ID A0A453CL48_AEGTS Unreviewed; 347 AA.
AC A0A453CL48;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE RecName: Full=Polyprenol reductase {ECO:0000256|RuleBase:RU367081};
DE EC=1.3.1.94 {ECO:0000256|RuleBase:RU367081};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20886100.8, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET2Gv20886100.8}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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. {ECO:0000256|RuleBase:RU367081}.
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:0000256|ARBA:ARBA00000394,
CC ECO:0000256|RuleBase:RU367081};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367081}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367081}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC reductase subfamily. {ECO:0000256|RuleBase:RU367081}.
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 AlphaFoldDB; A0A453CL48; -.
DR STRING; 200361.A0A453CL48; -.
DR EnsemblPlants; AET2Gv20886100.8; AET2Gv20886100.8; AET2Gv20886100.
DR Gramene; AET2Gv20886100.8; AET2Gv20886100.8; AET2Gv20886100.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000015105; Chromosome 2D.
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:UniProtKB-UniRule.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016095; P:polyprenol catabolic process; IEA:UniProtKB-UniRule.
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 {ECO:0000256|RuleBase:RU367081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367081};
KW NADP {ECO:0000256|RuleBase:RU367081};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367081};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367081}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..347
FT /note="Polyprenol reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018970687"
FT TRANSMEM 70..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 285..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT DOMAIN 239..322
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 347 AA; 39092 MW; D8D0EA33E0CA47C6 CRC64;
MEKGDGPALQ LLLCLAWLAA TLPILAAALP IPAAAGGRLL HSLLSAFSSR GKTVRRSGNN
SWKFTVPQKY FLHFYVVGVA VTTSLLLAIC FYAYMKMTPL LPEPSSYSTI ASHLIGSNSF
SFGSVLSRTM EHKYRVWRTV FVLLLMEIQV LRRLYETENV FHYSPSARMH IVGYLTGLFY
YTAAPLSLAS SCLPEAIDFI RGQIVEFIVK GRARMPDLVI DSPSLLKPLL KLGWCQWIGA
IVFIWGSLHQ IRCHAILGSL RENKDSDEYV IPCGDWFSRV SCPHYLAELV IYLGMLIASG
GSDISVWFLF IFVITNLSFA AVQTHRWYLQ KFEDYPRSRY AIIPFVL
//
