Q921X9 (PDIA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein disulfide-isomerase A5 EC=5.3.4.1 Alternative name(s): Protein disulfide isomerase-related protein | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 517 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | Catalyzes the rearrangement of -S-S- bonds in proteins. |
| Subcellular location | Endoplasmic reticulum lumen By similarity. |
| Sequence similarities | Belongs to the protein disulfide isomerase family. Contains 3 thioredoxin domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Redox-active center Repeat Signal |
| Molecular function | Isomerase |
| PTM | Disulfide bond |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic processInferred from electronic annotation. Source: InterPro protein foldingInferred from electronic annotation. Source: GOC response to stressInferred from direct assay PubMed 7556671. Source: UniProtKB |
| Cellular_component | endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activityInferred from electronic annotation. Source: EC protein disulfide oxidoreductase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||||
| Chain | 22 – 517 | 496 | Protein disulfide-isomerase A5 | PRO_0000034234 | |||||||
Regions | |||||||||||
| Domain | 132 – 259 | 128 | Thioredoxin 1 | ||||||||
| Domain | 268 – 382 | 115 | Thioredoxin 2 | ||||||||
| Domain | 376 – 504 | 129 | Thioredoxin 3 | ||||||||
| Motif | 514 – 517 | 4 | Prevents secretion from ER Potential | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 180 ↔ 183 | Redox-active By similarity | |||||||||
| Disulfide bond | 303 ↔ 306 | Redox-active By similarity | |||||||||
| Disulfide bond | 424 ↔ 427 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC009151 mRNA. Translation: AAH09151.1. |
| IPI | IPI00122362. |
| RefSeq | NP_082571.1. NM_028295.1. |
| UniGene | Mm.71015. |
3D structure databases | |
| ProteinModelPortal | Q921X9. |
| SMR | Q921X9. Positions 69-500. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10090.ENSMUSP00000023550. |
PTM databases | |
| PhosphoSite | Q921X9. |
Proteomic databases | |
| PaxDb | Q921X9. |
| PRIDE | Q921X9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000023550; ENSMUSP00000023550; ENSMUSG00000022844. |
| GeneID | 72599. |
| KEGG | mmu:72599. |
| UCSC | uc007zbl.1. mouse. |
Organism-specific databases | |
| CTD | 10954. |
| MGI | MGI:1919849. Pdia5. |
Phylogenomic databases | |
| eggNOG | COG0526. |
| GeneTree | ENSGT00700000104354. |
| HOGENOM | HOG000039967. |
| HOVERGEN | HBG053547. |
| InParanoid | Q921X9. |
| KO | K09583. |
| OMA | LAGMNVY. |
| OrthoDB | EOG49KFQF. |
Gene expression databases | |
| ArrayExpress | Q921X9. |
| Bgee | Q921X9. |
| CleanEx | MM_PDIA5. |
| Genevestigator | Q921X9. |
| GermOnline | ENSMUSG00000022844. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.40.30.10. 4 hits. |
| InterPro | IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view] |
| Pfam | PF00085. Thioredoxin. 3 hits. [Graphical view] |
| PRINTS | PR00421. THIOREDOXIN. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 4 hits. |
| PROSITE | PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | PDIA5. mouse. |
| NextBio | 336573. |
| SOURCE | Search... |
Entry information
| Entry name | PDIA5_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q921X9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
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
