Q29RV1 (PDIA4_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 55.
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 A4 EC=5.3.4.1 | ||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 643 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. |
| Subunit structure | Part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. |
| Subcellular location | Endoplasmic reticulum lumen By similarity. Melanosome 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 | Acetylation 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 |
| Cellular component | endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell melanosomeInferred 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 – 20 | 20 | Potential | ||||||||
| Chain | 21 – 643 | 623 | Protein disulfide-isomerase A4 | PRO_0000240338 | |||||||
Regions | |||||||||||
| Domain | 21 – 168 | 148 | Thioredoxin 1 | ||||||||
| Domain | 170 – 300 | 131 | Thioredoxin 2 | ||||||||
| Domain | 503 – 634 | 132 | Thioredoxin 3 | ||||||||
| Motif | 640 – 643 | 4 | Prevents secretion from ER By similarity | ||||||||
| Compositional bias | 39 – 54 | 16 | Asp/Glu-rich (acidic) | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 365 | 1 | N6-acetyllysine By similarity | ||||||||
| Disulfide bond | 90 ↔ 93 | Redox-active By similarity | |||||||||
| Disulfide bond | 205 ↔ 208 | Redox-active By similarity | |||||||||
| Disulfide bond | 553 ↔ 556 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 16 | 1 | V → A in ABG81434. Ref.2 | ||||||||
| Sequence conflict | 32 | 1 | T → S in ABG81434. Ref.2 | ||||||||
| Sequence conflict | 32 | 1 | T → S in ABQ12930. Ref.2 | ||||||||
| Sequence conflict | 415 | 1 | V → I in ABG81434. Ref.2 | ||||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis. |
| [2] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC114004 mRNA. Translation: AAI14005.1. BT026278 mRNA. Translation: ABG81434.1. BT030490 mRNA. Translation: ABQ12930.1. |
| IPI | IPI00706136. |
| RefSeq | NP_001039344.1. NM_001045879.1. |
| UniGene | Bt.23128. |
3D structure databases | |
| ProteinModelPortal | Q29RV1. |
| SMR | Q29RV1. Positions 55-283, 521-643. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q29RV1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 415110. |
| KEGG | bta:415110. |
Organism-specific databases | |
| CTD | 9601. |
Phylogenomic databases | |
| HOVERGEN | HBG005920. |
| InParanoid | Q29RV1. |
| OrthoDB | EOG405S0R. |
| PhylomeDB | Q29RV1. |
Family and domain databases | |
| InterPro | IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR017068. Protein_diS-isomerase_A4. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 4 hits. |
| KO | K09582. |
| Pfam | PF00085. Thioredoxin. 3 hits. [Graphical view] |
| PIRSF | PIRSF036862. Disulphide_isom_A4. 1 hit. |
| PRINTS | PR00421. THIOREDOXIN. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 5 hits. |
| TIGRFAMs | TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. Pdi_dom. 3 hits. |
| PROSITE | PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 3 hits. PS51352. THIOREDOXIN_2. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PDIA4_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q29RV1 Secondary accession number(s): A5D971, Q0V8E1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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