ID   EUG1_YEAST              Reviewed;         517 AA.
AC   P32474; D6VTD9; E9P901;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Protein disulfide-isomerase EUG1;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   AltName: Full=Endoplasmic reticulum protein EUG1;
DE   Flags: Precursor;
GN   Name=EUG1; OrderedLocusNames=YDR518W; ORFNames=D9719.23;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=1406650; DOI=10.1128/mcb.12.10.4601-4611.1992;
RA   Tachibana C., Stevens T.H.;
RT   "The yeast EUG1 gene encodes an endoplasmic reticulum protein that is
RT   functionally related to protein disulfide isomerase.";
RL   Mol. Cell. Biol. 12:4601-4611(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   CHARACTERIZATION OF PDI ACTIVITY, AND MUTAGENESIS OF SER-65 AND SER-408.
RX   PubMed=11485577; DOI=10.1042/0264-6021:3580269;
RA   Noergaard P., Winther J.R.;
RT   "Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic
RT   increase in protein disulphide isomerase activity.";
RL   Biochem. J. 358:269-274(2001).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH EPS1.
RX   PubMed=16002399; DOI=10.1074/jbc.m503377200;
RA   Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T.,
RA   Kikuchi M.;
RT   "Interactions among yeast protein-disulfide isomerase proteins and
RT   endoplasmic reticulum chaperone proteins influence their activities.";
RL   J. Biol. Chem. 280:31438-31441(2005).
CC   -!- FUNCTION: Probably interacts with nascent polypeptides in the
CC       endoplasmic reticulum. It is an essential gene only in the absence of
CC       PDI. Its native disulfide isomerase activity is very low.
CC       {ECO:0000269|PubMed:16002399}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBUNIT: Interacts with EPS1. {ECO:0000269|PubMed:16002399}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- PTM: May have O-linked mannose residues.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; M84796; AAA18226.1; -; Unassigned_DNA.
DR   EMBL; U33057; AAB64959.1; -; Genomic_DNA.
DR   EMBL; AY692970; AAT92989.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12349.1; -; Genomic_DNA.
DR   PIR; A44483; A44483.
DR   RefSeq; NP_010806.1; NM_001180826.1.
DR   AlphaFoldDB; P32474; -.
DR   SMR; P32474; -.
DR   BioGRID; 32569; 208.
DR   IntAct; P32474; 1.
DR   STRING; 4932.YDR518W; -.
DR   GlyCosmos; P32474; 5 sites, No reported glycans.
DR   GlyGen; P32474; 5 sites.
DR   iPTMnet; P32474; -.
DR   MaxQB; P32474; -.
DR   PaxDb; 4932-YDR518W; -.
DR   PeptideAtlas; P32474; -.
DR   EnsemblFungi; YDR518W_mRNA; YDR518W; YDR518W.
DR   GeneID; 852130; -.
DR   KEGG; sce:YDR518W; -.
DR   AGR; SGD:S000002926; -.
DR   SGD; S000002926; EUG1.
DR   VEuPathDB; FungiDB:YDR518W; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   GeneTree; ENSGT00940000168753; -.
DR   HOGENOM; CLU_025879_5_0_1; -.
DR   InParanoid; P32474; -.
DR   OMA; FCHSVFS; -.
DR   OrthoDB; 2021174at2759; -.
DR   BioCyc; YEAST:YDR518W-MONOMER; -.
DR   Reactome; R-SCE-264876; Insulin processing.
DR   BioGRID-ORCS; 852130; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P32474; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P32474; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:SGD.
DR   GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IDA:SGD.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IDA:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR   GO; GO:0006457; P:protein folding; IGI:SGD.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Isomerase; Redox-active center;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..517
FT                   /note="Protein disulfide-isomerase EUG1"
FT                   /id="PRO_0000034219"
FT   DOMAIN          30..141
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          355..487
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           514..517
FT                   /note="Prevents secretion from ER"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         65
FT                   /note="S->C: Increases PDI activity."
FT                   /evidence="ECO:0000269|PubMed:11485577"
FT   MUTAGEN         408
FT                   /note="S->C: Increases PDI activity."
FT                   /evidence="ECO:0000269|PubMed:11485577"
FT   CONFLICT        364
FT                   /note="V -> G (in Ref. 4; AAT92989)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   517 AA;  58982 MW;  5F78AD770A6A4083 CRC64;
     MQVTTRFISA IVSFCLFASF TLAENSARAT PGSDLLVLTE KKFKSFIESH PLVLVEFFAP
     WCLHSQILRP HLEEAASILK EHNVPVVQID CEANSMVCLQ QTINTYPTLK IFKNGRIFDG
     QVYRGVKITD EITQYMIQLY EASVIYLNSE DEIQPYLENA TLPVVINRGL TGLNETYQEV
     ALDLAEDYVF LSLLDSEDKS LSIHLPNTTE PILFDGNVDS LVGNSVALTQ WLKVVILPYF
     TDIEPDLFPK YISSNLPLAY FFYTSEEELE DYTDLFTQLG KENRGQINFI ALNSTMFPHH
     VRFLNMREQF PLFAIHNMIN NLKYGLPQLP EEEYAKLEKP QPLDRDMIVQ LVKDYREGTA
     KPIVKSEEIP KEQKSNVYKI VGKTHDDIVH DDDKDVLVKY YATWCIHSKR FAPIYEEIAN
     VLASDESVRD KILIAEVDSG ANDILSFPVT GYPTIALYPA GNNSKPIIFN KIRNLEDVFE
     FIKESGTHHI DGQAIYDKLH QAKDSEVSTE DTVHDEL
//