RER2/YBR002C Summary Help

Standard Name RER2 1
Systematic Name YBR002C
Feature Type ORF, Verified
Description Cis-prenyltransferase involved in dolichol synthesis; major enzyme of polyprenol synthesis in both the endoplasmic reticulum (ER) and in lipid droplets; participates in ER protein sorting (2, 3 and see Summary Paragraph)
Name Description Retention in the Endoplasmic Reticulum 1
Chromosomal Location
ChrII:242568 to 241708 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All RER2 GO evidence and references
  View Computational GO annotations for RER2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
null
Resources
29 total interaction(s) for 23 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-RNA: 2
  • Co-purification: 1
  • PCA: 10

Genetic Interactions
  • Dosage Rescue: 4
  • Negative Genetic: 1
  • Phenotypic Suppression: 2
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 3

Resources
Expression Summary
histogram
Resources
Length (a.a.) 286
Molecular Weight (Da) 32,693
Isoelectric Point (pI) 7.79
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrII:242568 to 241708 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..861 242568..241708 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000206
SUMMARY PARAGRAPH for RER2

Dolichols are a class of polyisoprenoid alcohols with five or more isoprene units in which the C2-C3 bond is saturated. In yeast, dolichols with 14-18 isoprene units are the carrier molecules on which many of the steps in N-linked glycosylation, O-linked glycosylation, and GPI anchor synthesis occur on the membrane of the endoplasmic reticulum (ER) (reviewed in 4). In mammals, dolichols with 19-22 isoprene units are the carrier molecules on which these steps occur.

RER2 encodes a cis-prenyltransferase that catalyzes the formation of dehydrodolichyl diphosphate, the committed step in dolichol synthesis, from farnesyl diphosphate and an isopentenyl pyrophosphate with 10-14 isoprene units. This results in the formation of a dolichol precursor with 14-18 isoprene units (2, 5). Rer2p is peripherally associated with the ER membrane (2, 5). RER2 is expressed in the early logarithmic phase (5). Overexpression of Erg20p, which synthesizes the Rer2p substrate farnesyl diphosphate, induces expression of RER2, SRT1, and DPM1.

Originally isolated as a mutant defective in retaining certain proteins in the ER (2), rer2 cells also grow slowly (2, 1) have defects in N-linked and O-linked glycosylation (2, 6), and form clumps when grown in suspension (2). They accumulate excessive ER and Golgi membrane material and are sensitive to hygromycin B and resistant to sodium orthovanadate (2).

Overexpression of the Rer2p homolog Srt1p, which synthesizes dolichol precursors with 19-22 isoprene units, suppresses deletion of RER2, but the resultant cells make only the longer-chain dolichols (2, 6). The rer2 srt1 double deletion is lethal (2).

The RER2 human homolog (OMIM), called hCIT(7) or hds (8) complements its deletion in yeast.

Last updated: 2005-07-08 Contact SGD

References cited on this page View Complete Literature Guide for RER2
1) Nishikawa S and Nakano A  (1993) Identification of a gene required for membrane protein retention in the early secretory pathway. Proc Natl Acad Sci U S A 90(17):8179-83
2) Sato M, et al.  (1999) The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol Cell Biol 19(1):471-83
3) Currie E, et al.  (2014) High-Confidence Proteomic Analysis of Yeast Lipid Droplets Identifies Additional Droplet Proteins and Reveals Connections to Dolichol Synthesis and Sterol Acetylation. J Lipid Res ()
4) Grabinska K and Palamarczyk G  (2002) Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase. FEMS Yeast Res 2(3):259-65
5) Sato M, et al.  (2001) Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6(6):495-506
6) Schenk B, et al.  (2001) An alternative cis-isoprenyltransferase activity in yeast that produces polyisoprenols with chain lengths similar to mammalian dolichols. Glycobiology 11(1):89-98
7) Shridas P, et al.  (2003) Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells. Biochem Biophys Res Commun 312(4):1349-56
8) Endo S, et al.  (2003) Identification of human dehydrodolichyl diphosphate synthase gene. Biochim Biophys Acta 1625(3):291-5