ID   PPRD1_ORYSI             Reviewed;         354 AA.
AC   A2XWN6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=Polyprenal reductase 1 {ECO:0000305};
DE            EC=1.3.1.94 {ECO:0000250|UniProtKB:Q9H8P0};
GN   ORFNames=OsI_17065;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Plays a key role in early steps of protein N-linked
CC       glycosylation by being involved in the conversion of polyprenol into
CC       dolichol (By similarity). Acts as a polyprenal reductase that mediates
CC       the reduction of polyprenal into dolichal in a NADP-dependent mechanism
CC       (By similarity). Dolichols are required for the synthesis of dolichol-
CC       linked monosaccharides and the oligosaccharide precursor used for N-
CC       glycosylation (By similarity). {ECO:0000250|UniProtKB:Q9CAH5,
CC       ECO:0000250|UniProtKB:Q9H8P0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichal + NADP(+) = a di-trans,poly-cis-
CC         polyprenal + NADPH + H(+); Xref=Rhea:RHEA:80727, Rhea:RHEA-
CC         COMP:19536, Rhea:RHEA-COMP:19537, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:231623,
CC         ChEBI:CHEBI:231637; EC=1.3.1.94;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:80729;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9CAH5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9CAH5};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenal
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; CM000129; EAY95246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XWN6; -.
DR   SMR; A2XWN6; -.
DR   STRING; 39946.A2XWN6; -.
DR   EnsemblPlants; BGIOSGA016966-TA; BGIOSGA016966-PA; BGIOSGA016966.
DR   Gramene; BGIOSGA016966-TA; BGIOSGA016966-PA; BGIOSGA016966.
DR   HOGENOM; CLU_044409_1_0_1; -.
DR   OMA; RFYETNF; -.
DR   OrthoDB; 541710at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000007015; Chromosome 4.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:TreeGrafter.
DR   GO; GO:0160198; F:polyprenal reductase activity; ISS:UniProtKB.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0043048; P:dolichyl monophosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016095; P:polyprenol catabolic process; IEA:TreeGrafter.
DR   FunFam; 1.20.120.1630:FF:000012; Polyprenol reductase 1; 1.
DR   Gene3D; 1.20.120.1630; -; 1.
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   Cell membrane; Membrane; NADP; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..354
FT                   /note="Polyprenal reductase 1"
FT                   /id="PRO_0000398658"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  39867 MW;  A307F4A8CA15DD38 CRC64;
     METEGWPALQ PLLCLAWIAT TLPIIVAALP IPAAAGGHLL RRLLSAFSSR GKTVRPSPAS
     SSGSSSSKAK FTVPQKYFMH FYVVGVLATT ILLLAIWFYA YMKMTPLLPE SSSYSTIASH
     LVGSNSFSFG RVHSRTMGHK YHVWRTVFVL LLMEIQVLRR LYETEHVFHY SPSARMHIVG
     YLTGLFYYVA APLSLASSCI PEAAEYLQGQ VAEFIVKGRA RMPDLVIDSS SLLQPLLKLG
     WTQWIGAVIF IWGSLHQIRC HAILGTLREH KDSDEYVIPC GDWFNRVSCP HYLAELVIYF
     GMLVASGGED IPVWFLFVFV ITNLSFAAVE THKWYLQKFE DYPRSRYAII PFVC
//