POED2_ARATH
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 03-AUG-2022, entry version 117.
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.AT2G16530.1; -.
DR iPTMnet; Q9SI62; -.
DR PaxDb; Q9SI62; -.
DR PRIDE; Q9SI62; -.
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; locus:2045126; AT2G16530.
DR eggNOG; KOG1640; Eukaryota.
DR HOGENOM; CLU_044409_1_0_1; -.
DR InParanoid; Q9SI62; -.
DR OMA; KRWFRHF; -.
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 Genevisible; Q9SI62; AT.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; PTHR14624; 2.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
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
