ID   POED2_ARATH             Reviewed;         343 AA.
AC   Q9SI62; Q3EBZ6; Q941B4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Polyprenol reductase 2 {ECO:0000303|PubMed:26628744};
DE            EC=1.3.1.94 {ECO:0000269|PubMed:26628744};
GN   Name=PPRD2 {ECO:0000303|PubMed:26628744};
GN   OrderedLocusNames=At2g16530 {ECO:0000312|Araport:AT2G16530};
GN   ORFNames=F1P15.9 {ECO:0000312|EMBL:AAD26491.2};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=26628744; DOI=10.1105/tpc.15.00463;
RA   Jozwiak A., Gutkowska M., Gawarecka K., Surmacz L., Buczkowska A.,
RA   Lichocka M., Nowakowska J., Swiezewska E.;
RT   "POLYPRENOL REDUCTASE2 deficiency is lethal in Arabidopsis due to male
RT   sterility.";
RL   Plant Cell 27:3336-3353(2015).
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. Involved in the regulation of plant growth
CC       and reproductive processes. {ECO:0000269|PubMed:26628744}.
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:0000269|PubMed:26628744};
CC   -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:26628744}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SI62-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SI62-2; Sequence=VSP_039793;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC       {ECO:0000269|PubMed:26628744}.
CC   -!- DISRUPTION PHENOTYPE: Male sterility, when homozygous. Deformed and
CC       non-viable pollen grains. {ECO:0000269|PubMed:26628744}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; AC007195; AAD26491.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06507.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06508.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM63071.1; -; Genomic_DNA.
DR   EMBL; AY052296; AAK96489.1; -; mRNA.
DR   EMBL; BT002716; AAO11632.1; -; mRNA.
DR   EMBL; BX819600; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; D84541; D84541.
DR   RefSeq; NP_001325183.1; NM_001335479.1. [Q9SI62-1]
DR   RefSeq; NP_565389.1; NM_127207.4. [Q9SI62-1]
DR   RefSeq; NP_973474.1; NM_201745.2. [Q9SI62-2]
DR   AlphaFoldDB; Q9SI62; -.
DR   SMR; Q9SI62; -.
DR   BioGRID; 1510; 1.
DR   IntAct; Q9SI62; 1.
DR   STRING; 3702.Q9SI62; -.
DR   iPTMnet; Q9SI62; -.
DR   PaxDb; 3702-AT2G16530-1; -.
DR   EnsemblPlants; AT2G16530.1; AT2G16530.1; AT2G16530. [Q9SI62-1]
DR   EnsemblPlants; AT2G16530.2; AT2G16530.2; AT2G16530. [Q9SI62-2]
DR   EnsemblPlants; AT2G16530.4; AT2G16530.4; AT2G16530. [Q9SI62-1]
DR   GeneID; 816152; -.
DR   Gramene; AT2G16530.1; AT2G16530.1; AT2G16530. [Q9SI62-1]
DR   Gramene; AT2G16530.2; AT2G16530.2; AT2G16530. [Q9SI62-2]
DR   Gramene; AT2G16530.4; AT2G16530.4; AT2G16530. [Q9SI62-1]
DR   KEGG; ath:AT2G16530; -.
DR   Araport; AT2G16530; -.
DR   TAIR; AT2G16530; PPRD2.
DR   eggNOG; KOG1640; Eukaryota.
DR   HOGENOM; CLU_044409_1_0_1; -.
DR   InParanoid; Q9SI62; -.
DR   OMA; FEICIYL; -.
DR   PhylomeDB; Q9SI62; -.
DR   BRENDA; 1.3.1.B13; 399.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q9SI62; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SI62; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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   GO; GO:0006487; P:protein N-linked glycosylation; IMP:TAIR.
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.
DR   Genevisible; Q9SI62; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Membrane; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..343
FT                   /note="Polyprenol reductase 2"
FT                   /id="PRO_0000398656"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         58
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_039793"
FT   CONFLICT        66
FT                   /note="F -> L (in Ref. 4; BX819600)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="F -> L (in Ref. 3; AAK96489/AAO11632)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  38678 MW;  49AB19FF40A9FA06 CRC64;
     MVELEIVWLV RGAWITVWIV SILPLVIASI PTSKLNSFRE LVLSFAGRGK ILHPSSQKFT
     IPQKCFAHFY VIGVVWTTLL LAATWMYACK MAPLSSEEFQ LSDIASRLAG GSDVFSVHKS
     NMTPVEHRFK VWRAVFLLLL MEIHVLRRLI ESFYVFKYSP SARMHILGYF AGLFFYVTAP
     LSLCSNIAPE VAGFVGNQVA EFIANGKSHT SAPEFNLLSS ISPLMKLGSL QWIGGAIFLW
     GWIHQRRCHA ILGSLRENPS QAKEYIIPYG DWFGMVSSPH FLAEIVLYAG LLIASGGTDI
     TIWLLFGFVA ANLTYAAGET HRWYLRKFEN YPANRHAIFP YVY
//