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Protein

Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase

Gene

Alg10

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

Functioni

Adds the third 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 Glc2Man9GlcNAc(2)-PP-Dol (By similarity).By similarity

Catalytic activityi

Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-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 = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-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.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarity
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

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT59. Glycosyltransferase Family 59.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferaseBy similarity (EC:2.4.1.256By similarity)
Alternative name(s):
Alpha-2-glucosyltransferase ALG101 Publication
Gene namesi
Name:Alg10
ORF Names:CG32076
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0052076. Alg10.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2 – 2221HelicalSequence analysisAdd
BLAST
Transmembranei59 – 7921HelicalSequence analysisAdd
BLAST
Transmembranei82 – 9817HelicalSequence analysisAdd
BLAST
Transmembranei233 – 25321HelicalSequence analysisAdd
BLAST
Transmembranei261 – 28121HelicalSequence analysisAdd
BLAST
Transmembranei299 – 31921HelicalSequence analysisAdd
BLAST
Transmembranei341 – 36121HelicalSequence analysisAdd
BLAST
Transmembranei370 – 39021HelicalSequence analysisAdd
BLAST
Transmembranei412 – 43221HelicalSequence 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 – 449449Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferasePRO_0000413533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8T8L8.
PRIDEiQ8T8L8.

Expressioni

Gene expression databases

BgeeiQ8T8L8.
ExpressionAtlasiQ8T8L8. differential.
GenevisibleiQ8T8L8. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0075946.

Structurei

3D structure databases

ProteinModelPortaliQ8T8L8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALG10 glucosyltransferase family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2642. Eukaryota.
ENOG410YGXE. LUCA.
GeneTreeiENSGT00390000012906.
InParanoidiQ8T8L8.
KOiK03850.
OMAiRKVQPRH.
OrthoDBiEOG76HQ16.
PhylomeDBiQ8T8L8.

Family and domain databases

InterProiIPR016900. Alg10.
[Graphical view]
PANTHERiPTHR12989. PTHR12989. 1 hit.
PfamiPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFiPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8T8L8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGSWKLILP VGFVLYSLPL FLRVNGTSDY VIDEEFHIPQ GLAFCRKEFD
60 70 80 90 100
VWDPKITTFP GLYLIALLLN PLSLCTVTGL RMLSLAGAGI NILLLYKIRR
110 120 130 140 150
RILAGSGGNS YAAHEAITMS VLPPLYFFSH LYYTDTLSLT MVLLFYNYWQ
160 170 180 190 200
QEAHLPAAVF GAASVLMRQT NIVWVCMATG MTVLDTLVNQ CARTGRVPKE
210 220 230 240 250
NVRLMGKELW LQLVSSPQLL CNCILSILAK CCFYASIILP FVGFLFINGS
260 270 280 290 300
IVVGDKSAHE ASLHVPQLFY FAIFAAGFGI SNTIRQFRPA AELIRRNRVL
310 320 330 340 350
SLLALLLILV VVHLNTEVHP YLLADNRHYT FYIWSRLYGR FWWFRYAMAP
360 370 380 390 400
AYLLSICVLF CGLRHMPESF KLMFPLSLFL VLCFQRLLEL RYFLVPYILF
410 420 430 440
RLNTRHTRKG YAEWLELGAH LLLNVATFYV YFTKEFYWKN YRTPQRIIW
Length:449
Mass (Da):51,783
Last modified:June 1, 2002 - v1
Checksum:i879E231B5D047BB7
GO

Sequence cautioni

The sequence AAM75090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1901Q → R in AAM75090 (PubMed:12537569).Curated
Sequence conflicti197 – 1971V → I in AAM75090 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ431376 mRNA. Translation: CAD24126.1.
AE014296 Genomic DNA. Translation: AAF50086.2.
AY128497 mRNA. Translation: AAM75090.1. Different initiation.
RefSeqiNP_729680.1. NM_168449.2.
UniGeneiDm.31152.

Genome annotation databases

EnsemblMetazoaiFBtr0076217; FBpp0075946; FBgn0052076.
GeneIDi326193.
KEGGidme:Dmel_CG32076.
UCSCiCG32076-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ431376 mRNA. Translation: CAD24126.1.
AE014296 Genomic DNA. Translation: AAF50086.2.
AY128497 mRNA. Translation: AAM75090.1. Different initiation.
RefSeqiNP_729680.1. NM_168449.2.
UniGeneiDm.31152.

3D structure databases

ProteinModelPortaliQ8T8L8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0075946.

Protein family/group databases

CAZyiGT59. Glycosyltransferase Family 59.

Proteomic databases

PaxDbiQ8T8L8.
PRIDEiQ8T8L8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076217; FBpp0075946; FBgn0052076.
GeneIDi326193.
KEGGidme:Dmel_CG32076.
UCSCiCG32076-RA. d. melanogaster.

Organism-specific databases

CTDi84920.
FlyBaseiFBgn0052076. Alg10.

Phylogenomic databases

eggNOGiKOG2642. Eukaryota.
ENOG410YGXE. LUCA.
GeneTreeiENSGT00390000012906.
InParanoidiQ8T8L8.
KOiK03850.
OMAiRKVQPRH.
OrthoDBiEOG76HQ16.
PhylomeDBiQ8T8L8.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

GenomeRNAii326193.
PROiQ8T8L8.

Gene expression databases

BgeeiQ8T8L8.
ExpressionAtlasiQ8T8L8. differential.
GenevisibleiQ8T8L8. DM.

Family and domain databases

InterProiIPR016900. Alg10.
[Graphical view]
PANTHERiPTHR12989. PTHR12989. 1 hit.
PfamiPF04922. DIE2_ALG10. 1 hit.
[Graphical view]
PIRSFiPIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate."
    Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P.
    Mol. Biol. Evol. 19:1451-1463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "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: BerkeleyImported.
    Tissue: HeadImported.

Entry informationi

Entry nameiALG10_DROME
AccessioniPrimary (citable) accession number: Q8T8L8
Secondary accession number(s): Q8MQM2, Q9VTG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 89 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

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 one 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.