EUG1_YEAST
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 03-AUG-2022, entry version 178.
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; 155.
DR IntAct; P32474; 1.
DR STRING; 4932.YDR518W; -.
DR iPTMnet; P32474; -.
DR MaxQB; P32474; -.
DR PaxDb; P32474; -.
DR PRIDE; P32474; -.
DR EnsemblFungi; YDR518W_mRNA; YDR518W; YDR518W.
DR GeneID; 852130; -.
DR KEGG; sce:YDR518W; -.
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; ISQPNWT; -.
DR BioCyc; YEAST:YDR518W-MON; -.
DR Reactome; R-SCE-901042; Calnexin/calreticulin cycle.
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 InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
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
