ID   POED2_ORYSJ             Reviewed;         353 AA.
AC   Q7F0Q2; A0A0P0X626;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Polyprenol reductase 2;
DE            EC=1.3.1.94;
GN   OrderedLocusNames=Os07g0493400, LOC_Os07g31140;
GN   ORFNames=OsJ_24314, P0038F10.126;
OS   Oryza sativa subsp. japonica (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=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare; TISSUE=Callus;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (OCT-2006) 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 (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; AP004266; BAC83358.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT01576.1; -; Genomic_DNA.
DR   EMBL; CM000144; EAZ39875.1; -; Genomic_DNA.
DR   EMBL; AK241048; BAH00939.1; -; mRNA.
DR   RefSeq; XP_015646164.1; XM_015790678.1.
DR   AlphaFoldDB; Q7F0Q2; -.
DR   SMR; Q7F0Q2; -.
DR   STRING; 39947.Q7F0Q2; -.
DR   PaxDb; 39947-Q7F0Q2; -.
DR   EnsemblPlants; Os07t0493400-01; Os07t0493400-01; Os07g0493400.
DR   GeneID; 4343281; -.
DR   Gramene; Os07t0493400-01; Os07t0493400-01; Os07g0493400.
DR   KEGG; osa:4343281; -.
DR   eggNOG; KOG1640; Eukaryota.
DR   HOGENOM; CLU_044409_1_0_1; -.
DR   InParanoid; Q7F0Q2; -.
DR   OMA; FEICIYL; -.
DR   OrthoDB; 2896758at2759; -.
DR   PlantReactome; R-OSA-1119456; Brassinosteroid biosynthesis II.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019408; P:dolichol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016095; P:polyprenol catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..353
FT                   /note="Polyprenol reductase 2"
FT                   /id="PRO_0000398659"
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;  39935 MW;  08E6F432E2DCE6C0 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 DYDEYVIPCG DCFNRVSCPH YLAELVIYFG
     MLVASGAEDI PVWFLFIFVI TNLSFAAVET YNWYLQKFED YPRSRYAIIP FVC
//