P52589 (PDI_WHEAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 84.
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 Short name=PDI EC=5.3.4.1 | ||
| Gene names |
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| Organism | Triticum aestivum (Wheat) | ||
| Taxonomic identifier | 4565 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum![]() |
Protein attributes
| Sequence length | 515 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)
| Function | Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer By similarity. |
| Catalytic activity | Catalyzes the rearrangement of -S-S- bonds in proteins. |
| Subcellular location | Endoplasmic reticulum lumen Potential. |
| 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 Glycoprotein |
| 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 |
| 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 – 25 | 25 | By similarity | ||||||||
| Chain | 26 – 515 | 490 | Protein disulfide-isomerase | PRO_0000034212 | |||||||
Regions | |||||||||||
| Domain | 26 – 150 | 125 | Thioredoxin 1 | ||||||||
| Domain | 346 – 489 | 144 | Thioredoxin 2 | ||||||||
| Motif | 512 – 515 | 4 | Prevents secretion from ER Potential | ||||||||
Sites | |||||||||||
| Active site | 68 | 1 | Nucleophile By similarity | ||||||||
| Active site | 71 | 1 | Nucleophile By similarity | ||||||||
| Active site | 412 | 1 | Nucleophile By similarity | ||||||||
| Active site | 415 | 1 | Nucleophile By similarity | ||||||||
| Site | 69 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 70 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 136 | 1 | Lowers pKa of C-terminal Cys of first active site By similarity | ||||||||
| Site | 413 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 414 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 475 | 1 | Lowers pKa of C-terminal Cys of second active site By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 283 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 68 ↔ 71 | Redox-active By similarity | |||||||||
| Disulfide bond | 412 ↔ 415 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Nucleotide sequence of a wheat cDNA encoding protein disulfide isomerase." Shimoni Y., Segal G., Zhu X.Z., Galili G. Plant Physiol. 107:281-281(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Chinese Spring. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U11496 mRNA. Translation: AAA19660.1. |
| PIR | T06262. |
| UniGene | Ta.2019. |
3D structure databases | |
| ProteinModelPortal | P52589. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| Gramene | P52589. |
Family and domain databases | |
| Gene3D | 3.40.30.10. 3 hits. |
| InterPro | IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view] |
| Pfam | PF00085. Thioredoxin. 2 hits. [Graphical view] |
| PRINTS | PR00421. THIOREDOXIN. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 4 hits. |
| TIGRFAMs | TIGR01130. ER_PDI_fam. 1 hit. 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 | PDI_WHEAT | ||||||||
| Accession | Primary (citable) accession number: P52589 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
