ID   POED2_ORYSI             Reviewed;         353 AA.
AC   B8B6G5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Polyprenol reductase 2;
DE            EC=1.3.1.94;
GN   ORFNames=OsI_26070;
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 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 (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC       reductase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEC82076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EEC82076.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CM000132; EEC82076.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; B8B6G5; -.
DR   SMR; B8B6G5; -.
DR   STRING; 39946.B8B6G5; -.
DR   HOGENOM; CLU_044409_1_0_1; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000007015; Chromosome 7.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR   InterPro; IPR039698; Dfg10/SRD5A3.
DR   PANTHER; PTHR14624; PTHR14624; 1.
DR   Pfam; PF02544; Steroid_dh; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..353
FT                   /note="Polyprenol reductase 2"
FT                   /id="PRO_0000398660"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  39903 MW;  08FAD5C4D509AFA0 CRC64;
     MESEGWPALQ PLLCFAWIAA TLPIIAAALP IPTAVGGHLL RRLLSAFSSR GKTVRPSPAS
     SSGSSSSKAK FTVPQKYFMH FYVVGVLATT ILLLAIWFYA YMKLTPLLLE SSSYSTIFSH
     LVGSNSFSFG RVRSRTMGHK YRVWRTVFAL LLMEVQVLRR LYETEHVFHY SPARMHIVGY
     LTGLFYYVAA PLSLASSCIP EAAEYFQGQV PEFVVKGRAR MPDLVIDSSS LLQPLLKLGW
     TQWIGAVIFI WGSLHQIRCH AILGSLREHK DSDEYVIPCS DCFNRVSCPH YLAELVIYFG
     MLVASGAEDI PVWFLFIFLI TNLSFAAVET YNWYLQKFED YPRSRYAIIP FVC