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Protein

Protein EMP46

Gene

EMP46

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

Involved in the secretion of glycoproteins and in nucleus architecture and gene silencing.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi177 – 1771Potassium

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • glycoprotein binding Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lectin, Metal-binding, Potassium

Enzyme and pathway databases

BioCyciYEAST:G3O-32231-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein EMP46
Alternative name(s):
46 kDa endomembrane protein
Gene namesi
Name:EMP46
Ordered Locus Names:YLR080W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR080W.
SGDiS000004070. EMP46.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini47 – 408362LumenalSequence analysisAdd
BLAST
Transmembranei409 – 42921HelicalSequence analysisAdd
BLAST
Topological domaini430 – 44415CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • ER to Golgi transport vesicle Source: SGD
  • Golgi membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi177 – 1771Y → F: Impairs potassium-binding. 1 Publication
Mutagenesisi429 – 4291Y → A: Impairs interaction with COP1, SEC21 and SEC23 and loss of reticulum endoplasmic exit. 1 Publication
Mutagenesisi432 – 4321F → A: Impairs interaction with COP1, SEC21 and SEC23 and loss of reticulum endoplasmic exit. 1 Publication
Mutagenesisi440 – 4445Missing : Loss of endoplasmic reticulum exit. 1 Publication
Mutagenesisi440 – 4423KVK → SVS or RVR: Impairs interaction with COP1 and SEC21 and mislocalizes to the vacuole. 1 Publication
Mutagenesisi443 – 4442LL → AA: Loss of endoplasmic reticulum exit. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 46461 PublicationAdd
BLAST
Chaini47 – 444398Protein EMP46PRO_0000239645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi196 ↔ 230

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ12396.

Interactioni

Subunit structurei

Interacts with EMP47 in the endoplasmic reticulum membrane in order to be transported to the Golgi apparatus. Interacts with the coatomer proteins COP1, SEC21 and SEC23.2 Publications

GO - Molecular functioni

  • glycoprotein binding Source: SGD

Protein-protein interaction databases

BioGridi31353. 23 interactions.
DIPiDIP-4209N.
IntActiQ12396. 1 interaction.
MINTiMINT-497123.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi58 – 603Combined sources
Turni65 – 673Combined sources
Helixi71 – 744Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 825Combined sources
Beta strandi85 – 873Combined sources
Beta strandi90 – 934Combined sources
Beta strandi100 – 1078Combined sources
Beta strandi115 – 12511Combined sources
Beta strandi133 – 1397Combined sources
Turni150 – 1523Combined sources
Beta strandi158 – 16710Combined sources
Turni168 – 1703Combined sources
Beta strandi171 – 18313Combined sources
Turni187 – 1893Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi207 – 2148Combined sources
Helixi215 – 2173Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi228 – 2347Combined sources
Helixi238 – 2403Combined sources
Beta strandi244 – 2518Combined sources
Beta strandi258 – 26912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A6VX-ray1.52A/B52-275[»]
2A6WX-ray1.75A/B52-275[»]
2A6XX-ray1.55A/B52-275[»]
ProteinModelPortaliQ12396.
SMRiQ12396. Positions 55-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 269218L-type lectin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni429 – 4324Mediates the interactions with COPI and COPII coat complexes

