SRT1_YEAST
ID SRT1_YEAST Reviewed; 343 AA.
AC Q03175; D6VZS4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit SRT1 {ECO:0000305};
DE EC=2.5.1.87 {ECO:0000303|PubMed:25066056};
DE AltName: Full=Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) {ECO:0000305};
GN Name=SRT1 {ECO:0000312|SGD:S000004707};
GN OrderedLocusNames=YMR101C {ECO:0000312|SGD:S000004707};
GN ORFNames=YM6543.08C;
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], AND PRELIMINARY CHARACTERIZATION.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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, ECO:0000269|PubMed:25066056}.
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:0000303|PubMed:25066056};
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: Lipid droplet {ECO:0000269|PubMed:11442630}.
CC -!- INDUCTION: Expression is induced in the stationary phase.
CC {ECO:0000269|PubMed:11442630}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; AB013498; BAA36578.1; -; Genomic_DNA.
DR EMBL; Z49807; CAA89902.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09998.1; -; Genomic_DNA.
DR PIR; S55087; S55087.
DR RefSeq; NP_013819.1; NM_001182601.1.
DR AlphaFoldDB; Q03175; -.
DR SMR; Q03175; -.
DR BioGRID; 35277; 65.
DR ComplexPortal; CPX-166; Dehydrodolichyl diphosphate synthase complex variant SRT1.
DR DIP; DIP-4439N; -.
DR IntAct; Q03175; 1.
DR STRING; 4932.YMR101C; -.
DR PaxDb; Q03175; -.
DR PRIDE; Q03175; -.
DR EnsemblFungi; YMR101C_mRNA; YMR101C; YMR101C.
DR GeneID; 855127; -.
DR KEGG; sce:YMR101C; -.
DR SGD; S000004707; SRT1.
DR VEuPathDB; FungiDB:YMR101C; -.
DR eggNOG; KOG1602; Eukaryota.
DR GeneTree; ENSGT00390000007879; -.
DR HOGENOM; CLU_038505_0_0_1; -.
DR InParanoid; Q03175; -.
DR OMA; TKGQPDP; -.
DR BioCyc; MetaCyc:YMR101C-MON; -.
DR BioCyc; YEAST:YMR101C-MON; -.
DR BRENDA; 2.5.1.87; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q03175; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03175; protein.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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: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 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 Lipid droplet; Magnesium; Reference proteome; Transferase.
FT CHAIN 1..343
FT /note="Dehydrodolichyl diphosphate synthase complex subunit
FT SRT1"
FT /id="PRO_0000123760"
SQ SEQUENCE 343 AA; 40200 MW; 6B9E925663597AF0 CRC64;
MKMPSIIQIQ FVALKRLLVE TKEQMCFAVK SIFQRVFAWV MSLSLFSWFY VNLQNILIKA
LRVGPVPEHV SFIMDGNRRY AKSRRLPVKK GHEAGGLTLL TLLYICKRLG VKCVSAYAFS
IENFNRPKEE VDTLMNLFTV KLDEFAKRAK DYKDPLYGSK IRIVGDQSLL SPEMRKKIKK
VEEITQDGDD FTLFICFPYT SRNDMLHTIR DSVEDHLENK SPRINIRKFT NKMYMGFHSN
KCELLIRTSG HRRLSDYMLW QVHENATIEF SDTLWPNFSF FAMYLMILKW SFFSTIQKYN
EKNHSLFEKI HESVPSIFKK KKTAMSLYNF PNPPISVSVT GDE
