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Protein

Coatomer subunit delta

Gene

RET2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).By similarity

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: SGD
  • Golgi inheritance Source: SGD
  • Golgi localization Source: SGD
  • protein transport Source: UniProtKB-KW
  • retrograde vesicle-mediated transport, Golgi to ER Source: SGD
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30497-MONOMER.
ReactomeiR-SCE-6807878. COPI-mediated anterograde transport.
R-SCE-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit delta
Alternative name(s):
Delta-coat protein
Short name:
Delta-COP
Gene namesi
Name:RET2
Ordered Locus Names:YFR051C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFR051C.
SGDiS000001947. RET2.

Subcellular locationi

GO - Cellular componenti

  • 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
Initiator methionineiRemoved1 Publication
Chaini2 – 546545Coatomer subunit deltaPRO_0000193848Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei277 – 2771PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43621.

PTM databases

iPTMnetiP43621.

Interactioni

Subunit structurei

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with DSL1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RET3P536003EBI-4876,EBI-4905

Protein-protein interaction databases

BioGridi31209. 176 interactions.
DIPiDIP-5255N.
IntActiP43621. 37 interactions.
MINTiMINT-548122.

Structurei

Secondary structure

1
546
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi289 – 30315Combined sources
Beta strandi309 – 32214Combined sources
Helixi325 – 3273Combined sources
Beta strandi328 – 3347Combined sources
Helixi343 – 3453Combined sources
Helixi355 – 3617Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi380 – 38910Combined sources
Beta strandi398 – 40710Combined sources
Beta strandi409 – 42214Combined sources
Beta strandi428 – 4369Combined sources
Helixi447 – 4493Combined sources
Turni451 – 4544Combined sources
Beta strandi456 – 4583Combined sources
Beta strandi463 – 47311Combined sources
Beta strandi478 – 4869Combined sources
Helixi490 – 4934Combined sources
Beta strandi495 – 4995Combined sources
Beta strandi501 – 5055Combined sources
Beta strandi517 – 5248Combined sources
Beta strandi525 – 5295Combined sources
Beta strandi533 – 54513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FJWX-ray2.80A/B/C/D/E/F/G/H288-546[»]
5FJXX-ray2.45A/B/C282-546[»]
5FJZX-ray1.90A/B/C/D282-546[»]
5FK0X-ray3.00A/B/C/D/E/F/G/H282-546[»]
ProteinModelPortaliP43621.
SMRiP43621. Positions 1-135, 293-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini288 – 546259MHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 440251Interaction with DSL1Add
BLAST

Sequence similaritiesi

Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000017207.
HOGENOMiHOG000203984.
InParanoidiP43621.
OMAiQAVASHG.
OrthoDBiEOG72ZCQF.

Family and domain databases

InterProiIPR022775. AP_mu_sigma_su.
IPR027059. Coatomer_dsu.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PANTHERiPTHR10121. PTHR10121. 1 hit.
PfamiPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43621-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVLAASITT RQGKPLLSRQ FKDLSKDRVL ELLSNFQNLV SEISSDHTFV
60 70 80 90 100
EDKHVRYVYR PFDNYYIILI TNRQSNIIKD LATLNLFSQT INSYLSSFQD
110 120 130 140 150
QEIFHNAFEI LSSFDEIVSM GGYKENLSFT QVQTYLSMES HEERIQEIIE
160 170 180 190 200
RNKEIEATEE RKRRAKEIAR KEHERKHGFM SSNGDYDGAN RFMGSKDPNV
210 220 230 240 250
TNAINSYYSH ASPAAQQSYL QSSHAAAAEV APVASPMATS QRAGHSATGG
260 270 280 290 300
MKLGGGAGRR AGAAPRPSAI SSASSGTPPP PEEDVPENNG ILISIKEVIN
310 320 330 340 350
AEFSRDGTIH SSELKGVLEL RINDHDLSHS NLKLADSIDV RDKSFQFKTH
360 370 380 390 400
PNIDKQSFLS TKLISLRDKS KAFPANDQSL GVLRWRKVAP AEDDSLIPLT
410 420 430 440 450
LTTWVSPSES QQGFDVIIEY ESVLETELAD VIFTIPVFPQ EPVDINTESS
460 470 480 490 500
TCSDAEVVNM DQEMGTSIKI SKIAANDAGA LAFTIEAPYE DALYPMTVSF
510 520 530 540
QESTRDKLAK SFTGMAIQSV VMANDHDQEL PYDVITSLKS DEYLVQ
Length:546
Mass (Da):60,628
Last modified:January 23, 2007 - v3
Checksum:iAA730F046655EE5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09290.1.
BK006940 Genomic DNA. Translation: DAA12494.1.
PIRiS56306.
RefSeqiNP_116709.3. NM_001180016.3.

Genome annotation databases

EnsemblFungiiBAA09290; BAA09290; BAA09290.
YFR051C; YFR051C; YFR051C.
GeneIDi850612.
KEGGisce:YFR051C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09290.1.
BK006940 Genomic DNA. Translation: DAA12494.1.
PIRiS56306.
RefSeqiNP_116709.3. NM_001180016.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FJWX-ray2.80A/B/C/D/E/F/G/H288-546[»]
5FJXX-ray2.45A/B/C282-546[»]
5FJZX-ray1.90A/B/C/D282-546[»]
5FK0X-ray3.00A/B/C/D/E/F/G/H282-546[»]
ProteinModelPortaliP43621.
SMRiP43621. Positions 1-135, 293-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31209. 176 interactions.
DIPiDIP-5255N.
IntActiP43621. 37 interactions.
MINTiMINT-548122.

PTM databases

iPTMnetiP43621.

Proteomic databases

MaxQBiP43621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09290; BAA09290; BAA09290.
YFR051C; YFR051C; YFR051C.
GeneIDi850612.
KEGGisce:YFR051C.

Organism-specific databases

EuPathDBiFungiDB:YFR051C.
SGDiS000001947. RET2.

Phylogenomic databases

GeneTreeiENSGT00390000017207.
HOGENOMiHOG000203984.
InParanoidiP43621.
OMAiQAVASHG.
OrthoDBiEOG72ZCQF.

Enzyme and pathway databases

BioCyciYEAST:G3O-30497-MONOMER.
ReactomeiR-SCE-6807878. COPI-mediated anterograde transport.
R-SCE-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Miscellaneous databases

PROiP43621.

Family and domain databases

InterProiIPR022775. AP_mu_sigma_su.
IPR027059. Coatomer_dsu.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PANTHERiPTHR10121. PTHR10121. 1 hit.
PfamiPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
    Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
    Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  4. "Delta- and zeta-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval."
    Cosson P., Demolliere C., Hennecke S., Duden R., Letourneur F.
    EMBO J. 15:1792-1798(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15, CHARACTERIZATION.
  5. "Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat."
    Andag U., Schmitt H.D.
    J. Biol. Chem. 278:51722-51734(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DSL1.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOPD_YEAST
AccessioniPrimary (citable) accession number: P43621
Secondary accession number(s): D6VTT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.