ID Q0U8M2_PHANO Unreviewed; 329 AA.
AC Q0U8M2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Polyprenol reductase {ECO:0000256|RuleBase:RU367081};
DE EC=1.3.1.94 {ECO:0000256|RuleBase:RU367081};
GN ORFNames=SNOG_11892 {ECO:0000313|EMBL:EAT80936.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80936.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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:0000256|RuleBase:RU367081}.
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:0000256|RuleBase:RU367081};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367081}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367081}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC reductase subfamily. {ECO:0000256|RuleBase:RU367081}.
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DR EMBL; CH445344; EAT80936.2; -; Genomic_DNA.
DR RefSeq; XP_001802128.1; XM_001802076.1.
DR AlphaFoldDB; Q0U8M2; -.
DR STRING; 321614.Q0U8M2; -.
DR EnsemblFungi; SNOT_11892; SNOT_11892; SNOG_11892.
DR GeneID; 5979036; -.
DR KEGG; pno:SNOG_11892; -.
DR VEuPathDB; FungiDB:JI435_118920; -.
DR eggNOG; KOG1640; Eukaryota.
DR HOGENOM; CLU_044409_0_1_1; -.
DR InParanoid; Q0U8M2; -.
DR OrthoDB; 2896758at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019408; P:dolichol biosynthetic process; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0016095; P:polyprenol catabolic process; IBA:GO_Central.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039698; Dfg10/SRD5A3.
DR PANTHER; PTHR14624; DFG10 PROTEIN; 1.
DR PANTHER; PTHR14624:SF0; POLYPRENOL REDUCTASE; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367081};
KW NADP {ECO:0000256|RuleBase:RU367081};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367081};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367081}.
FT TRANSMEM 58..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 129..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT DOMAIN 223..302
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 329 AA; 37438 MW; 3A91FFB33D1DBD05 CRC64;
MGQTLIRIIG ALRPHHFLVT VLCPPSASRS AHFSLITTMS RPAPPASSLE HPANTPAVLL
RVFYLAASLL ILAIQLVPAL RRRFLVYGSR TTPTGKSAPS EEPAQKTALD TLLDDFAAIQ
VPHNYFTHFY ITSVISSLFW GLWLRVWTTP GQLQVVWMLM LLQGVRRLLE SDAYTSKSKS
RMWFVHWLLG IAFYLAMNVS IWIEGAHQGP RHWSTTMLVP AVLTAHVFQH SFHAYLYRLR
SEKKGYQLPS HPIFTNLLCP HYTCEVLIYT FLSFLAAPDG RWVSWTMVCG TIFVASNLGV
TAWGTKEWYA EKFGQDKVGH RKRMVPWIW
//
