ID A0A1Q5T0U3_9EURO Unreviewed; 321 AA.
AC A0A1Q5T0U3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JUN-2023, entry version 16.
DE RecName: Full=Polyprenol reductase {ECO:0000256|RuleBase:RU367081};
DE EC=1.3.1.94 {ECO:0000256|RuleBase:RU367081};
GN ORFNames=PENSUB_11984 {ECO:0000313|EMBL:OKO93705.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO93705.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO93705.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO93705.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367081}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKO93705.1}.
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DR EMBL; MNBE01000723; OKO93705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5T0U3; -.
DR STRING; 1316194.A0A1Q5T0U3; -.
DR OrthoDB; 2896758at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016095; P:polyprenol catabolic process; IEA:UniProtKB-UniRule.
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:UP000186955};
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 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT DOMAIN 217..268
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 321 AA; 35513 MW; 8B6C23FACEBC867B CRC64;
MDLLAHVDSA LEAAHMDAID ALRAFFLLAA ATAVSVSIPS ALRDRFVTYG PRATATGAEP
VAGSRPPAQA SSSGLLDYLA TWQVPHSYFI QFYIASVASS VFWAVQLCWR GRVFEAIASR
VSEEHLQQSM SLTQVLICWI LLAIQGSRRL WECIIFAKPS SSKMSFAHWV LGMGFYLAAG
IAIWIEGSGA ILSRSLTLAD FQFTNAPTAR TFICVPLFLI ASGLQHDCHH FLFSLKKYTL
PDHPIFRGIV CPHYGAECLI YLSLTYLAAP PGQVVNKTML SCLALVAVNL GLTAHNTKKW
YMQKFGREAV QDRWLMIPYI Y
//
