PORED_DROME
ID PORED_DROME Reviewed; 326 AA.
AC Q9VLP9; A0ANR0; A0ANR1; A0ANR2; A0ANR3; A0ANR5; Q8MR21;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Polyprenol reductase;
DE EC=1.3.1.94;
GN ORFNames=CG7840;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229,
RC ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL84, and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17,
RC MEL18, MEL19, and MEL20;
RX PubMed=19126864; DOI=10.1093/molbev/msn297;
RA Parsch J., Zhang Z., Baines J.F.;
RT "The influence of demography and weak selection on the McDonald-Kreitman
RT test: an empirical study in Drosophila.";
RL Mol. Biol. Evol. 26:691-698(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM52687.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AM294298; CAL26216.1; -; Genomic_DNA.
DR EMBL; AM294299; CAL26217.1; -; Genomic_DNA.
DR EMBL; AM294300; CAL26218.1; -; Genomic_DNA.
DR EMBL; AM294301; CAL26219.1; -; Genomic_DNA.
DR EMBL; AM294302; CAL26220.1; -; Genomic_DNA.
DR EMBL; AM294303; CAL26221.1; -; Genomic_DNA.
DR EMBL; AM294304; CAL26230.1; -; Genomic_DNA.
DR EMBL; AM294305; CAL26235.1; -; Genomic_DNA.
DR EMBL; AM294306; CAL26236.1; -; Genomic_DNA.
DR EMBL; AM294307; CAL26237.1; -; Genomic_DNA.
DR EMBL; AM294308; CAL26238.1; -; Genomic_DNA.
DR EMBL; FM245364; CAR93290.1; -; Genomic_DNA.
DR EMBL; FM245365; CAR93291.1; -; Genomic_DNA.
DR EMBL; FM245366; CAR93292.1; -; Genomic_DNA.
DR EMBL; FM245367; CAR93293.1; -; Genomic_DNA.
DR EMBL; FM245368; CAR93294.1; -; Genomic_DNA.
DR EMBL; FM245369; CAR93295.1; -; Genomic_DNA.
DR EMBL; FM245370; CAR93296.1; -; Genomic_DNA.
DR EMBL; FM245371; CAR93297.1; -; Genomic_DNA.
DR EMBL; FM245372; CAR93298.1; -; Genomic_DNA.
DR EMBL; FM245373; CAR93299.1; -; Genomic_DNA.
DR EMBL; FM245374; CAR93300.1; -; Genomic_DNA.
DR EMBL; FM245375; CAR93301.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52635.1; -; Genomic_DNA.
DR EMBL; AY122175; AAM52687.1; ALT_INIT; mRNA.
DR RefSeq; NP_609203.1; NM_135359.3.
DR AlphaFoldDB; Q9VLP9; -.
DR BioGRID; 60262; 1.
DR IntAct; Q9VLP9; 2.
DR STRING; 7227.FBpp0079218; -.
DR PaxDb; Q9VLP9; -.
DR PRIDE; Q9VLP9; -.
DR DNASU; 34136; -.
DR EnsemblMetazoa; FBtr0079598; FBpp0079218; FBgn0032014.
DR GeneID; 34136; -.
DR KEGG; dme:Dmel_CG7840; -.
DR UCSC; CG7840-RA; d. melanogaster.
DR FlyBase; FBgn0032014; CG7840.
DR VEuPathDB; VectorBase:FBgn0032014; -.
DR eggNOG; KOG1640; Eukaryota.
DR GeneTree; ENSGT00500000044920; -.
DR HOGENOM; CLU_044409_2_0_1; -.
DR InParanoid; Q9VLP9; -.
DR OMA; SSPHMFF; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; Q9VLP9; -.
DR Reactome; R-DME-193048; Androgen biosynthesis.
DR Reactome; R-DME-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 34136; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34136; -.
DR PRO; PR:Q9VLP9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032014; Expressed in cleaving embryo and 25 other tissues.
DR Genevisible; Q9VLP9; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; ISS:FlyBase.
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:0019348; P:dolichol metabolic process; ISS:UniProtKB.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016095; P:polyprenol catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Polyprenol reductase"
FT /id="PRO_0000398654"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 9
FT /note="L -> P (in strain: ZBMEL95 and ZBMEL157)"
FT VARIANT 96
FT /note="A -> V (in strain: MEL11, ZBMEL145, ZBMEL131,
FT ZBMEL229 and ZBMEL384)"
FT VARIANT 125
FT /note="R -> H (in strain: MEL01, MEL02, MEL12, MEL13,
FT MEL14, MEL15, MEL16, MEL17, MEL18, MEL19, MEL20, ZBMEL84,
FT ZBMEL95, ZBMEL131, ZBMEL157, ZBMEL191, ZBMEL377 and
FT ZBMEL398)"
FT VARIANT 239
FT /note="P -> R (in strain: ZBMEL186)"
SQ SEQUENCE 326 AA; 38034 MW; B1DF380F2631AD90 CRC64;
MAPPENGILE VLENLLDRYK INLLQMMFGT FIATIVFFGG LMTFVEKYLP NSIRQSFRYG
KHSFKGETDP LVAWLEVPKS WFKHFYTFAL FWSWLAFYVL VSTVREQKEA PEYVLQFLDI
MGGGRSHRKV EIDSTTACVG AFMLTLQCTR RFYETNFVQI FSKKSKINLS HYAVGYVHYF
GAVIALLSNT SGFVRGSKPM EFSLDKLTSQ QILYLGVFFL AWQQQYASNM ILVNLRKDPR
TGSVKTEKHL LPKGGLFNLL SSPHMFLEVV MYFCIADLYM PVRIWRLIFL WVASNQTINA
LLTHKWYQET FREYPKNRRA IIPFLL
