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P40509 (COPE_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coatomer subunit epsilon
Alternative name(s):
Epsilon-coat protein
Short name=Epsilon-COP
Gene names
Name:SEC28
Ordered Locus Names:YIL076W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence 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. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. 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 vesicleCOPI-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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296Coatomer subunit epsilon
PRO_0000193856

Secondary structure

.............................................. 296
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40509 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 95ACA8BB647817DB

FASTA29633,829
        10         20         30         40         50         60 
MDYFNIKQNY YTGNFVQCLQ EIEKFSKVTD NTLLFYKAKT LLALGQYQSQ DPTSKLGKVL 

        70         80         90        100        110        120 
DLYVQFLDTK NIEELENLLK DKQNSPYELY LLATAQAILG DLDKSLETCV EGIDNDEAEG 

       130        140        150        160        170        180 
TTELLLLAIE VALLNNNVST ASTIFDNYTN AIEDTVSGDN EMILNLAESY IKFATNKETA 

       190        200        210        220        230        240 
TSNFYYYEEL SQTFPTWKTQ LGLLNLHLQQ RNIAEAQGIV ELLLSDYYSV EQKENAVLYK 

       250        260        270        280        290 
PTFLANQITL ALMQGLDTED LTNQLVKLDH EHAFIKHHQE IDAKFDELVR KYDTSN 

« Hide

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. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
PIRS48368.
RefSeqNP_012189.2. NM_001179426.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MV2X-ray2.90B/D/F1-296[»]
3MV3X-ray3.25B/D/F1-296[»]
ProteinModelPortalP40509.
SMRP40509. Positions 1-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34916. 339 interactions.
DIPDIP-4711N.
IntActP40509. 18 interactions.
MINTMINT-429031.
STRING4932.YIL076W.

Proteomic databases

MaxQBP40509.
PaxDbP40509.
PeptideAtlasP40509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL076W; YIL076W; YIL076W.
GeneID854734.
KEGGsce:YIL076W.

Organism-specific databases

CYGDYIL076w.
SGDS000001338. SEC28.

Phylogenomic databases

eggNOGNOG252891.
HOGENOMHOG000000967.
KOK17268.
OMAASTMFEN.
OrthoDBEOG7PCJT7.

Enzyme and pathway databases

BioCycYEAST:G3O-31341-MONOMER.

Gene expression databases

GenevestigatorP40509.

Family and domain databases

InterProIPR006822. Coatomer_esu.
[Graphical view]
PANTHERPTHR10805. PTHR10805. 1 hit.
PfamPF04733. Coatomer_E. 1 hit.
[Graphical view]
PIRSFPIRSF016478. Coatomer_esu. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP40509.
NextBio977434.

Entry information

Entry nameCOPE_YEAST
AccessionPrimary (citable) accession number: P40509
Secondary accession number(s): D6VVK8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references