COPE_YEAST
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 03-AUG-2022, entry version 176.
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;
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=11; IntAct=EBI-4884, EBI-4860;
CC P40509; P41811: SEC27; NbExp=4; 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 PDBsum; 3MV2; -.
DR PDBsum; 3MV3; -.
DR PDBsum; 6U3W; -.
DR AlphaFoldDB; P40509; -.
DR SMR; P40509; -.
DR BioGRID; 34916; 580.
DR ComplexPortal; CPX-1652; COPI vesicle coat complex.
DR DIP; DIP-4711N; -.
DR IntAct; P40509; 20.
DR MINT; P40509; -.
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 MaxQB; P40509; -.
DR PaxDb; P40509; -.
DR PRIDE; P40509; -.
DR EnsemblFungi; YIL076W_mRNA; YIL076W; YIL076W.
DR GeneID; 854734; -.
DR KEGG; sce:YIL076W; -.
DR SGD; S000001338; SEC28.
DR VEuPathDB; FungiDB:YIL076W; -.
DR eggNOG; KOG3081; Eukaryota.
DR GeneTree; ENSGT00390000003478; -.
DR HOGENOM; CLU_075638_0_0_1; -.
DR InParanoid; P40509; -.
DR OMA; SNFYYFE; -.
DR BioCyc; YEAST:G3O-31341-MON; -.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
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:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IC:ComplexPortal.
DR GO; GO:0006901; P:vesicle coating; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006822; Coatomer_esu.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10805; PTHR10805; 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
