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Protein

Polyprenol reductase

Gene

CG7840

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism (By similarity).By similarity

Catalytic activityi

Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH.

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_283183. Androgen biosynthesis.
REACT_285839. Synthesis of Dolichyl-phosphate.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyprenol reductase (EC:1.3.1.94)
Gene namesi
ORF Names:CG7840
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032014. CG7840.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei26 – 4621HelicalSequence AnalysisAdd
BLAST
Transmembranei84 – 10421HelicalSequence AnalysisAdd
BLAST
Transmembranei167 – 18721HelicalSequence AnalysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence AnalysisAdd
BLAST
Transmembranei256 – 27621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Polyprenol reductasePRO_0000398654Add
BLAST

Proteomic databases

PaxDbiQ9VLP9.
PRIDEiQ9VLP9.

Expressioni

Gene expression databases

BgeeiQ9VLP9.
GenevisibleiQ9VLP9. DM.

Interactioni

Protein-protein interaction databases

BioGridi60262. 1 interaction.
IntActiQ9VLP9. 1 interaction.
MINTiMINT-313018.
STRINGi7227.FBpp0079218.

Structurei

3D structure databases

ProteinModelPortaliQ9VLP9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG330066.
GeneTreeiENSGT00500000044920.
InParanoidiQ9VLP9.
KOiK12345.
OMAiWLHSARR.
OrthoDBiEOG72ZCFT.
PhylomeDBiQ9VLP9.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VLP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPENGILE VLENLLDRYK INLLQMMFGT FIATIVFFGG LMTFVEKYLP
60 70 80 90 100
NSIRQSFRYG KHSFKGETDP LVAWLEVPKS WFKHFYTFAL FWSWLAFYVL
110 120 130 140 150
VSTVREQKEA PEYVLQFLDI MGGGRSHRKV EIDSTTACVG AFMLTLQCTR
160 170 180 190 200
RFYETNFVQI FSKKSKINLS HYAVGYVHYF GAVIALLSNT SGFVRGSKPM
210 220 230 240 250
EFSLDKLTSQ QILYLGVFFL AWQQQYASNM ILVNLRKDPR TGSVKTEKHL
260 270 280 290 300
LPKGGLFNLL SSPHMFLEVV MYFCIADLYM PVRIWRLIFL WVASNQTINA
310 320
LLTHKWYQET FREYPKNRRA IIPFLL
Length:326
Mass (Da):38,034
Last modified:May 1, 2000 - v1
Checksum:iB1DF380F2631AD90
GO

Sequence cautioni

The sequence AAM52687.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91L → P in strain: ZBMEL95 and ZBMEL157.
Natural varianti96 – 961A → V in strain: MEL11, ZBMEL145, ZBMEL131, ZBMEL229 and ZBMEL384.
Natural varianti125 – 1251R → H in strain: MEL01, MEL02, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17, MEL18, MEL19, MEL20, ZBMEL84, ZBMEL95, ZBMEL131, ZBMEL157, ZBMEL191, ZBMEL377 and ZBMEL398.
Natural varianti239 – 2391P → R in strain: ZBMEL186.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM294298 Genomic DNA. Translation: CAL26216.1.
AM294299 Genomic DNA. Translation: CAL26217.1.
AM294300 Genomic DNA. Translation: CAL26218.1.
AM294301 Genomic DNA. Translation: CAL26219.1.
AM294302 Genomic DNA. Translation: CAL26220.1.
AM294303 Genomic DNA. Translation: CAL26221.1.
AM294304 Genomic DNA. Translation: CAL26230.1.
AM294305 Genomic DNA. Translation: CAL26235.1.
AM294306 Genomic DNA. Translation: CAL26236.1.
AM294307 Genomic DNA. Translation: CAL26237.1.
AM294308 Genomic DNA. Translation: CAL26238.1.
FM245364 Genomic DNA. Translation: CAR93290.1.
FM245365 Genomic DNA. Translation: CAR93291.1.
FM245366 Genomic DNA. Translation: CAR93292.1.
FM245367 Genomic DNA. Translation: CAR93293.1.
FM245368 Genomic DNA. Translation: CAR93294.1.
FM245369 Genomic DNA. Translation: CAR93295.1.
FM245370 Genomic DNA. Translation: CAR93296.1.
FM245371 Genomic DNA. Translation: CAR93297.1.
FM245372 Genomic DNA. Translation: CAR93298.1.
FM245373 Genomic DNA. Translation: CAR93299.1.
FM245374 Genomic DNA. Translation: CAR93300.1.
FM245375 Genomic DNA. Translation: CAR93301.1.
AE014134 Genomic DNA. Translation: AAF52635.1.
AY122175 mRNA. Translation: AAM52687.1. Different initiation.
RefSeqiNP_609203.1. NM_135359.3.
UniGeneiDm.23194.

