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Database: UniProt
Entry: A0A3M9Y8Z7_9PEZI
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ID   A0A3M9Y8Z7_9PEZI        Unreviewed;       332 AA.
AC   A0A3M9Y8Z7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   28-JUN-2023, entry version 13.
DE   RecName: Full=Polyprenol reductase {ECO:0000256|RuleBase:RU367081};
DE            EC=1.3.1.94 {ECO:0000256|RuleBase:RU367081};
GN   ORFNames=D7B24_006595 {ECO:0000313|EMBL:RNJ56949.1};
OS   Verticillium nonalfalfae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ56949.1, ECO:0000313|Proteomes:UP000267145};
RN   [1] {ECO:0000313|EMBL:RNJ56949.1, ECO:0000313|Proteomes:UP000267145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ56949.1,
RC   ECO:0000313|Proteomes:UP000267145};
RA   Stajich J.E., Kasson M.T.;
RT   "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL   Submitted (OCT-2018) 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:RNJ56949.1}.
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DR   EMBL; RBVV01000048; RNJ56949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9Y8Z7; -.
DR   STRING; 1051616.A0A3M9Y8Z7; -.
DR   OrthoDB; 2896758at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000267145; 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367081}.
FT   TRANSMEM        167..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   DOMAIN          225..306
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   332 AA;  36994 MW;  90767B19F4E38948 CRC64;
     MALPAPLLEI IACAMTDTAP SKWCQAFFAI ATITALSVQL IPKASQSLLL DYGPRATQAK
     YGAPGDQAGW LYTSVRLVTA VQVPHSWFTH FYVASVAASA FWAYQYFAGR SLLLAIITKQ
     AAVEGPSMGK EQVWLVWILM ALQGGRRLFE CFYVMKPSRS KMWLGHWALG LIYYLDMSVA
     IWIEGSRMFH RMAPRLATNH AAGSLLHSEA DTAVSSGFST SQLVGIAIFT TGWLQQHKCH
     QYLASLKKYT LPEEGLFRHI VCAHYTCECL LYSGLAMAAA PAGRWFNRTL ICGLWFVIVN
     LGSTAHGTKK WYSEKFGEAK VEPKWKMIPF VF
//
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