POED1_ARATH
ID POED1_ARATH Reviewed; 320 AA.
AC Q9CAH5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Polyprenol reductase 1 {ECO:0000303|PubMed:26628744};
DE EC=1.3.1.94 {ECO:0000269|PubMed:26628744};
GN Name=PPRD1 {ECO:0000303|PubMed:26628744};
GN OrderedLocusNames=At1g72590 {ECO:0000312|Araport:AT1G72590};
GN ORFNames=F28P22.22 {ECO:0000312|EMBL:AAG51854.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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: Cell membrane {ECO:0000269|PubMed:26628744};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {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; AC010926; AAG51854.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35345.1; -; Genomic_DNA.
DR PIR; D96750; D96750.
DR RefSeq; NP_177403.1; NM_105918.3.
DR AlphaFoldDB; Q9CAH5; -.
DR SMR; Q9CAH5; -.
DR STRING; 3702.AT1G72590.1; -.
DR PaxDb; Q9CAH5; -.
DR PRIDE; Q9CAH5; -.
DR ProteomicsDB; 226287; -.
DR EnsemblPlants; AT1G72590.1; AT1G72590.1; AT1G72590.
DR GeneID; 843591; -.
DR Gramene; AT1G72590.1; AT1G72590.1; AT1G72590.
DR KEGG; ath:AT1G72590; -.
DR Araport; AT1G72590; -.
DR TAIR; locus:2030235; AT1G72590.
DR eggNOG; KOG1640; Eukaryota.
DR HOGENOM; CLU_044409_1_0_1; -.
DR InParanoid; Q9CAH5; -.
DR OMA; WSLHGKN; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; Q9CAH5; -.
DR BRENDA; 1.3.1.B13; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9CAH5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAH5; baseline and differential.
DR Genevisible; Q9CAH5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IGI:TAIR.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IDA:CACAO.
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:0016093; P:polyprenol metabolic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="Polyprenol reductase 1"
FT /id="PRO_0000398655"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 320 AA; 36313 MW; 326E51CF4A5719E5 CRC64;
MEVEIVWLVK AAWITVWIVS ILPLVIASIP SSKLNSFREL VLSFAGRGKI LHPSSQKFTV
PQKFFGHFYV VGVVWTTLLL AATWMYACKM AGGSHVFSFH MTHVEHRFKV GRAVFLLLLM
EIHVLRRVIE SFYVFKYSTS ARMHILAYVG ALFYYVAAPL SLCSNIAPEV ARFVGSQVAE
FIASGKSHSH DFNLLLSISP LMKLGSLQWI GGAIFLWGWI HQRRCHAILG SLREYPSQAK
EYIIPYGDWF EMVSCPHFLA EIVLYLGLLI SSGGTDISIW LLFGFVAANL TYAAGETHRW
YLQKFENYPA SRHAIFPHVY
