RER2_YEAST
ID RER2_YEAST Reviewed; 286 AA.
AC P35196; D6VQ03;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit RER2 {ECO:0000305};
DE Short=DEDOL-PP synthase {ECO:0000305};
DE EC=2.5.1.87 {ECO:0000269|PubMed:25066056, ECO:0000269|PubMed:9858571};
DE AltName: Full=Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) {ECO:0000305};
GN Name=RER2 {ECO:0000312|SGD:S000000206};
GN OrderedLocusNames=YBR002C {ECO:0000312|SGD:S000000206}; ORFNames=YBR0107;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP MUTAGENESIS OF GLY-164 AND SER-209.
RX PubMed=9858571; DOI=10.1128/mcb.19.1.471;
RA Sato M., Sato K., Nishikawa S., Hirata A., Kato J., Nakano A.;
RT "The yeast RER2 gene, identified by endoplasmic reticulum protein
RT localization mutations, encodes cis-prenyltransferase, a key enzyme in
RT dolichol synthesis.";
RL Mol. Cell. Biol. 19:471-483(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091860; DOI=10.1002/yea.320100006;
RA Wolfe K.H., Lohan A.J.E.;
RT "Sequence around the centromere of Saccharomyces cerevisiae chromosome II:
RT similarity of CEN2 to CEN4.";
RL Yeast 10:S41-S46(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11442630; DOI=10.1046/j.1365-2443.2001.00438.x;
RA Sato M., Fujisaki S., Sato K., Nishimura Y., Nakano A.;
RT "Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with
RT different properties and localizations. Implication for their distinct
RT physiological roles in dolichol synthesis.";
RL Genes Cells 6:495-506(2001).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=17345630; DOI=10.1002/bip.20715;
RA Poznanski J., Szkopinska A.;
RT "Precise bacterial polyprenol length control fails in Saccharomyces
RT cerevisiae.";
RL Biopolymers 86:155-164(2007).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX PubMed=25066056; DOI=10.1016/j.cmet.2014.06.016;
RA Park E.J., Grabinska K.A., Guan Z., Stranecky V., Hartmannova H.,
RA Hodanova K., Baresova V., Sovova J., Jozsef L., Ondruskova N.,
RA Hansikova H., Honzik T., Zeman J., Hulkova H., Wen R., Kmoch S.,
RA Sessa W.C.;
RT "Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a
RT congenital disorder of glycosylation.";
RL Cell Metab. 20:448-457(2014).
CC -!- FUNCTION: With NUS1, forms the dehydrodolichyl diphosphate synthase
CC (DDS) complex, an essential component of the dolichol monophosphate
CC (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl
CC pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce
CC dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which
CC is utilized as a sugar carrier in protein glycosylation in the
CC endoplasmic reticulum (ER). {ECO:0000269|PubMed:11442630,
CC ECO:0000269|PubMed:17345630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-
CC trans,poly-cis-polyprenyl diphosphate + n diphosphate;
CC Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763;
CC EC=2.5.1.87; Evidence={ECO:0000269|PubMed:25066056,
CC ECO:0000269|PubMed:9858571};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q86SQ9};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Forms an active dehydrodolichyl diphosphate synthase complex
CC with NUS1. {ECO:0000303|PubMed:25066056}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11442630}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11442630}.
CC -!- INDUCTION: Mainly expressed in the early logarithmic phase.
CC {ECO:0000269|PubMed:11442630}.
CC -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; AB013497; BAA36577.1; -; Genomic_DNA.
DR EMBL; Z26494; CAA81271.1; -; Genomic_DNA.
DR EMBL; Z35871; CAA84938.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07123.1; -; Genomic_DNA.
DR PIR; S44561; S44561.
DR RefSeq; NP_009556.1; NM_001178350.1.
DR AlphaFoldDB; P35196; -.
DR SMR; P35196; -.
DR BioGRID; 32703; 386.
DR ComplexPortal; CPX-162; Dehydrodolichyl diphosphate synthase complex variant RER2.
DR IntAct; P35196; 21.
DR MINT; P35196; -.
DR STRING; 4932.YBR002C; -.
DR iPTMnet; P35196; -.
DR MaxQB; P35196; -.
DR PaxDb; P35196; -.
DR PRIDE; P35196; -.
DR EnsemblFungi; YBR002C_mRNA; YBR002C; YBR002C.
DR GeneID; 852287; -.
DR KEGG; sce:YBR002C; -.
DR SGD; S000000206; RER2.
DR VEuPathDB; FungiDB:YBR002C; -.
DR eggNOG; KOG1602; Eukaryota.
DR GeneTree; ENSGT00390000007879; -.
DR HOGENOM; CLU_038505_0_0_1; -.
DR InParanoid; P35196; -.
DR OMA; PRTEGHK; -.
DR BioCyc; MetaCyc:YBR002C-MON; -.
DR BioCyc; YEAST:YBR002C-MON; -.
DR BRENDA; 2.5.1.87; 984.
DR Reactome; R-SCE-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:P35196; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P35196; protein.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IDA:SGD.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:SGD.
DR GO; GO:0019408; P:dolichol biosynthetic process; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IDA:SGD.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Magnesium; Membrane; Reference proteome;
KW Transferase.
FT CHAIN 1..286
FT /note="Dehydrodolichyl diphosphate synthase complex subunit
FT RER2"
FT /id="PRO_0000123759"
FT MUTAGEN 164
FT /note="G->D: In RER2-1; loss of activity."
FT MUTAGEN 209
FT /note="S->N: In RER2-2; loss of activity."
SQ SEQUENCE 286 AA; 32694 MW; 73F27FC9EED61F4E CRC64;
METDSGIPGH SFVLKWTKNI FSRTLRASNC VPRHVGFIMD GNRRFARKKE MDVKEGHEAG
FVSMSRILEL CYEAGVDTAT VFAFSIENFK RSSREVESLM TLARERIRQI TERGELACKY
GVRIKIIGDL SLLDKSLLED VRVAVETTKN NKRATLNICF PYTGREEILH AMKETIVQHK
KGAAIDESTL ESHLYTAGVP PLDLLIRTSG VSRLSDFLIW QASSKGVRIE LLDCLWPEFG
PIRMAWILLK FSFHKSFLNK EYRLEEGDYD EETNGDPIDL KEKKLN
