P40509 (COPE_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Coatomer subunit epsilon Alternative name(s): Epsilon-coat protein Short name=Epsilon-COP | ||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||
| Taxonomic identifier | 559292 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 296 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors By similarity. Ref.1 Ref.7 |
| Subunit structure | Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with the ESCRT-0 subunit VPS27. Ref.7 |
| Subcellular location | Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle › COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it By similarity. Ref.4 Ref.7 |
| Miscellaneous | Present with 23100 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the COPE family. |
| Sequence caution | The sequence CAA86094.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | ER-Golgi transport Protein transport Transport |
| Cellular component | Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | ER to Golgi vesicle-mediated transport Inferred from mutant phenotype PubMed 10532354. Source: SGD late endosome to vacuole transport via multivesicular body sorting pathwayInferred from mutant phenotype Ref.7. Source: SGD protein transportInferred from electronic annotation. Source: UniProtKB-KW retrograde vesicle-mediated transport, Golgi to ERInferred from electronic annotation. Source: InterPro vesicle coatingInferred from mutant phenotype Ref.1. Source: SGD |
| Cellular_component | COPI vesicle coat Inferred from mutant phenotype Ref.1. Source: SGD |
| Molecular_function | structural molecule activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| COP1 | P53622 | 9 | EBI-4884,EBI-4860 | |
| SEC27 | P41811 | 7 | EBI-4884,EBI-4898 | |
| VPS27 | P40343 | 2 | EBI-4884,EBI-20380 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 296 | 296 | Coatomer subunit epsilon | PRO_0000193856 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 4 – 10 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 11 – 13 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 15 – 18 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 20 – 23 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 31 – 43 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 52 – 54 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 57 – 67 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 73 – 77 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 78 – 81 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 86 – 99 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 102 – 113 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 114 – 117 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 118 – 120 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 121 – 134 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 138 – 151 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 154 – 175 | 22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 179 – 181 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 182 – 191 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 197 – 210 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 213 – 224 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 226 – 229 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 230 – 232 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 234 – 236 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 237 – 239 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 240 – 253 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 259 – 267 | 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 273 – 290 | 18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Epsilon-COP is a structural component of coatomer that functions to stabilize alpha-COP." Duden R., Kajikawa L., Wuestehube L., Schekman R. EMBO J. 17:985-995(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF INITIATION SITE, FUNCTION. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G.Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [3] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [4] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [5] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [6] | "Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE." Zhang Z., Dietrich F.S. Nucleic Acids Res. 33:2838-2851(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE. |
| [7] | "Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast." Gabriely G., Kama R., Gerst J.E. Mol. Cell. Biol. 27:526-540(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS27. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF043582 Genomic DNA. Translation: AAC14023.1. Z37997 Genomic DNA. Translation: CAA86094.1. Different initiation. BK006942 Genomic DNA. Translation: DAA08474.1. | ||||||||||||||||||
| PIR | S48368. | ||||||||||||||||||
| RefSeq | NP_012189.2. NM_001179426.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P40509. | ||||||||||||||||||
| SMR | P40509. Positions 1-293. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-4711N. | ||||||||||||||||||
| IntAct | P40509. 17 interactions. | ||||||||||||||||||
| MINT | MINT-429031. | ||||||||||||||||||
| STRING | 4932.YIL076W. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | P40509. | ||||||||||||||||||
| PeptideAtlas | P40509. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblFungi | YIL076W; YIL076W; YIL076W. | ||||||||||||||||||
| GeneID | 854734. | ||||||||||||||||||
| KEGG | sce:YIL076W. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CYGD | YIL076w. | ||||||||||||||||||
| SGD | S000001338. SEC28. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | NOG252891. | ||||||||||||||||||
| HOGENOM | HOG000000967. | ||||||||||||||||||
| OMA | ASTMFEN. | ||||||||||||||||||
| OrthoDB | EOG41RT44. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| Genevestigator | P40509. | ||||||||||||||||||
| GermOnline | YIL076W. Saccharomyces cerevisiae. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR006822. Coatomer_esu. [Graphical view] | ||||||||||||||||||
| Pfam | PF04733. Coatomer_E. 1 hit. [Graphical view] | ||||||||||||||||||
| PIRSF | PIRSF016478. Coatomer_esu. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P40509. | ||||||||||||||||||
| NextBio | 977434. | ||||||||||||||||||
Entry information
| Entry name | COPE_YEAST | ||||||||
| Accession | Primary (citable) accession number: P40509 Secondary accession number(s): D6VVK8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome IX Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
