DFG10_YEAST
ID DFG10_YEAST Reviewed; 253 AA.
AC P40526; D6VVN2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Polyprenol reductase;
DE EC=1.3.1.94;
DE AltName: Full=Protein DFG10;
GN Name=DFG10; OrderedLocusNames=YIL049W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
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 [3]
RP GENE NAME, AND DISRUPTION PHENOTYPE.
RX PubMed=9055077; DOI=10.1093/genetics/145.3.671;
RA Moesch H.-U., Fink G.R.;
RT "Dissection of filamentous growth by transposon mutagenesis in
RT Saccharomyces cerevisiae.";
RL Genetics 145:671-684(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20637498; DOI=10.1016/j.cell.2010.06.001;
RA Cantagrel V., Lefeber D.J., Ng B.G., Guan Z., Silhavy J.L., Bielas S.L.,
RA Lehle L., Hombauer H., Adamowicz M., Swiezewska E., De Brouwer A.P.,
RA Blumel P., Sykut-Cegielska J., Houliston S., Swistun D., Ali B.R.,
RA Dobyns W.B., Babovic-Vuksanovic D., van Bokhoven H., Wevers R.A.,
RA Raetz C.R., Freeze H.H., Morava E., Al-Gazali L., Gleeson J.G.;
RT "SRD5A3 is required for converting polyprenol to dolichol and is mutated in
RT a congenital glycosylation disorder.";
RL Cell 142:203-217(2010).
CC -!- FUNCTION: Plays a key role in early steps of protein N-linked
CC glycosylation by being required for the conversion of polyprenol into
CC dolichol. Dolichols are required for the synthesis of dolichol-linked
CC monosaccharides and the oligosaccharide precursor used for N-
CC glycosylation. Acts as a polyprenol reductase that promotes the
CC reduction of the alpha-isoprene unit of polyprenols into dolichols in a
CC NADP-dependent mechanism. {ECO:0000269|PubMed:20637498}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol
CC + H(+) + NADPH; Xref=Rhea:RHEA:34279, Rhea:RHEA-COMP:9521, Rhea:RHEA-
CC COMP:9525, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:67132; EC=1.3.1.94;
CC Evidence={ECO:0000269|PubMed:20637498};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Suppression of filamentatous growth, defects in
CC cell polarity, and cellular elongation, due to defects in N-
CC glycosylation. {ECO:0000269|PubMed:20637498,
CC ECO:0000269|PubMed:9055077}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; Z38060; CAA86173.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08498.1; -; Genomic_DNA.
DR PIR; S48430; S48430.
DR RefSeq; NP_012215.1; NM_001179399.1.
DR AlphaFoldDB; P40526; -.
DR SMR; P40526; -.
DR BioGRID; 34941; 112.
DR DIP; DIP-4658N; -.
DR STRING; 4932.YIL049W; -.
DR MaxQB; P40526; -.
DR PaxDb; P40526; -.
DR EnsemblFungi; YIL049W_mRNA; YIL049W; YIL049W.
DR GeneID; 854762; -.
DR KEGG; sce:YIL049W; -.
DR SGD; S000001311; DFG10.
DR VEuPathDB; FungiDB:YIL049W; -.
DR eggNOG; KOG1640; Eukaryota.
DR GeneTree; ENSGT00500000044920; -.
DR HOGENOM; CLU_044409_0_0_1; -.
DR InParanoid; P40526; -.
DR OMA; SSPHMFF; -.
DR BioCyc; MetaCyc:G3O-31320-MON; -.
DR BioCyc; YEAST:G3O-31320-MON; -.
DR Reactome; R-SCE-193048; Androgen biosynthesis.
DR Reactome; R-SCE-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:P40526; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40526; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:SGD.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019408; P:dolichol biosynthetic process; IMP:SGD.
DR GO; GO:0019348; P:dolichol metabolic process; IMP:UniProtKB.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0016095; P:polyprenol catabolic process; IMP:UniProtKB.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039698; Dfg10/SRD5A3.
DR PANTHER; PTHR14624; PTHR14624; 2.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..253
FT /note="Polyprenol reductase"
FT /id="PRO_0000213682"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 253 AA; 30306 MW; FBADD31A3BC5B054 CRC64;
MYFDEEQLLK YTIYAYRLSF FVGICSLFIA KSCLPEFLQY GKTYRPKENS KYSSILERIK
KFTVPKAYFS HFYYLATFLS LVTLYFYPKF PIVWIIFGHS LRRLYETLYV LHYTSNSRMN
WSHYLVGIWF YSVLLLILNI SLYKNSIPNT LNMNAFIIFC IASWDQYKNH VILANLVKYS
LPTGRLFRLV CCPHYLDEII IYSTLLPYEQ EFYLTLVWVI TSLTISALET KNYYRHKFKD
NHVAPYAIIP FII
