SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P40509

- COPE_YEAST

UniProt

P40509 - COPE_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Coatomer subunit epsilon

Gene
SEC28, YIL076W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. ER to Golgi vesicle-mediated transport Source: SGD
  2. late endosome to vacuole transport via multivesicular body sorting pathway Source: SGD
  3. protein transport Source: UniProtKB-KW
  4. retrograde vesicle-mediated transport, Golgi to ER Source: InterPro
  5. vesicle coating Source: SGD
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-31341-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit epsilon
Alternative name(s):
Epsilon-coat protein
Short name:
Epsilon-COP
Gene namesi
Name:SEC28
Ordered Locus Names:YIL076W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL076w.
SGDiS000001338. SEC28.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. COPI vesicle coat Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Coatomer subunit epsilonPRO_0000193856Add
BLAST

Proteomic databases

MaxQBiP40509.
PaxDbiP40509.
PeptideAtlasiP40509.

Expressioni

Gene expression databases

GenevestigatoriP40509.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with the ESCRT-0 subunit VPS27.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
COP1P536225EBI-4884,EBI-4860
SEC27P418114EBI-4884,EBI-4898
VPS27P403432EBI-4884,EBI-20380

Protein-protein interaction databases

BioGridi34916. 340 interactions.
DIPiDIP-4711N.
IntActiP40509. 18 interactions.
MINTiMINT-429031.
STRINGi4932.YIL076W.

Structurei

Secondary structure

1
296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107
Turni11 – 133
Helixi15 – 184
Helixi20 – 234
Helixi31 – 4313
Beta strandi52 – 543
Helixi57 – 6711
Helixi73 – 775
Turni78 – 814
Helixi86 – 9914
Helixi102 – 11312
Turni114 – 1174
Beta strandi118 – 1203
Helixi121 – 13414
Helixi138 – 15114
Helixi154 – 17522
Turni179 – 1813
Helixi182 – 19110
Helixi197 – 21014
Helixi213 – 22412
Helixi226 – 2294
Turni230 – 2323
Helixi234 – 2363
Beta strandi237 – 2393
Helixi240 – 25314
Helixi259 – 2679
Helixi273 – 29018

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MV2X-ray2.90B/D/F1-296[»]
3MV3X-ray3.25B/D/F1-296[»]
ProteinModelPortaliP40509.
SMRiP40509. Positions 1-293.

Miscellaneous databases

EvolutionaryTraceiP40509.

Family & Domainsi

Sequence similaritiesi

Belongs to the COPE family.

Phylogenomic databases

eggNOGiNOG252891.
HOGENOMiHOG000000967.
KOiK17268.
OMAiASTMFEN.
OrthoDBiEOG7PCJT7.

Family and domain databases

InterProiIPR006822. Coatomer_esu.
[Graphical view]
PANTHERiPTHR10805. PTHR10805. 1 hit.
PfamiPF04733. Coatomer_E. 1 hit.
[Graphical view]
PIRSFiPIRSF016478. Coatomer_esu. 1 hit.

Sequencei

Sequence statusi: Complete.

P40509-1 [UniParc]FASTAAdd to Basket

« Hide

MDYFNIKQNY YTGNFVQCLQ EIEKFSKVTD NTLLFYKAKT LLALGQYQSQ    50
DPTSKLGKVL DLYVQFLDTK NIEELENLLK DKQNSPYELY LLATAQAILG 100
DLDKSLETCV EGIDNDEAEG TTELLLLAIE VALLNNNVST ASTIFDNYTN 150
AIEDTVSGDN EMILNLAESY IKFATNKETA TSNFYYYEEL SQTFPTWKTQ 200
LGLLNLHLQQ RNIAEAQGIV ELLLSDYYSV EQKENAVLYK PTFLANQITL 250
ALMQGLDTED LTNQLVKLDH EHAFIKHHQE IDAKFDELVR KYDTSN 296
Length:296
Mass (Da):33,829
Last modified:December 15, 1998 - v2
Checksum:i95ACA8BB647817DB
GO

Sequence cautioni

The sequence CAA86094.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF043582 Genomic DNA. Translation: AAC14023.1.
Z37997 Genomic DNA. Translation: CAA86094.1. Different initiation.
BK006942 Genomic DNA. Translation: DAA08474.1.
PIRiS48368.
RefSeqiNP_012189.2. NM_001179426.1.

Genome annotation databases

EnsemblFungiiYIL076W; YIL076W; YIL076W.
GeneIDi854734.
KEGGisce:YIL076W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF043582 Genomic DNA. Translation: AAC14023.1 .
Z37997 Genomic DNA. Translation: CAA86094.1 . Different initiation.
BK006942 Genomic DNA. Translation: DAA08474.1 .
PIRi S48368.
RefSeqi NP_012189.2. NM_001179426.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MV2 X-ray 2.90 B/D/F 1-296 [» ]
3MV3 X-ray 3.25 B/D/F 1-296 [» ]
ProteinModelPortali P40509.
SMRi P40509. Positions 1-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34916. 340 interactions.
DIPi DIP-4711N.
IntActi P40509. 18 interactions.
MINTi MINT-429031.
STRINGi 4932.YIL076W.

Proteomic databases

MaxQBi P40509.
PaxDbi P40509.
PeptideAtlasi P40509.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIL076W ; YIL076W ; YIL076W .
GeneIDi 854734.
KEGGi sce:YIL076W.

Organism-specific databases

CYGDi YIL076w.
SGDi S000001338. SEC28.

Phylogenomic databases

eggNOGi NOG252891.
HOGENOMi HOG000000967.
KOi K17268.
OMAi ASTMFEN.
OrthoDBi EOG7PCJT7.

Enzyme and pathway databases

BioCyci YEAST:G3O-31341-MONOMER.

Miscellaneous databases

EvolutionaryTracei P40509.
NextBioi 977434.

Gene expression databases

Genevestigatori P40509.

Family and domain databases

InterProi IPR006822. Coatomer_esu.
[Graphical view ]
PANTHERi PTHR10805. PTHR10805. 1 hit.
Pfami PF04733. Coatomer_E. 1 hit.
[Graphical view ]
PIRSFi PIRSF016478. Coatomer_esu. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. 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.

Entry informationi

Entry nameiCOPE_YEAST
AccessioniPrimary (citable) accession number: P40509
Secondary accession number(s): D6VVK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 15, 1998
Last modified: September 3, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 23100 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

Similar proteinsi