Reviewed,
UniProtKB/Swiss-Prot Q99316 (MPD2_YEAST)
Last modified
January 19, 2010.
Version 72.
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 MPD2 EC=5.3.4.1 | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 277 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 | Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1. Ref.1 |
| Catalytic activity | Catalyzes the rearrangement of -S-S- bonds in proteins. |
| Subcellular location | |
| Miscellaneous | Present with 1520 molecules/cell in log phase SD medium. Ref.6 |
| Sequence similarities | Belongs to the protein disulfide isomerase family. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Redox-active center Signal |
| Molecular function | Isomerase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro protein foldingInferred from genetic interaction. Source: SGD |
| Cellular component | endoplasmic reticulum Inferred from genetic interaction. Source: SGD |
| Molecular function | protein disulfide isomerase activity Inferred from direct assay. Source: SGD protein disulfide oxidoreductase activityInferred from direct assay. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||||
| Chain | 23 – 277 | 255 | Protein disulfide isomerase MPD2 | PRO_0000034182 | |||||||
Regions | |||||||||||
| Domain | 27 – 172 | 146 | Thioredoxin | ||||||||
| Motif | 274 – 277 | 4 | Prevents secretion from ER Potential | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 56 ↔ 59 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Mutagenesis | 56 | 1 | C → S: Loss of function; when associated with S-59. Ref.1 | ||||||||
| Mutagenesis | 59 | 1 | C → S: Loss of function; when associated with S-56. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner." Tachikawa H., Funahashi W., Takeuchi Y., Nakanishi H., Nishihara R., Katoh S., Gao X.D., Mizunaga T., Fujimoto D. Biochem. Biophys. Res. Commun. 239:710-714(1997) [PubMed: 9367834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF CYS-56 AND CYS-59. |
| [2] | "A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames." Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M. Yeast 11:975-986(1995) [PubMed: 8533473] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [3] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K.Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [4] | "Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum." Frand A.R., Kaiser C.A. Mol. Cell 4:469-477(1999) [PubMed: 10549279] [Abstract] Cited for: OXIDATION BY ERO1. |
| [5] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [6] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D34634 Genomic DNA. Translation: BAA22222.1. X83121 Genomic DNA. Translation: CAA58191.1. Z74830 Genomic DNA. Translation: CAA99100.1. |
| PIR | S57381. |
| RefSeq | NP_014553.1. |
3D structure databases | |
| SMR | Q99316. Positions 37-113, 43-172. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-1451N. |
| IntAct | Q99316. 3 interactions. |
| STRING | Q99316. |
Genome annotation databases | |
| Ensembl | YOL088C; YOL088C; YOL088C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 854065. |
| KEGG | sce:YOL088C. |
| NMPDR | fig|4932.3.peg.5642. |
Organism-specific databases | |
| CYGD | YOL088c. |
| SGD | S000005448. MPD2. |
Phylogenomic databases | |
| eggNOG | fuNOG10906. |
| OMA | SHCKKLK. |
| OrthoDB | EOG90CK15. |
| PhylomeDB | Q99316. |
Enzyme and pathway databases | |
| BRENDA | 5.3.4.1. 250. |
Gene expression databases | |
| ArrayExpress | Q99316. |
| Genevestigator | Q99316. |
| GermOnline | YOL088C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF00085. Thioredoxin. 1 hit. [Graphical view] |
| PROSITE | PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. False negative. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 975674. |
Entry information
| Entry name | MPD2_YEAST | ||||||||
| Accession | Primary (citable) accession number: Q99316 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


