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Q9VLP9 (PORED_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

unc-119Q9XYQ21EBI-88569,EBI-127298

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Polyprenol reductase
PRO_0000398654

Regions

Transmembrane26 – 4621Helical; Potential
Transmembrane84 – 10421Helical; Potential
Transmembrane167 – 18721Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane256 – 27621Helical; Potential

Natural variations

Natural variant91L → P in strain: ZBMEL95 and ZBMEL157.
Natural variant961A → V in strain: MEL11, ZBMEL145, ZBMEL131, ZBMEL229 and ZBMEL384.
Natural variant1251R → H in strain: MEL01, MEL02, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17, MEL18, MEL19, MEL20, ZBMEL84, ZBMEL95, ZBMEL131, ZBMEL157, ZBMEL191, ZBMEL377 and ZBMEL398.
Natural variant2391P → R in strain: ZBMEL186.

Sequences

Sequence LengthMass (Da)Tools
Q9VLP9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B1DF380F2631AD90

FASTA32638,034
        10         20         30         40         50         60 
MAPPENGILE VLENLLDRYK INLLQMMFGT FIATIVFFGG LMTFVEKYLP NSIRQSFRYG 

        70         80         90        100        110        120 
KHSFKGETDP LVAWLEVPKS WFKHFYTFAL FWSWLAFYVL VSTVREQKEA PEYVLQFLDI 

       130        140        150        160        170        180 
MGGGRSHRKV EIDSTTACVG AFMLTLQCTR RFYETNFVQI FSKKSKINLS HYAVGYVHYF 

       190        200        210        220        230        240 
GAVIALLSNT SGFVRGSKPM EFSLDKLTSQ QILYLGVFFL AWQQQYASNM ILVNLRKDPR 

       250        260        270        280        290        300 
TGSVKTEKHL LPKGGLFNLL SSPHMFLEVV MYFCIADLYM PVRIWRLIFL WVASNQTINA 

       310        320 
LLTHKWYQET FREYPKNRRA IIPFLL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_609203.1. NM_135359.3.
UniGeneDm.23194.

3D structure databases

ProteinModelPortalQ9VLP9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60262. 1 interaction.
IntActQ9VLP9. 1 interaction.
MINTMINT-313018.
STRING7227.FBpp0079218.

Proteomic databases

PaxDbQ9VLP9.
PRIDEQ9VLP9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079598; FBpp0079218; FBgn0032014.
GeneID34136.
KEGGdme:Dmel_CG7840.
UCSCCG7840-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0032014. CG7840.

Phylogenomic databases

eggNOGNOG330066.
GeneTreeENSGT00500000044920.
InParanoidQ9VLP9.
KOK12345.
OMASSPHMFF.
OrthoDBEOG72ZCFT.
PhylomeDBQ9VLP9.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ9VLP9.

Family and domain databases

InterProIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi34136.
NextBio787042.
PROQ9VLP9.

Entry information

Entry namePORED_DROME
AccessionPrimary (citable) accession number: Q9VLP9
Secondary accession number(s): A0ANR0 expand/collapse secondary AC list , A0ANR1, A0ANR2, A0ANR3, A0ANR5, Q8MR21
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase