfide bond Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro |
| Cellular component | endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell melanosomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein disulfide isomerase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Ref.1 | ||||||||
| Chain | 20 – 439 | 420 | Protein disulfide-isomerase A6 | PRO_0000034237 | |||||||
Regions | |||||||||||
| Domain | 20 – 133 | 114 | Thioredoxin 1 | ||||||||
| Domain | 151 – 287 | 137 | Thioredoxin 2 | ||||||||
| Motif | 436 – 439 | 4 | Prevents secretion from ER By similarity | ||||||||
| Compositional bias | 421 – 435 | 15 | Asp/Glu-rich (acidic) | ||||||||
Sites | |||||||||||
| Active site | 55 | 1 | Nucleophile By similarity | ||||||||
| Active site | 58 | 1 | Nucleophile By similarity | ||||||||
| Active site | 190 | 1 | Nucleophile By similarity | ||||||||
| Active site | 193 | 1 | Nucleophile By similarity | ||||||||
| Site | 56 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 57 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 118 | 1 | Lowers pKa of C-terminal Cys of first active site By similarity | ||||||||
| Site | 191 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 192 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 256 | 1 | Lowers pKa of C-terminal Cys of second active site By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 427 | 1 | Phosphoserine By similarity | ||||||||
| Disulfide bond | 55 ↔ 58 | Redox-active By similarity | |||||||||
| Disulfide bond | 190 ↔ 193 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells." Chaudhuri M.M., Tonin P.N., Lewis W.H., Srinivasan P.R. Biochem. J. 281:645-650(1992) [PubMed: 1311171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-43. |
Cross-references
Sequence databases | |
|---|---|
| X62678 mRNA. Translation: CAA44550.1. | |
| PIR | S19656. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MEK based on UniProtKB P07237. |
| SMR | P38660. Positions 20-132, 154-280. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P38660. |
Enzyme and pathway databases | |
| BRENDA | 5.3.4.1. 824. |
Family and domain databases | |
| InterPro | IPR005788. Disulphide_isomerase. IPR000886. ER_target_seq_motif. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits. |
| Pfam | PF00085. Thioredoxin. 2 hits. [Graphical view] |
| PRINTS | PR00421. THIOREDOXIN. |
| TIGRFAMs | TIGR01126. pdi_dom. 2 hits. |
| PROSITE | PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PDIA6_MESAU | ||||||||
| Accession | Primary (citable) accession number: P38660 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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