EPS1_YEAST
ID EPS1_YEAST Reviewed; 701 AA.
AC P40557; D6VVS5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=ER-retained PMA1-suppressing protein 1;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=EPS1; OrderedLocusNames=YIL005W; ORFNames=YIA5W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-701.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762303; DOI=10.1002/yea.320110109;
RA Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT "Nucleotide sequence and analysis of the centromeric region of yeast
RT chromosome IX.";
RL Yeast 11:61-78(1995).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10545109; DOI=10.1093/emboj/18.21.5972;
RA Wang Q., Chang A.;
RT "Eps1, a novel PDI-related protein involved in ER quality control in
RT yeast.";
RL EMBO J. 18:5972-5982(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PMA1.
RX PubMed=12881414; DOI=10.1093/emboj/cdg378;
RA Wang Q., Chang A.;
RT "Substrate recognition in ER-associated degradation mediated by Eps1, a
RT member of the protein disulfide isomerase family.";
RL EMBO J. 22:3792-3802(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=15848158; DOI=10.1016/j.febslet.2005.03.019;
RA He J., Sakamoto T., Song Y., Saito A., Harada A., Azakami H., Kato A.;
RT "Effect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion
RT of foreign proteins which have disulfide bridges.";
RL FEBS Lett. 579:2277-2283(2005).
RN [9]
RP INTERACTION WITH EUG1; KAR2; MPD1 AND PDI1.
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: Acts as a membrane-bound chaperone in endoplasmic reticulum
CC quality control. Probably facilitates presentation of substrate to
CC membrane-bound components of the degradation machinery.
CC {ECO:0000269|PubMed:10545109, ECO:0000269|PubMed:12881414,
CC ECO:0000269|PubMed:15848158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBUNIT: Interacts with mutated PMA1-D378N but not wild type PMA1.
CC Interacts with EUG1, KAR2, MPD1 AND PDI1. {ECO:0000269|PubMed:12881414,
CC ECO:0000269|PubMed:16002399}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10545109, ECO:0000269|PubMed:12881414}; Single-pass
CC membrane protein {ECO:0000269|PubMed:10545109,
CC ECO:0000269|PubMed:12881414}.
CC -!- MISCELLANEOUS: Present with 6020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; Z38113; CAA86246.1; -; Genomic_DNA.
DR EMBL; AY723829; AAU09746.1; -; Genomic_DNA.
DR EMBL; X79743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006942; DAA08541.1; -; Genomic_DNA.
DR PIR; S48452; S48452.
DR RefSeq; NP_012261.1; NM_001179355.1.
DR AlphaFoldDB; P40557; -.
DR SMR; P40557; -.
DR BioGRID; 34987; 72.
DR DIP; DIP-3860N; -.
DR IntAct; P40557; 2.
DR MINT; P40557; -.
DR STRING; 4932.YIL005W; -.
DR iPTMnet; P40557; -.
DR MaxQB; P40557; -.
DR PaxDb; P40557; -.
DR PRIDE; P40557; -.
DR EnsemblFungi; YIL005W_mRNA; YIL005W; YIL005W.
DR GeneID; 854812; -.
DR KEGG; sce:YIL005W; -.
DR SGD; S000001267; EPS1.
DR VEuPathDB; FungiDB:YIL005W; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_024937_0_0_1; -.
DR InParanoid; P40557; -.
DR OMA; RQVNCVE; -.
DR BioCyc; YEAST:G3O-31284-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P40557; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40557; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IMP:SGD.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0006621; P:protein retention in ER lumen; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Membrane; Redox-active center; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..701
FT /note="ER-retained PMA1-suppressing protein 1"
FT /id="PRO_0000034221"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 28..142
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 408..446
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..63
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 200..203
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 701 AA; 81219 MW; 31666693790E04EB CRC64;
MKMNLKRLVV TFFSCITFLL KFTIAAAEPP EGFPEPLNPT NFKEELSKGL HIIDFYSPYC
PHCKHLAPVW METWEEFKEE SKTLNITFSQ VNCIESADLC GDENIEYFPE IRLYNPSGYI
KSFTETPRTK ESLIAFARRE SMDPNNLDTD LDSAKSESQY LEGFDFLELI AGKATRPHLV
SFWPTKDMKN SDDSLEFKNC DKCHEFQRTW KIISRQLAVD DINTGHVNCE SNPTICEELG
FGDLVKITNH RADREPKVAL VLPNKTSNNL FDYPNGYSAK SDGYVDFARR TFTNSKFPNI
TEGELEKKAN RDIDFLQERG RVTNNDIHLV FSYDPETVVI EDFDILEYLI EPLSKIPNIY
LHQIDKNLIN LSRNLFGRMY EKINYDASQT QKVFNKEYFT MNTVTQLPTF FMFKDGDPIS
YVFPGYSTTE MRNIDAIMDW VKKYSNPLVT EVDSSNLKKL ISFQTKSYSD LAIQLISSTD
HKHIKGSNKL IKNLLLASWE YEHIRMENNF EEINERRARK ADGIKKIKEK KAPANKIVDK
MREEIPHMDQ KKLLLGYLDI SKEKNFFRKY GITGEYKIGD VIIIDKSNNY YYNKDNFGNS
LTSNNPQLLR EAFVSLNIPS KALYSSKLKG RLINSPFHNV LSFLDIIHGN GMPGYLIVIV
LFIAILKGPS IYRRYKVRKH YRAKRNAVGI LGNMEKKKNQ D
