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Reviewed, UniProtKB/Swiss-Prot Q9VKX7 (ALG6_DROME)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
      Short name=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
    EC=2.4.1.-
Alternative name(s):
    Asparagine-linked glycosylation protein 6
Gene names
ORF Names: CG5091
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man9GlcNAc(2)-PP-Dol By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the ALG6/ALG8 glucosyltransferase family.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransferase activity, transferring hexosyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
PRO_0000174158

Regions

Transmembrane114 – 13320 Potential
Transmembrane161 – 18121 Potential
Transmembrane235 – 25521 Potential
Transmembrane296 – 31621 Potential
Transmembrane322 – 34221 Potential
Transmembrane385 – 40521 Potential
Transmembrane418 – 43821 Potential
Transmembrane441 – 46121 Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9VKX7-1 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: C9F67AE977E30E60

FASTA47553,653
        10         20         30         40         50         60 
MRSEILASAF LGLAVRSIIS LYSYSGFDSP PMHGDYEAQR HWQEITVNLA VGEWYTNSSN 

        70         80         90        100        110        120 
NDLQYWGLDY PPLTAYHSYL VGRIGASIDP RFVELHKSRG FESKEHKRFM RATVVSADVL 

       130        140        150        160        170        180 
IYLPAMLLLA YSLDKAFRSD DKLFLFTLVA AYPGQTLIDN GHFQYNNISL GFAAVAIAAI 

       190        200        210        220        230        240 
LRRRFYAAAF FFTLALNYKQ MELYHSLPFF AFLLGECVSQ KSFASFIAEI SRIAAVVLGT 

       250        260        270        280        290        300 
FAILWVPWLG SLQAVLQVLH RLFPVARGVF EDKVANVWCA VNVVWKLKKH ISNDQMALVC 

       310        320        330        340        350        360 
IACTLIASLP TNVLLFRRRT NVGFLLALFN TSLAFFLFSF QVHEKTILLT ALPALFLLKC 

       370        380        390        400        410        420 
WPDEMILFLE VTVFSMLPLL ARDELLVPAV VATVAFHLIF KCFDSKSKLS NEYPLKYIAN 

       430        440        450        460        470 
ISQILMISVV VASLTVPAPT KYPDLWPLII SVTSCGHFFL FFLWGNVQQF SSKLS

« Hide

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References

« Hide 'large scale' references
[1]"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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.

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Cross-references

Sequence databases

AE014134 Genomic DNA. Translation: AAF52930.2.
AY051761 mRNA. Translation: AAK93185.1.
RefSeqNP_609393.1.
UniGeneDm.21277

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

Genome annotation databases

EnsemblFBgn0032234. Drosophila melanogaster. [Contig view]
GeneID34409.
KEGGdme:Dmel_CG5091.
NMPDRfig|7227.3.peg.1809.

Organism-specific databases

FlyBaseFBgn0032234. CG5091.

Phylogenomic databases

HOGENOMQ9VKX7.
OMAQ9VKX7. CATCFSI.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-008369-MON.

Gene expression databases

ArrayExpressQ9VKX7.
GermOnlineCG5091. Drosophila melanogaster.

Family and domain databases

InterProIPR004856. Glycosyltransferase_ALG6/ALG8.
[Graphical view]
PANTHERPTHR12413. Alg6_Alg8. 1 hit.
PfamPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio788359.

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Entry information

Entry nameALG6_DROME
AccessionPrimary (citable) accession number: Q9VKX7
Secondary accession number(s): Q960Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 27, 2002
Last modified: June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents