P29828 (PDI_MEDSA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 91.
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 |
| ||
| Organism | Medicago sativa (Alfalfa) | ||
| Taxonomic identifier | 3879 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago![]() |
Protein attributes
| Sequence length | 512 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)
| 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 – 24 | 24 | By similarity | ||||||||
| Chain | 25 – 512 | 488 | Protein disulfide-isomerase | PRO_0000034209 | |||||||
Regions | |||||||||||
| Domain | 25 – 144 | 120 | Thioredoxin 1 | ||||||||
| Domain | 357 – 485 | 129 | Thioredoxin 2 | ||||||||
| Motif | 509 – 512 | 4 | Prevents secretion from ER | ||||||||
Sites | |||||||||||
| Active site | 62 | 1 | Nucleophile By similarity | ||||||||
| Active site | 65 | 1 | Nucleophile By similarity | ||||||||
| Active site | 407 | 1 | Nucleophile By similarity | ||||||||
| Active site | 410 | 1 | Nucleophile By similarity | ||||||||
| Site | 63 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 64 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 130 | 1 | Lowers pKa of C-terminal Cys of first active site By similarity | ||||||||
| Site | 408 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 409 | 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 | |||||||||||
| Glycosylation | 278 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 62 ↔ 65 | Redox-active By similarity | |||||||||
| Disulfide bond | 407 ↔ 410 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 16 | 1 | L → V in AAA32662. Ref.2 | ||||||||
| Sequence conflict | 395 | 1 | G → A in AAA32662. Ref.2 | ||||||||
| Sequence conflict | 491 | 1 | H → Q in AAA32662. Ref.2 | ||||||||
Sequences
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References
| [1] | "Sequence analysis and developmental expression of an alfalfa protein disulfide isomerase." Shorrosh B.S., Dixon R.A. Plant Mol. Biol. 19:319-321(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Apollo. |
| [2] | "Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C." Shorrosh B.S., Dixon R.A. Proc. Natl. Acad. Sci. U.S.A. 88:10941-10945(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z11499 mRNA. Translation: CAA77575.1. M82973 mRNA. Translation: AAA32662.1. |
| PIR | A41440. ISAASS. S22479. |
3D structure databases | |
| ProteinModelPortal | P29828. |
| ModBase | Search... |
Proteomic databases | |
| ProMEX | P29828. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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_MEDSA | ||||||||
| Accession | Primary (citable) accession number: P29828 | ||||||||
| 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
