ID POED1_ORYSI Reviewed; 354 AA. AC A2XWN6; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Polyprenol reductase 1; DE EC=1.3.1.94; 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 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; HMFFEVV; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000007015; Chromosome 4. 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: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 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 Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..354 FT /note="Polyprenol 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 //