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Reviewed, UniProtKB/Swiss-Prot Q9W3V8 (ALG8_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 Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
      Short name=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase
    EC=2.4.1.-
Alternative name(s):
    Asparagine-linked glycosylation protein 8
Gene names
ORF Names: CG4542
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 length511 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 second 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 Glc1Man9GlcNAc(2)-PP-Dol By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

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 – 511511Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
PRO_0000174165

Regions

Transmembrane4 – 2421 Potential
Transmembrane94 – 11219 Potential
Transmembrane124 – 14421 Potential
Transmembrane151 – 17121 Potential
Transmembrane210 – 23021 Potential
Transmembrane300 – 32021 Potential
Transmembrane332 – 35221 Potential
Transmembrane356 – 37015 Potential
Transmembrane377 – 39418 Potential
Transmembrane432 – 45221 Potential
Transmembrane469 – 49123 Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9W3V8-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: BD8C5A20CB3D6A0F

FASTA51157,945
        10         20         30         40         50         60 
MKDLFWHLVG IATGLKILLI PAYHSTDFEV HRNWLAITHS LPLNQWYVDA TSEWTLDYPP 

        70         80         90        100        110        120 
FFAYFEWLLS QVAKYVDPRM LVVDNLNYES KATVYFQRLS VIVTDLVYVL GVRSCLGSLG 

       130        140        150        160        170        180 
LGRDTQQFFA ASMLLLLNVG LIFVDHIHFQ YNGLLFGILL LSIGSLIRQR FLWSAFAFAV 

       190        200        210        220        230        240 
LLNFKHIFLY MAPAFGVYLL RFYCLEQASV VSAVGAVVKL LVVGLTPFAV SFGPFWQQLP 

       250        260        270        280        290        300 
QVLSRLFPFK RGLTHAYWAP NFWALYNAAD KLAAGVLKVQ DGGASTTSGL VQEVRHSVLP 

       310        320        330        340        350        360 
AITPPVTFAL TALFMLPILV KLFRSAKKQS PLVFLRAVVL CGCSSFVFGW HVHEKAILMV 

       370        380        390        400        410        420 
LLPLCLLTLV NREDARYAYV LGIAGYFSLF PLLFDADLYI PRYSLYMSYV AMMYGQLYRI 

       430        440        450        460        470        480 
FPGFRGFHTL EWLYMLGFMA IPLYEHLLSF LLHLDQRLPF LPLLLTSVYS ALGVLYFFGA 

       490        500        510 
YYLYALGISW GKVPIASSTS AAAVKRKRKT K

« 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.
[4]Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.

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Cross-references

Sequence databases

AE014298 Genomic DNA. Translation: AAF46205.1.
AY069662 mRNA. Translation: AAL39807.1.
BT029072 mRNA. Translation: ABJ17005.1.
RefSeqNP_001138170.1.
NP_572355.1.
UniGeneDm.59

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT57. Glycosyltransferase Family 57.

Proteomic databases

PRIDEQ9W3V8.

Genome annotation databases

EnsemblFBgn0029906. Drosophila melanogaster. [Contig view]
GeneID31623.
KEGGdme:Dmel_CG4542.
NMPDRfig|7227.3.peg.16783.

Organism-specific databases

FlyBaseFBgn0029906. CG4542.

Phylogenomic databases

HOGENOMQ9W3V8.
OMAQ9W3V8. HNLNYSS.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-000883-MON.

Gene expression databases

ArrayExpressQ9W3V8.
GermOnlineCG4542. 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

NextBio774548.

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Entry information

Entry nameALG8_DROME
AccessionPrimary (citable) accession number: Q9W3V8
Secondary accession number(s): Q058Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 56 of the entry and version 1 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