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P32474

- EUG1_YEAST

UniProt

P32474 - EUG1_YEAST

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Protein

Protein disulfide-isomerase EUG1

Gene

EUG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: SGD
  2. protein disulfide oxidoreductase activity Source: SGD
  3. protein-disulfide reductase (glutathione) activity Source: SGD
  4. unfolded protein binding Source: SGD

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. oxidation-reduction process Source: GOC
  3. protein folding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciYEAST:YDR518W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase EUG1 (EC:5.3.4.1)
Short name:
PDI
Alternative name(s):
Endoplasmic reticulum protein EUG1
Gene namesi
Name:EUG1
Ordered Locus Names:YDR518W
ORF Names:D9719.23
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR518w.
SGDiS000002926. EUG1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651S → C: Increases PDI activity. 1 Publication
Mutagenesisi408 – 4081S → C: Increases PDI activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 517488Protein disulfide-isomerase EUG1PRO_0000034219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

May have O-linked mannose residues.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP32474.
PaxDbiP32474.
PeptideAtlasiP32474.

Expressioni

Gene expression databases

GenevestigatoriP32474.

Interactioni

Subunit structurei

Interacts with EPS1.1 Publication

Protein-protein interaction databases

BioGridi32569. 117 interactions.
IntActiP32474. 1 interaction.
MINTiMINT-4811793.
STRINGi4932.YDR518W.

Structurei

3D structure databases

ProteinModelPortaliP32474.
SMRiP32474. Positions 24-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 141112Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 487133Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi514 – 5174Prevents secretion from ER

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000162459.
InParanoidiP32474.
KOiK09580.
OrthoDBiEOG71CFZN.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32474-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQVTTRFISA IVSFCLFASF TLAENSARAT PGSDLLVLTE KKFKSFIESH
60 70 80 90 100
PLVLVEFFAP WCLHSQILRP HLEEAASILK EHNVPVVQID CEANSMVCLQ
110 120 130 140 150
QTINTYPTLK IFKNGRIFDG QVYRGVKITD EITQYMIQLY EASVIYLNSE
160 170 180 190 200
DEIQPYLENA TLPVVINRGL TGLNETYQEV ALDLAEDYVF LSLLDSEDKS
210 220 230 240 250
LSIHLPNTTE PILFDGNVDS LVGNSVALTQ WLKVVILPYF TDIEPDLFPK
260 270 280 290 300
YISSNLPLAY FFYTSEEELE DYTDLFTQLG KENRGQINFI ALNSTMFPHH
310 320 330 340 350
VRFLNMREQF PLFAIHNMIN NLKYGLPQLP EEEYAKLEKP QPLDRDMIVQ
360 370 380 390 400
LVKDYREGTA KPIVKSEEIP KEQKSNVYKI VGKTHDDIVH DDDKDVLVKY
410 420 430 440 450
YATWCIHSKR FAPIYEEIAN VLASDESVRD KILIAEVDSG ANDILSFPVT
460 470 480 490 500
GYPTIALYPA GNNSKPIIFN KIRNLEDVFE FIKESGTHHI DGQAIYDKLH
510
QAKDSEVSTE DTVHDEL
Length:517
Mass (Da):58,982
Last modified:October 1, 1993 - v1
Checksum:i5F78AD770A6A4083
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti364 – 3641V → G in AAT92989. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84796 Unassigned DNA. Translation: AAA18226.1.
U33057 Genomic DNA. Translation: AAB64959.1.
AY692970 Genomic DNA. Translation: AAT92989.1.
BK006938 Genomic DNA. Translation: DAA12349.1.
PIRiA44483.
RefSeqiNP_010806.1. NM_001180826.1.

Genome annotation databases

EnsemblFungiiYDR518W; YDR518W; YDR518W.
GeneIDi852130.
KEGGisce:YDR518W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84796 Unassigned DNA. Translation: AAA18226.1 .
U33057 Genomic DNA. Translation: AAB64959.1 .
AY692970 Genomic DNA. Translation: AAT92989.1 .
BK006938 Genomic DNA. Translation: DAA12349.1 .
PIRi A44483.
RefSeqi NP_010806.1. NM_001180826.1.

3D structure databases

ProteinModelPortali P32474.
SMRi P32474. Positions 24-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32569. 117 interactions.
IntActi P32474. 1 interaction.
MINTi MINT-4811793.
STRINGi 4932.YDR518W.

Proteomic databases

MaxQBi P32474.
PaxDbi P32474.
PeptideAtlasi P32474.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR518W ; YDR518W ; YDR518W .
GeneIDi 852130.
KEGGi sce:YDR518W.

Organism-specific databases

CYGDi YDR518w.
SGDi S000002926. EUG1.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00760000119201.
HOGENOMi HOG000162459.
InParanoidi P32474.
KOi K09580.
OrthoDBi EOG71CFZN.

Enzyme and pathway databases

BioCyci YEAST:YDR518W-MONOMER.

Miscellaneous databases

NextBioi 970528.
PROi P32474.

Gene expression databases

Genevestigatori P32474.

Family and domain databases

Gene3Di 3.40.30.10. 2 hits.
InterProi IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 4 hits.
TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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.

Entry informationi

Entry nameiEUG1_YEAST
AccessioniPrimary (citable) accession number: P32474
Secondary accession number(s): D6VTD9, E9P901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3