Genome annotation databases

EnsemblMetazoaiFBtr0079598; FBpp0079218; FBgn0032014.
GeneIDi34136.
KEGGidme:Dmel_CG7840.
UCSCiCG7840-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM294298 Genomic DNA. Translation: CAL26216.1.
AM294299 Genomic DNA. Translation: CAL26217.1.
AM294300 Genomic DNA. Translation: CAL26218.1.
AM294301 Genomic DNA. Translation: CAL26219.1.
AM294302 Genomic DNA. Translation: CAL26220.1.
AM294303 Genomic DNA. Translation: CAL26221.1.
AM294304 Genomic DNA. Translation: CAL26230.1.
AM294305 Genomic DNA. Translation: CAL26235.1.
AM294306 Genomic DNA. Translation: CAL26236.1.
AM294307 Genomic DNA. Translation: CAL26237.1.
AM294308 Genomic DNA. Translation: CAL26238.1.
FM245364 Genomic DNA. Translation: CAR93290.1.
FM245365 Genomic DNA. Translation: CAR93291.1.
FM245366 Genomic DNA. Translation: CAR93292.1.
FM245367 Genomic DNA. Translation: CAR93293.1.
FM245368 Genomic DNA. Translation: CAR93294.1.
FM245369 Genomic DNA. Translation: CAR93295.1.
FM245370 Genomic DNA. Translation: CAR93296.1.
FM245371 Genomic DNA. Translation: CAR93297.1.
FM245372 Genomic DNA. Translation: CAR93298.1.
FM245373 Genomic DNA. Translation: CAR93299.1.
FM245374 Genomic DNA. Translation: CAR93300.1.
FM245375 Genomic DNA. Translation: CAR93301.1.
AE014134 Genomic DNA. Translation: AAF52635.1.
AY122175 mRNA. Translation: AAM52687.1. Different initiation.
RefSeqiNP_609203.1. NM_135359.3.
UniGeneiDm.23194.

3D structure databases

ProteinModelPortaliQ9VLP9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60262. 1 interaction.
IntActiQ9VLP9. 1 interaction.
MINTiMINT-313018.
STRINGi7227.FBpp0079218.

Proteomic databases

PaxDbiQ9VLP9.
PRIDEiQ9VLP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079598; FBpp0079218; FBgn0032014.
GeneIDi34136.
KEGGidme:Dmel_CG7840.
UCSCiCG7840-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0032014. CG7840.

Phylogenomic databases

eggNOGiNOG330066.
GeneTreeiENSGT00500000044920.
InParanoidiQ9VLP9.
KOiK12345.
OMAiWLHSARR.
OrthoDBiEOG72ZCFT.
PhylomeDBiQ9VLP9.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_283183. Androgen biosynthesis.
REACT_285839. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

GenomeRNAii34136.
NextBioi787042.
PROiQ9VLP9.

Gene expression databases

BgeeiQ9VLP9.
GenevisibleiQ9VLP9. DM.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Widespread adaptive evolution of Drosophila genes with sex-biased expression."
    Proeschel M., Zhang Z., Parsch J.
    Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL84 and ZBMEL95.
  2. "The influence of demography and weak selection on the McDonald-Kreitman test: an empirical study in Drosophila."
    Parsch J., Zhang Z., Baines J.F.
    Mol. Biol. Evol. 26:691-698(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17, MEL18, MEL19 and MEL20.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPORED_DROME
AccessioniPrimary (citable) accession number: Q9VLP9
Secondary accession number(s): A0ANR0
, A0ANR1, A0ANR2, A0ANR3, A0ANR5, Q8MR21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.