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Q9VKX7 (ALG6_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

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

Names and origin

Protein namesRecommended name:
Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
Short name=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
EC=2.4.1.267
Alternative name(s):
Asparagine-linked glycosylation protein 6 homolog
Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase
Gene names
ORF Names:CG5091
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Catalytic activity

Dolichyl beta-D-glucosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the ALG6/ALG8 glucosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q9VKX7 [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

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.
Strain: Berkeley.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014134 Genomic DNA. Translation: AAF52930.2.
AY051761 mRNA. Translation: AAK93185.1.
RefSeqNP_609393.1. NM_135549.3.
UniGeneDm.21277.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9VKX7.

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080005; FBpp0079595; FBgn0032234.
GeneID34409.
KEGGdme:Dmel_CG5091.
NMPDRfig|7227.3.peg.1809.
UCSCCG5091-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0032234. CG5091.

Phylogenomic databases

eggNOGinNOG09146.
GeneTreeEMGT00050000012559.
InParanoidQ9VKX7.
OMAFLISVIT.
OrthoDBEOG4KSN14.
PhylomeDBQ9VKX7.

Gene expression databases

BgeeQ9VKX7.
GermOnlineCG5091. Drosophila melanogaster.

Family and domain databases

InterProIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
KOK03848.
PANTHERPTHR12413. Alg6_Alg8. 1 hit.
PfamPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio788359.

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: January 25, 2012
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents