ID A0A194VLL9_9PEZI Unreviewed; 342 AA.
AC A0A194VLL9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE RecName: Full=Polyprenol reductase {ECO:0000256|RuleBase:RU367081};
DE EC=1.3.1.94 {ECO:0000256|RuleBase:RU367081};
GN ORFNames=VM1G_01115 {ECO:0000313|EMBL:KUI65054.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI65054.1};
RN [1] {ECO:0000313|EMBL:KUI65054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI65054.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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}.
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DR EMBL; CM003098; KUI65054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VLL9; -.
DR OrthoDB; 2896758at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000078559; Chromosome 1.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367081}.
FT TRANSMEM 109..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 228..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 266..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT DOMAIN 235..316
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 342 AA; 38453 MW; A22BF162A8351F6B CRC64;
MWYPPKVDYQ LIDVFTRKMG PWQEDAAELL LSVSPASWCQ TCFTLATCAV LAVAIAPTAE
RKLLVNYGAR AHDPTATAAA DAPAPEGGDD VFLQAVRRLT SLGQVPHSWF FTFYFVYIQC
ALFWAVQFIS GGSVLQFIAR QQVEHGTPAS INRNQVVITW CLMLFQAARR LYECWAFAKP
SKATMWFVHW LLGQFFYLGI SVAIWIEGSD VAVHNELLSS THEFTADALF KVAAALPMFV
FGWVSQYRCH KYLASLEKYS LPDLSMFRYL ICPHYTCECL IYLSLAIVAA PEGQWCNRTL
LSALVFVAVN LGVTAQGTRA WYIEKFGSEK VAGRNVLVPF LY
//