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi440 – 4445Di-lysine motif

Domaini

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

Sequence similaritiesi

Belongs to the EMP46/EMP47 family.Curated
Contains 1 L-type lectin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00510000053646.
HOGENOMiHOG000112365.
InParanoidiQ12396.
KOiK10080.
OMAiGKIMAND.
OrthoDBiEOG7N6414.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016710. Emp46/Emp47.
IPR005052. Lectin_leg.
[Graphical view]
PfamiPF03388. Lectin_leg-like. 1 hit.
[Graphical view]
PIRSFiPIRSF018136. L-type_lectin_fungi. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTRKTASSL QLLGKITGTK AGTKQKKMNF INGLIWLYMC VWMVHGKVTQ
60 70 80 90 100
KDELKWNKGY SLPNLLEVTD QQKELSQWTL GDKVKLEEGR FVLTPGKNTK
110 120 130 140 150
GSLWLKPEYS IKDAMTIEWT FRSFGFRGST KGGLAFWLKQ GNEGDSTELF
160 170 180 190 200
GGSSKKFNGL MILLRLDDKL GESVTAYLND GTKDLDIESS PYFASCLFQY
210 220 230 240 250
QDSMVPSTLR LTYNPLDNHL LKLQMDNRVC FQTRKVKFMG SSPFRIGTSA
260 270 280 290 300
INDASKESFE ILKMKLYDGV IEDSLIPNVN PMGQPRVVTK VINSQTGEES
310 320 330 340 350
FREKMPFSDK EESITSNELF EKMNKLEGKI MANDIDPLLR KMNKIVENER
360 370 380 390 400
ELIQRLRPLL DLKKTAISDD SFQDFLSMNA NLDRLIKEQE KIRQDAKLYG
410 420 430 440
KQTKGHDEIF SKISVWLALL IFIMITLAYY MFRINQDIKK VKLL
Length:444
Mass (Da):50,947
Last modified:November 1, 1996 - v1
Checksum:i9B83B61667814DBE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73252 Genomic DNA. Translation: CAA97639.1.
U53880 Genomic DNA. Translation: AAB67584.1.
BK006945 Genomic DNA. Translation: DAA09396.1.
PIRiS64912.
RefSeqiNP_013181.1. NM_001181967.1.

Genome annotation databases

EnsemblFungiiYLR080W; YLR080W; YLR080W.
GeneIDi850769.
KEGGisce:YLR080W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73252 Genomic DNA. Translation: CAA97639.1.
U53880 Genomic DNA. Translation: AAB67584.1.
BK006945 Genomic DNA. Translation: DAA09396.1.
PIRiS64912.
RefSeqiNP_013181.1. NM_001181967.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A6VX-ray1.52A/B52-275[»]
2A6WX-ray1.75A/B52-275[»]
2A6XX-ray1.55A/B52-275[»]
ProteinModelPortaliQ12396.
SMRiQ12396. Positions 55-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31353. 23 interactions.
DIPiDIP-4209N.
IntActiQ12396. 1 interaction.
MINTiMINT-497123.

Proteomic databases

MaxQBiQ12396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR080W; YLR080W; YLR080W.
GeneIDi850769.
KEGGisce:YLR080W.

Organism-specific databases

EuPathDBiFungiDB:YLR080W.
SGDiS000004070. EMP46.

Phylogenomic databases

GeneTreeiENSGT00510000053646.
HOGENOMiHOG000112365.
InParanoidiQ12396.
KOiK10080.
OMAiGKIMAND.
OrthoDBiEOG7N6414.

Enzyme and pathway databases

BioCyciYEAST:G3O-32231-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12396.
PROiQ12396.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016710. Emp46/Emp47.
IPR005052. Lectin_leg.
[Graphical view]
PfamiPF03388. Lectin_leg-like. 1 hit.
[Graphical view]
PIRSFiPIRSF018136. L-type_lectin_fungi. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae."
    Sato K., Nakano A.
    Mol. Biol. Cell 13:2518-2532(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 47-56, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COP1; SEC21 AND SEC23, MUTAGENESIS OF TYR-429; PHE-432; 440-LYS--LYS-442; 440-LYS--LEU-444 AND 443-LEU-LEU-444.
  4. "Genome-wide nuclear morphology screen identifies novel genes involved in nuclear architecture and gene-silencing in Saccharomyces cerevisiae."
    Teixeira M.T., Dujon B., Fabre E.
    J. Mol. Biol. 321:551-561(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles."
    Sato K., Nakano A.
    Mol. Biol. Cell 14:3055-3063(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMP47, SUBCELLULAR LOCATION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. "Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting."
    Sato K., Nakano A.
    J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. "Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p."
    Satoh T., Sato K., Kanoh A., Yamashita K., Yamada Y., Igarashi N., Kato R., Nakano A., Wakatsuki S.
    J. Biol. Chem. 281:10410-10419(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 52-275, POTASSIUM-BINDING, MUTAGENESIS OF TYR-177.

Entry informationi

Entry nameiEMP46_YEAST
AccessioniPrimary (citable) accession number: Q12396
Secondary accession number(s): D6VY80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 113 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

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.