The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP.

doi:10.1083/jcb.131.4.895

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Article

The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP.

The Journal of cell biology - 1 Nov 1995

Schröder S, Schimmöller F, Singer-Krüger B, Riezman H

Abstract excerpt

The Saccharomyces cerevisiae EMP47 gene encodes a nonessential type-I transmembrane protein with sequence homology to a class of intracellular lectins defined by ERGIC-53 and VIP36. The 12-amino acid COOH-terminal cytoplasmic tail of Emp47p ends in the sequence KTKLL, which conforms with the consensus for di-lysine-based ER-localization signals. Despite the presence of this motif, Emp47p was shown to be a Golgi...

Topics

Amino Acid Sequence
Base Sequence
Coatomer Protein
Endoplasmic Reticulum
Fungal Proteins
Golgi Apparatus
Lectins
Lysine
Mannose
Mannose-Binding Lectins
Mannosyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Molecular Sequence Data

Mutation

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Sequence Homology, Amino Acid

Subcellular Fractions

Source

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Identifiers

PMID: 7490292
DOI: 10.1083/jcb.131.4.895
PMCID: PMC2200007

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7490292-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP.PMID 7490292Read ↗

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