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P32474 (EUG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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 EUG1

Short name=PDI
EC=5.3.4.1
Alternative name(s):
Endoplasmic reticulum protein EUG1
Gene names
Name:EUG1
Ordered Locus Names:YDR518W
ORF Names:D9719.23
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably interacts with nascent polypeptides in the endoplasmic reticulum. It is an essential gene only in the absence of PDI. Its native disulfide isomerase activity is very low. Ref.6

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subunit structure

Interacts with EPS1. Ref.6

Subcellular location

Endoplasmic reticulum lumen.

Post-translational modification

May have O-linked mannose residues.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 517488Protein disulfide-isomerase EUG1
PRO_0000034219

Regions

Domain30 – 141112Thioredoxin 1
Domain355 – 487133Thioredoxin 2
Motif514 – 5174Prevents secretion from ER

Amino acid modifications

Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation4621N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis651S → C: Increases PDI activity. Ref.5
Mutagenesis4081S → C: Increases PDI activity. Ref.5
Sequence conflict3641V → G in AAT92989. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P32474 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 5F78AD770A6A4083

FASTA51758,982
        10         20         30         40         50         60 
MQVTTRFISA IVSFCLFASF TLAENSARAT PGSDLLVLTE KKFKSFIESH PLVLVEFFAP 

        70         80         90        100        110        120 
WCLHSQILRP HLEEAASILK EHNVPVVQID CEANSMVCLQ QTINTYPTLK IFKNGRIFDG 

       130        140        150        160        170        180 
QVYRGVKITD EITQYMIQLY EASVIYLNSE DEIQPYLENA TLPVVINRGL TGLNETYQEV 

       190        200        210        220        230        240 
ALDLAEDYVF LSLLDSEDKS LSIHLPNTTE PILFDGNVDS LVGNSVALTQ WLKVVILPYF 

       250        260        270        280        290        300 
TDIEPDLFPK YISSNLPLAY FFYTSEEELE DYTDLFTQLG KENRGQINFI ALNSTMFPHH 

       310        320        330        340        350        360 
VRFLNMREQF PLFAIHNMIN NLKYGLPQLP EEEYAKLEKP QPLDRDMIVQ LVKDYREGTA 

       370        380        390        400        410        420 
KPIVKSEEIP KEQKSNVYKI VGKTHDDIVH DDDKDVLVKY YATWCIHSKR FAPIYEEIAN 

       430        440        450        460        470        480 
VLASDESVRD KILIAEVDSG ANDILSFPVT GYPTIALYPA GNNSKPIIFN KIRNLEDVFE 

       490        500        510 
FIKESGTHHI DGQAIYDKLH QAKDSEVSTE DTVHDEL 

« Hide

References

« Hide 'large scale' references
[1]"The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase."
Tachibana C., Stevens T.H.
Mol. Cell. Biol. 12:4601-4611(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity."
Noergaard P., Winther J.R.
Biochem. J. 358:269-274(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF PDI ACTIVITY, MUTAGENESIS OF SER-65 AND SER-408.
[6]"Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities."
Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T., Kikuchi M.
J. Biol. Chem. 280:31438-31441(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EPS1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84796 Unassigned DNA. Translation: AAA18226.1.
U33057 Genomic DNA. Translation: AAB64959.1.
AY692970 Genomic DNA. Translation: AAT92989.1.
BK006938 Genomic DNA. Translation: DAA12349.1.
PIRA44483.
RefSeqNP_010806.1. NM_001180826.1.

3D structure databases

ProteinModelPortalP32474.
SMRP32474. Positions 24-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32569. 117 interactions.
IntActP32474. 1 interaction.
MINTMINT-4811793.
STRING4932.YDR518W.

Proteomic databases

PaxDbP32474.
PeptideAtlasP32474.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR518W; YDR518W; YDR518W.
GeneID852130.
KEGGsce:YDR518W.

Organism-specific databases

CYGDYDR518w.
SGDS000002926. EUG1.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115037.
HOGENOMHOG000162459.
KOK09580.
OMADSGANDI.
OrthoDBEOG71CFZN.

Enzyme and pathway databases

BioCycYEAST:YDR518W-MONOMER.

Gene expression databases

GenevestigatorP32474.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio970528.
PROP32474.

Entry information

Entry nameEUG1_YEAST
AccessionPrimary (citable) accession number: P32474
Secondary accession number(s): D6VTD9, E9P901
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 124 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 IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families