Q8T8L8 (ALG10_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
EC=2.4.1.256

Alternative name(s):
Alpha-2-glucosyltransferase ALG10

Gene names

Name:	Alg10
ORF Names:	CG32076

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. UniProtKB P50076
Catalytic activity	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. UniProtKB P50076
Pathway	Protein modification; protein glycosylation. UniProtKB P50076
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity UniProtKB P50076.
Sequence similarities	Belongs to the ALG10 glucosyltransferase family.
Sequence caution	The sequence AAM75090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	transferase activity, transferring hexosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase		PRO_0000413533
Regions
	Transmembrane	2 – 22	21	Helical; Potential
	Transmembrane	59 – 79	21	Helical; Potential
	Transmembrane	82 – 98	17	Helical; Potential
	Transmembrane	233 – 253	21	Helical; Potential
	Transmembrane	261 – 281	21	Helical; Potential
	Transmembrane	299 – 319	21	Helical; Potential
	Transmembrane	341 – 361	21	Helical; Potential
	Transmembrane	370 – 390	21	Helical; Potential
	Transmembrane	412 – 432	21	Helical; Potential
Amino acid modifications
	Glycosylation	25	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	190	1	Q → R in AAM75090. Ref.4
	Sequence conflict	197	1	V → I in AAM75090. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8T8L8 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 879E231B5D047BB7	FASTA	449	51,783
	10 20 30 40 50 60 MNGSWKLILP VGFVLYSLPL FLRVNGTSDY VIDEEFHIPQ GLAFCRKEFD VWDPKITTFP 70 80 90 100 110 120 GLYLIALLLN PLSLCTVTGL RMLSLAGAGI NILLLYKIRR RILAGSGGNS YAAHEAITMS 130 140 150 160 170 180 VLPPLYFFSH LYYTDTLSLT MVLLFYNYWQ QEAHLPAAVF GAASVLMRQT NIVWVCMATG 190 200 210 220 230 240 MTVLDTLVNQ CARTGRVPKE NVRLMGKELW LQLVSSPQLL CNCILSILAK CCFYASIILP 250 260 270 280 290 300 FVGFLFINGS IVVGDKSAHE ASLHVPQLFY FAIFAAGFGI SNTIRQFRPA AELIRRNRVL 310 320 330 340 350 360 SLLALLLILV VVHLNTEVHP YLLADNRHYT FYIWSRLYGR FWWFRYAMAP AYLLSICVLF 370 380 390 400 410 420 CGLRHMPESF KLMFPLSLFL VLCFQRLLEL RYFLVPYILF RLNTRHTRKG YAEWLELGAH 430 440 LLLNVATFYV YFTKEFYWKN YRTPQRIIW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 12200473] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"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. , 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.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ431376 mRNA. Translation: CAD24126.1. AE014296 Genomic DNA. Translation: AAF50086.2. AY128497 mRNA. Translation: AAM75090.1. Different initiation.
RefSeq	NP_729680.1. NM_168449.1.
UniGene	Dm.31152.
3D structure databases
ProteinModelPortal	Q8T8L8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8T8L8.
Protein family/group databases
CAZy	GT59. Glycosyltransferase Family 59.
Proteomic databases
PRIDE	Q8T8L8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076217; FBpp0075946; FBgn0052076.
GeneID	326193.
KEGG	dme:Dmel_CG32076.
NMPDR	fig|7227.3.peg.9324.
UCSC	CG32076-RA. d. melanogaster.
Organism-specific databases
CTD	84920.
FlyBase	FBgn0052076. Alg10.
Phylogenomic databases
GeneTree	EMGT00050000017918.
InParanoid	Q8T8L8.
OMA	TFEWPNE.
PhylomeDB	Q8T8L8.
Gene expression databases
ArrayExpress	Q8T8L8.
Bgee	Q8T8L8.
Family and domain databases
InterPro	IPR016900. Alpha1_2_glucosyltferase_Alg10. IPR007006. Glycosyltransferase_ALG10. [Graphical view]
KO	K03850.
PANTHER	PTHR12989. DIE2_ALG10. 1 hit.
Pfam	PF04922. DIE2_ALG10. 1 hit. [Graphical view]
PIRSF	PIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNet	Search...
Other
NextBio	847561.

Entry information

Entry name

ALG10_DROME

Accession

Primary (citable) accession number: Q8T8L8
Secondary accession number(s): Q8MQM2, Q9VTG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2011
Last sequence update:	June 1, 2002
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project