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Protein

Dehydrodolichyl diphosphate synthase complex subunit RER2

Gene

RER2

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

With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precusrosor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).2 Publications

Catalytic activityi

(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).2 Publications

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • dehydrodolichyl diphosphate synthase activity Source: SGD
  • prenyltransferase activity Source: SGD

GO - Biological processi

  • dolichol biosynthetic process Source: SGD
  • ER to Golgi vesicle-mediated transport Source: SGD
  • protein glycosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14490.
YEAST:YBR002C-MONOMER.
BRENDAi2.5.1.87. 984.
ReactomeiR-SCE-446199. Synthesis of Dolichyl-phosphate.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrodolichyl diphosphate synthase complex subunit RER2Curated (EC:2.5.1.872 Publications)
Short name:
DEDOL-PP synthaseCurated
Alternative name(s):
Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)Curated
Gene namesi
Name:RER2Imported
Ordered Locus Names:YBR002CImported
ORF Names:YBR0107
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR002C.
SGDiS000000206. RER2.

Subcellular locationi

GO - Cellular componenti

  • dehydrodolichyl diphosphate synthase complex Source: SGD
  • endoplasmic reticulum Source: SGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • lipid particle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi164 – 1641G → D in RER2-1; loss of activity.
Mutagenesisi209 – 2091S → N in RER2-2; loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286Dehydrodolichyl diphosphate synthase complex subunit RER2PRO_0000123759Add
BLAST

Proteomic databases

MaxQBiP35196.

Expressioni

Inductioni

Mainly expressed in the early logarithmic phase.1 Publication

Interactioni

Subunit structurei

Forms an active dehydrodolichyl diphosphate synthase complex with NUS1.1 Publication

Protein-protein interaction databases

BioGridi32703. 23 interactions.
IntActiP35196. 21 interactions.
MINTiMINT-4476587.

Structurei

3D structure databases

ProteinModelPortaliP35196.
SMRiP35196. Positions 28-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000007879.
HOGENOMiHOG000006053.
InParanoidiP35196.
KOiK11778.
OMAiDESTHIF.
OrthoDBiEOG73BVQX.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35196-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METDSGIPGH SFVLKWTKNI FSRTLRASNC VPRHVGFIMD GNRRFARKKE
60 70 80 90 100
MDVKEGHEAG FVSMSRILEL CYEAGVDTAT VFAFSIENFK RSSREVESLM
110 120 130 140 150
TLARERIRQI TERGELACKY GVRIKIIGDL SLLDKSLLED VRVAVETTKN
160 170 180 190 200
NKRATLNICF PYTGREEILH AMKETIVQHK KGAAIDESTL ESHLYTAGVP
210 220 230 240 250
PLDLLIRTSG VSRLSDFLIW QASSKGVRIE LLDCLWPEFG PIRMAWILLK
260 270 280
FSFHKSFLNK EYRLEEGDYD EETNGDPIDL KEKKLN
Length:286
Mass (Da):32,694
Last modified:February 1, 1994 - v1
Checksum:i73F27FC9EED61F4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013497 Genomic DNA. Translation: BAA36577.1.
Z26494 Genomic DNA. Translation: CAA81271.1.
Z35871 Genomic DNA. Translation: CAA84938.1.
BK006936 Genomic DNA. Translation: DAA07123.1.
PIRiS44561.
RefSeqiNP_009556.1. NM_001178350.1.

Genome annotation databases

EnsemblFungiiYBR002C; YBR002C; YBR002C.
GeneIDi852287.
KEGGisce:YBR002C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013497 Genomic DNA. Translation: BAA36577.1.
Z26494 Genomic DNA. Translation: CAA81271.1.
Z35871 Genomic DNA. Translation: CAA84938.1.
BK006936 Genomic DNA. Translation: DAA07123.1.
PIRiS44561.
RefSeqiNP_009556.1. NM_001178350.1.

3D structure databases

ProteinModelPortaliP35196.
SMRiP35196. Positions 28-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32703. 23 interactions.
IntActiP35196. 21 interactions.
MINTiMINT-4476587.

Proteomic databases

MaxQBiP35196.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR002C; YBR002C; YBR002C.
GeneIDi852287.
KEGGisce:YBR002C.

Organism-specific databases

EuPathDBiFungiDB:YBR002C.
SGDiS000000206. RER2.

Phylogenomic databases

GeneTreeiENSGT00390000007879.
HOGENOMiHOG000006053.
InParanoidiP35196.
KOiK11778.
OMAiDESTHIF.
OrthoDBiEOG73BVQX.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:MONOMER-14490.
YEAST:YBR002C-MONOMER.
BRENDAi2.5.1.87. 984.
ReactomeiR-SCE-446199. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

PROiP35196.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT.
InterProiIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERiPTHR10291. PTHR10291. 1 hit.
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
TIGRFAMsiTIGR00055. uppS. 1 hit.
PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis."
    Sato M., Sato K., Nishikawa S., Hirata A., Kato J., Nakano A.
    Mol. Cell. Biol. 19:471-483(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF GLY-164 AND SER-209.
  2. "Sequence around the centromere of Saccharomyces cerevisiae chromosome II: similarity of CEN2 to CEN4."
    Wolfe K.H., Lohan A.J.E.
    Yeast 10:S41-S46(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis."
    Sato M., Fujisaki S., Sato K., Nishimura Y., Nakano A.
    Genes Cells 6:495-506(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae."
    Poznanski J., Szkopinska A.
    Biopolymers 86:155-164(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation."
    Park E.J., Grabinska K.A., Guan Z., Stranecky V., Hartmannova H., Hodanova K., Baresova V., Sovova J., Jozsef L., Ondruskova N., Hansikova H., Honzik T., Zeman J., Hulkova H., Wen R., Kmoch S., Sessa W.C.
    Cell Metab. 20:448-457(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiRER2_YEAST
AccessioniPrimary (citable) accession number: P35196
Secondary accession number(s): D6VQ03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 8, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8970 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.