Reviewed,
UniProtKB/Swiss-Prot P27773 (PDIA3_MOUSE)
Last modified
June 16, 2009.
Version 95.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein disulfide-isomerase A3 EC=5.3.4.1 Alternative name(s): Disulfide isomerase ER-60 ERp60 58 kDa microsomal protein p58 ERp57 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 505 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. |
| Subunit structure | Interacts with ERP27 and CANX By similarity. |
| Subcellular location | Endoplasmic reticulum lumen By similarity. Melanosome By similarity. |
| Post-translational modification | Phosphorylated. Ref.7 |
| Sequence similarities | Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains. |
| Caution | Was originally (Ref.1) thought to be a phosphatidylinositol-4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha). |
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 positive regulation of apoptosisInferred from mutant phenotype. Source: MGI |
| Cellular component | endoplasmic reticulum Inferred from direct assay. Source: MGI endoplasmic reticulum lumenInferred 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 – 24 | 24 | Ref.7 Ref.6 | ||||||||
| Chain | 25 – 505 | 481 | Protein disulfide-isomerase A3 | PRO_0000034226 | |||||||
Regions | |||||||||||
| Domain | 25 – 133 | 109 | Thioredoxin 1 | ||||||||
| Domain | 343 – 485 | 143 | Thioredoxin 2 | ||||||||
| Motif | 502 – 505 | 4 | Prevents secretion from ER By similarity | ||||||||
Sites | |||||||||||
| Active site | 57 | 1 | Nucleophile By similarity | ||||||||
| Active site | 60 | 1 | Nucleophile By similarity | ||||||||
| Active site | 406 | 1 | Nucleophile By similarity | ||||||||
| Active site | 409 | 1 | Nucleophile By similarity | ||||||||
| Site | 58 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 59 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 119 | 1 | Lowers pKa of C-terminal Cys of first active site By similarity | ||||||||
| Site | 407 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 408 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 471 | 1 | Lowers pKa of C-terminal Cys of second active site By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 57 ↔ 60 | Redox-active By similarity | |||||||||
| Disulfide bond | 406 ↔ 409 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 20 | 1 | R → C in BAC40527. Ref.3 | ||||||||
| Sequence conflict | 20 | 1 | R → C in BAE41259. Ref.3 | ||||||||
| Sequence conflict | 76 | 1 | Missing in AAA39944. Ref.1 | ||||||||
| Sequence conflict | 108 | 1 | D → A in AAA39944. Ref.1 | ||||||||
| Sequence conflict | 230 | 1 | G → A in AAA39944. Ref.1 | ||||||||
| Sequence conflict | 264 | 1 | Y → F in BAE39834. Ref.3 | ||||||||
| Sequence conflict | 315 | 1 | G → S in AAA39944. Ref.1 | ||||||||
| Sequence conflict | 387 | 1 | D → G in BAE39834. Ref.3 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Expression of phospholipase C isozymes by murine B lymphocytes." Hempel W.M., Defranco A.L. J. Immunol. 146:3713-3720(1991) [PubMed: 2033248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Mouse GRP58 gene structure." Wang W., Jaiswal A.K. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J, DBA/2 and NOD. Tissue: Thymus. |
| [4] | The mouse genome sequencing consortium Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II and FVB/N. Tissue: Mammary tumor. |
| [6] | "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis." Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K. Electrophoresis 15:735-745(1994) [PubMed: 7523108] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-41 AND 306-329. Tissue: Fibroblast. |
| [7] | "Identification of the two isoforms of phospholipase C-alpha from dividing murine fibroblasts by protein microsequencing." Merrick B.A., Wichter L.L., Patterson R.M., He C., Selkirk J.K. Biochem. Arch. 9:335-340(1993) Cited for: PROTEIN SEQUENCE OF 25-41, PHOSPHORYLATION. Tissue: Fibroblast. |
| [8] | Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 63-73; 94-103; 119-128; 130-139; 147-172; 183-193; 195-214; 234-251; 258-270; 306-329; 335-343; 347-362; 366-378; 448-459 AND 472-495, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M73329 mRNA. Translation: AAA39944.1. DQ000491 Genomic DNA. Translation: AAY16987.1. AK088721 mRNA. Translation: BAC40527.1. AK133799 mRNA. Translation: BAE21849.1. AK167807 mRNA. Translation: BAE39834.1. AK169611 mRNA. Translation: BAE41259.1. AL845466 Genomic DNA. Translation: CAM24231.1. BC003285 mRNA. Translation: AAH03285.1. BC033439 mRNA. Translation: AAH33439.1. | |
| IPI | IPI00230108. |
| RefSeq | NP_031978.2. |
| UniGene | Mm.263177 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MEK based on UniProtKB P07237. |
| SMR | P27773. Positions 25-137, 134-365, 357-488. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P27773. |
2-D gel databases | |
| SWISS-2DPAGE | P27773. |
| REPRODUCTION-2DPAGE | P27773. Q3TEI9. Q8C2F4. |
Proteomic databases | |
| PRIDE | P27773. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000027248. Mus musculus. [Contig view] |
| GeneID | 14827. |
| KEGG | mmu:14827. |
Organism-specific databases | |
| MGI | MGI:95834. Pdia3. |
Phylogenomic databases | |
| HOGENOM | P27773. |
| HOVERGEN | P27773. |
| OMA | P27773. EGITLFR. |
Enzyme and pathway databases | |
| BRENDA | 5.3.4.1. 244. |
Gene expression databases | |
| ArrayExpress | P27773. |
| Bgee | P27773. |
| CleanEx | MM_PDIA3. |
| GermOnline | ENSMUSG00000027248. Mus musculus. |
Family and domain databases | |
| InterPro | IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. 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. 1 hit. |
| Pfam | PF00085. Thioredoxin. 2 hits. [Graphical view] |
| PRINTS | PR00421. THIOREDOXIN. |
| TIGRFAMs | TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. pdi_dom. 2 hits. |
| PROSITE | PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 287035. |
| SOURCE | Search... |
Entry information
| Entry name | PDIA3_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P27773 Secondary accession number(s): Q3TEI9 Q99LF6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


