ID   COPE_YEAST              Reviewed;         296 AA.
AC   P40509; D6VVK8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   04-NOV-2026, entry version 192.
DE   RecName: Full=Coatomer subunit epsilon;
DE   AltName: Full=Epsilon-coat protein;
DE            Short=Epsilon-COP;
GN   Name=SEC28; OrderedLocusNames=YIL076W;
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 [GENOMIC DNA], IDENTIFICATION OF INITIATION SITE, AND
RP   FUNCTION.
RX   PubMed=9463377; DOI=10.1093/emboj/17.4.985;
RA   Duden R., Kajikawa L., Wuestehube L., Schekman R.;
RT   "Epsilon-COP is a structural component of coatomer that functions to
RT   stabilize alpha-COP.";
RL   EMBO J. 17:985-995(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870; DOI=10.1038/387s084;
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   [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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
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   [6]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=15905473; DOI=10.1093/nar/gki583;
RA   Zhang Z., Dietrich F.S.;
RT   "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT   SAGE.";
RL   Nucleic Acids Res. 33:2838-2851(2005).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS27.
RX   PubMed=17101773; DOI=10.1128/mcb.00577-06;
RA   Gabriely G., Kama R., Gerst J.E.;
RT   "Involvement of specific COPI subunits in protein sorting from the late
RT   endosome to the vacuole in yeast.";
RL   Mol. Cell. Biol. 27:526-540(2007).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. The coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC       {ECO:0000269|PubMed:17101773, ECO:0000269|PubMed:9463377}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. Interacts with the
CC       ESCRT-0 subunit VPS27. {ECO:0000269|PubMed:17101773}.
CC   -!- INTERACTION:
CC       P40509; P53622: COP1; NbExp=12; IntAct=EBI-4884, EBI-4860;
CC       P40509; P41811: SEC27; NbExp=5; IntAct=EBI-4884, EBI-4898;
CC       P40509; P40343: VPS27; NbExp=2; IntAct=EBI-4884, EBI-20380;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 23100 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the COPE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA86094.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF043582; AAC14023.1; -; Genomic_DNA.
DR   EMBL; Z37997; CAA86094.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006942; DAA08474.1; -; Genomic_DNA.
DR   PIR; S48368; S48368.
DR   RefSeq; NP_012189.2; NM_001179426.1.
DR   PDB; 3MV2; X-ray; 2.90 A; B/D/F=1-296.
DR   PDB; 3MV3; X-ray; 3.25 A; B/D/F=1-296.
DR   PDB; 6U3W; X-ray; 2.39 A; B=1-296.
DR   AlphaFoldDB; P40509; -.
DR   SMR; P40509; -.
DR   BioGRID; 34916; 595.
DR   ComplexPortal; CPX-1652; COPI vesicle coat complex.
DR   DIP; DIP-4711N; -.
DR   FunCoup; P40509; 295.
DR   IntAct; P40509; 27.
DR   STRING; 4932.YIL076W; -.
DR   TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR   iPTMnet; P40509; -.
DR   PaxDb; 4932-YIL076W; -.
DR   PeptideAtlas; P40509; -.
DR   EnsemblFungi; YIL076W_mRNA; YIL076W; YIL076W.
DR   GeneID; 854734; -.
DR   KEGG; sce:YIL076W; -.
DR   AGR; SGD:S000001338; -.
DR   SGD; S000001338; SEC28.
DR   VEuPathDB; FungiDB:YIL076W; -.
DR   eggNOG; KOG3081; Eukaryota.
DR   HOGENOM; CLU_075638_0_0_1; -.
DR   InParanoid; P40509; -.
DR   OMA; AAWETCT; -.
DR   OrthoDB; 310217at2759; -.
DR   BioCyc; YEAST:G3O-31341-MONOMER; -.
DR   Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 854734; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P40509; -.
DR   PRO; PR:P40509; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40509; protein.
DR   GO; GO:0030126; C:COPI vesicle coat; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:SGD.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:GO_Central.
DR   GO; GO:0006901; P:vesicle coat assembly; IMP:SGD.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR006822; Coatomer_esu.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10805; COATOMER SUBUNIT EPSILON; 1.
DR   PANTHER; PTHR10805:SF0; COATOMER SUBUNIT EPSILON; 1.
DR   Pfam; PF04733; Coatomer_E; 1.
DR   PIRSF; PIRSF016478; Coatomer_esu; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..296
FT                   /note="Coatomer subunit epsilon"
FT                   /id="PRO_0000193856"
FT   HELIX           4..11
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            24..27
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           55..69
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           86..98
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           102..111
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            114..117
FT                   /evidence="ECO:0007829|PDB:3MV3"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:3MV3"
FT   HELIX           121..134
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           138..150
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            153..155
FT                   /evidence="ECO:0007829|PDB:3MV3"
FT   HELIX           160..174
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            179..181
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           182..193
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           197..209
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           213..224
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           226..229
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   TURN            230..232
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           233..254
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           259..268
FT                   /evidence="ECO:0007829|PDB:6U3W"
FT   HELIX           273..291
FT                   /evidence="ECO:0007829|PDB:6U3W"
SQ   SEQUENCE   296 AA;  33829 MW;  95ACA8BB647817DB CRC64;
     MDYFNIKQNY YTGNFVQCLQ EIEKFSKVTD NTLLFYKAKT LLALGQYQSQ DPTSKLGKVL
     DLYVQFLDTK NIEELENLLK DKQNSPYELY LLATAQAILG DLDKSLETCV EGIDNDEAEG
     TTELLLLAIE VALLNNNVST ASTIFDNYTN AIEDTVSGDN EMILNLAESY IKFATNKETA
     TSNFYYYEEL SQTFPTWKTQ LGLLNLHLQQ RNIAEAQGIV ELLLSDYYSV EQKENAVLYK
     PTFLANQITL ALMQGLDTED LTNQLVKLDH EHAFIKHHQE IDAKFDELVR KYDTSN
//