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Q99316 (MPD2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide isomerase MPD2

EC=5.3.4.1
Gene names
Name:MPD2
Ordered Locus Names:YOL088C
ORF Names:O0941
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Endoplasmic reticulum Ref.6.

Miscellaneous

Present with 1520 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 277255Protein disulfide isomerase MPD2
PRO_0000034182

Regions

Domain27 – 172146Thioredoxin
Motif274 – 2774Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond56 ↔ 59Redox-active By similarity

Experimental info

Mutagenesis561C → S: Loss of function; when associated with S-59. Ref.1
Mutagenesis591C → S: Loss of function; when associated with S-56. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99316 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: ECCEA7C6CBB10488

FASTA27732,401
        10         20         30         40         50         60 
MKLHGFLFSV LSTCVVILPA LAYSEAVTMV KSIEQYFDIC NRNDSYTMIK YYTSWCQHCK 

        70         80         90        100        110        120 
TLAPVYEELG ELYAKKANKD DTPINFLEVN CEFFGPTLCT DLPGFPIIEL VKPRTKPLVL 

       130        140        150        160        170        180 
PKLDWSSMKF HERLWQRIKT WFNNPKYQLD TSRVVRFEGS RNLKSLSNFI DTVRSKDTEE 

       190        200        210        220        230        240 
RFIEHIFDDS RNCNEELRSQ QLLCKAGKEY YSDTLSKLYG DVNGLEKERR RLEALIKQNG 

       250        260        270 
DDLSKEVKEK LKIIRLQLSL LSHIEDQLED TSSHDEL 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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] [Europe PMC] [Abstract]
Cited for: OXIDATION BY ERO1.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [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.
BK006948 Genomic DNA. Translation: DAA10696.1.
PIRS57381.
RefSeqNP_014553.1. NM_001183342.1.

3D structure databases

ProteinModelPortalQ99316.
SMRQ99316. Positions 24-110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34314. 41 interactions.
DIPDIP-1451N.
IntActQ99316. 5 interactions.
MINTMINT-392339.
STRING4932.YOL088C.

Proteomic databases

MaxQBQ99316.
PaxDbQ99316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL088C; YOL088C; YOL088C.
GeneID854065.
KEGGsce:YOL088C.

Organism-specific databases

CYGDYOL088c.
SGDS000005448. MPD2.

Phylogenomic databases

eggNOGNOG314639.
HOGENOMHOG000113635.
OMAYTVVKYY.
OrthoDBEOG71CFZN.

Enzyme and pathway databases

BioCycYEAST:YOL088C-MONOMER.

Gene expression databases

GenevestigatorQ99316.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975674.

Entry information

Entry nameMPD2_YEAST
AccessionPrimary (citable) accession number: Q99316
Secondary accession number(s): D6W1Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families