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Protein

ER-derived vesicles protein ERV29

Gene

ERV29

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Constituent of COPII-coated endoplasmic reticulum-derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal di-lysine motif is required for exit from the endoplasmic reticulum. Required directly for packaging glycosylated pro-alpha-factor into COPII vesicles. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum.2 Publications

GO - Molecular functioni

  • COPII adaptor activity Source: SGD

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30946-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.
R-SCE-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
ER-derived vesicles protein ERV29
Gene namesi
Name:ERV29
Ordered Locus Names:YGR284C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR284C.
SGDiS000003516. ERV29.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 108CytoplasmicSequence analysisAdd BLAST108
Transmembranei109 – 129HelicalSequence analysisAdd BLAST21
Topological domaini130 – 137LumenalSequence analysis8
Transmembranei138 – 158HelicalSequence analysisAdd BLAST21
Topological domaini159 – 160CytoplasmicSequence analysis2
Transmembranei161 – 181HelicalSequence analysisAdd BLAST21
Topological domaini182 – 209LumenalSequence analysisAdd BLAST28
Transmembranei210 – 230HelicalSequence analysisAdd BLAST21
Topological domaini231 – 245CytoplasmicSequence analysisAdd BLAST15
Transmembranei246 – 266HelicalSequence analysisAdd BLAST21
Topological domaini267 – 282LumenalSequence analysisAdd BLAST16
Transmembranei283 – 303HelicalSequence analysisAdd BLAST21
Topological domaini304 – 310CytoplasmicSequence analysis7

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001276711 – 310ER-derived vesicles protein ERV29Add BLAST310

Proteomic databases

MaxQBiP53337.
PRIDEiP53337.
TopDownProteomicsiP53337.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SSH1P383533EBI-23662,EBI-18175

GO - Molecular functioni

  • COPII adaptor activity Source: SGD

Protein-protein interaction databases

BioGridi33534. 114 interactors.
DIPiDIP-8110N.
IntActiP53337. 44 interactors.
MINTiMINT-1356006.

Structurei

3D structure databases

ProteinModelPortaliP53337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi307 – 310Di-lysine motif4

Domaini

The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.By similarity

Sequence similaritiesi

Belongs to the SURF4 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000064123.
HOGENOMiHOG000206959.
InParanoidiP53337.
KOiK20369.
OMAiSIVRDKR.
OrthoDBiEOG092C3ID0.

Family and domain databases

InterProiIPR002995. Surf4.
[Graphical view]
PfamiPF02077. SURF4. 1 hit.
[Graphical view]
PROSITEiPS01339. SURF4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYRGPIGNF GGMPMSSSQG PYSGGAQFRS NQNQSTSGIL KQWKHSFEKF
60 70 80 90 100
ASRIEGLTDN AVVYKLKPYI PSLSRFFIVA TFYEDSFRIL SQWSDQIFYL
110 120 130 140 150
NKWKHYPYFF VVVFLVVVTV SMLIGASLLV LRKQTNYATG VLCACVISQA
160 170 180 190 200
LVYGLFTGSS FVLRNFSVIG GLLIAFSDSI VQNKTTFGML PELNSKNDKA
210 220 230 240 250
KGYLLFAGRI LIVLMFIAFT FSKSWFTVVL TIIGTICFAI GYKTKFASIM
260 270 280 290 300
LGLILTFYNI TLNNYWFYNN TKRDFLKYEF YQNLSIIGGL LLVTNTGAGE
310
LSVDEKKKIY
Length:310
Mass (Da):35,013
Last modified:October 1, 1996 - v1
Checksum:i6AE744904294DC76
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64Y → C in AAS56155 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73069 Genomic DNA. Translation: CAA97315.1.
AY557829 Genomic DNA. Translation: AAS56155.1.
BK006941 Genomic DNA. Translation: DAA08372.1.
PIRiS64619.
RefSeqiNP_011800.3. NM_001181413.3.

Genome annotation databases

EnsemblFungiiYGR284C; YGR284C; YGR284C.
GeneIDi853201.
KEGGisce:YGR284C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73069 Genomic DNA. Translation: CAA97315.1.
AY557829 Genomic DNA. Translation: AAS56155.1.
BK006941 Genomic DNA. Translation: DAA08372.1.
PIRiS64619.
RefSeqiNP_011800.3. NM_001181413.3.

3D structure databases

ProteinModelPortaliP53337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33534. 114 interactors.
DIPiDIP-8110N.
IntActiP53337. 44 interactors.
MINTiMINT-1356006.

Proteomic databases

MaxQBiP53337.
PRIDEiP53337.
TopDownProteomicsiP53337.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR284C; YGR284C; YGR284C.
GeneIDi853201.
KEGGisce:YGR284C.

Organism-specific databases

EuPathDBiFungiDB:YGR284C.
SGDiS000003516. ERV29.

Phylogenomic databases

GeneTreeiENSGT00530000064123.
HOGENOMiHOG000206959.
InParanoidiP53337.
KOiK20369.
OMAiSIVRDKR.
OrthoDBiEOG092C3ID0.

Enzyme and pathway databases

BioCyciYEAST:G3O-30946-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.
R-SCE-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Miscellaneous databases

PROiP53337.

Family and domain databases

InterProiIPR002995. Surf4.
[Graphical view]
PfamiPF02077. SURF4. 1 hit.
[Graphical view]
PROSITEiPS01339. SURF4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERV29_YEAST
AccessioniPrimary (citable) accession number: P53337
Secondary accession number(s): D6VV61, E9P8T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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