Reviewed, UniProtKB/Swiss-Prot Q9VLA1 (B3G2S_DROME)

Names and origin

Protein names

Recommended name:
    Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase S
    EC=2.4.1.135
Alternative name(s):
    Beta-1,3-glucuronyltransferase S
    Glucuronosyltransferase-S
    GlcAT-S
    UDP-glucuronosyltransferase-S
      Short name=DmGlcAT-BSI

Gene names

Name:	GlcAT-S
Synonyms:	GLCAT-BSI
ORF Names:	CG3881

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

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	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Enzyme has a broad specificity.
Catalytic activity	UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein.
Cofactor	Manganese.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane proteinPotential.
Developmental stage	Expressed from early embryos to adults; maximal expression in third instar larvae through to adulthood.
Sequence similarities	Belongs to the glycosyltransferase 43 family.
Sequence caution	The sequence BAC65096.1 differs from that shown. Reason: Frameshift at positions 27 and 44.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycoprotein biosynthetic process Ref.4 Non-traceable author statement. Source: FlyBase glycosphingolipid biosynthetic process Ref.4 Non-traceable author statement. Source: FlyBase proteoglycan biosynthetic process Ref.4 Non-traceable author statement. Source: FlyBase
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	N-acetyllactosamine beta-1,3-glucuronosyltransferase activity Ref.4 Inferred from direct assay. Source: FlyBase asioloorosomucoid beta-1,3-glucuronosyltransferase activity Ref.4 Inferred from direct assay. Source: FlyBase galactosyl beta-1,3 N-acetylgalactosamine beta-1,3-glucuronosyltransferase activity Ref.4 Inferred from direct assay. Source: FlyBase galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Ref.4 Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform b (identifier: Q9VLA1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform a (identifier: Q9VLA1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.
     83-93: EDSEEGSHHGL → MNLFENENKVK

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 409	409	Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase S		PRO_0000195181
Regions
	Topological domain	1 – 53	53	Cytoplasmic Potential
	Transmembrane	54 – 73	20	Signal-anchor for type II membrane protein Potential
	Topological domain	74 – 409	336	Lumenal Potential
Sites
	Active site	318	1	Proton acceptor By similarity
	Metal binding	235	1	Manganese By similarity
Amino acid modifications
	Modified residue	9	1	Phosphoserine
	Modified residue	11	1	Phosphothreonine
	Modified residue	12	1	Phosphoserine
	Modified residue	32	1	Phosphoserine
	Glycosylation	102	1	N-linked (GlcNAc...) Potential
	Glycosylation	223	1	N-linked (GlcNAc...) Potential
	Glycosylation	338	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 82	82	Missing in isoform a.		VSP_050624
	Alternative sequence	83 – 93	11	EDSEEGSHHGL → MNLFENENKVK in isoform a.		VSP_050625

Sequences

	Sequence		Length	Mass (Da)
	Isoform b [UniParc]. Last modified October 1, 2002. Version 2. Checksum: D3CB9DBD5C666A3B	FASTA	409	46,711
	10 20 30 40 50 60 MSSARLLESQ TSDEDNEDIE RRPHQSHSRS CSNNTTPTHP PHPMVRKGGV ARRICLIGGA 70 80 90 100 110 120 LFLLLVALCY LTLSGDTRLG GSEDSEEGSH HGLDSMNFRP LNETVHICSE SYEDRRQFMQ 130 140 150 160 170 180 DKPQSDYVQL PVIYFVTPTY PRREQIPELT RLAHTLLHIP RLHWLVADDQ EKCNDYMDTL 190 200 210 220 230 240 LYRFGMPFTH MVSPMPSKFR NEKPAPRGVA NRRAALQWIR QHNLTNGILY FGDDDNTYDL 250 260 270 280 290 300 RLFSEIRKTQ RVSMFPVGLI ADYGVSGPVV RKGKVVAFLD SWVAGRRWPV DMAGFAVNLE 310 320 330 340 350 360 YMAQYPYVNM PYKPGYEEDL FLRSIGLQMN LIEPRGNNCT EILVWHTQTK SKKLGMVRLE 370 380 390 400 SKYLDDRSNL GALLHNLKLM GVTSTTESEG RNALISKNGR ENPHSKILS
	Isoform a [UniParc]. Checksum: 3A435803FBD8130D		327	37,969
	10 20 30 40 50 60 MNLFENENKV KDSMNFRPLN ETVHICSESY EDRRQFMQDK PQSDYVQLPV IYFVTPTYPR 70 80 90 100 110 120 REQIPELTRL AHTLLHIPRL HWLVADDQEK CNDYMDTLLY RFGMPFTHMV SPMPSKFRNE 130 140 150 160 170 180 KPAPRGVANR RAALQWIRQH NLTNGILYFG DDDNTYDLRL FSEIRKTQRV SMFPVGLIAD 190 200 210 220 230 240 YGVSGPVVRK GKVVAFLDSW VAGRRWPVDM AGFAVNLEYM AQYPYVNMPY KPGYEEDLFL 250 260 270 280 290 300 RSIGLQMNLI EPRGNNCTEI LVWHTQTKSK KLGMVRLESK YLDDRSNLGA LLHNLKLMGV 310 320 TSTTESEGRN ALISKNGREN PHSKILS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, ALTERNATIVE SPLICING.
[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] (ISOFORM B). Strain: Berkeley. Tissue: Head.
[4]	"Identification and characterization of three Drosophila melanogaster glucuronyltransferases responsible for the synthesis of the conserved glycosaminoglycan-protein linkage region of proteoglycans: two novel homologs exhibit broad specificity toward oligosaccharides from proteoglycans, glycoproteins, and glycosphingolipids." Kim B.-T., Tsuchida K., Lincecum J., Kitagawa K., Bernfield M., Sugahara K. J. Biol. Chem. 278:9116-9124(2003) [PubMed: 12511570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-409 (ISOFORM B), FUNCTION, COFACTOR, DEVELOPMENTAL STAGE.
[5]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; THR-11; SER-12 AND SER-32, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014134 Genomic DNA. Translation: AAF52795.2. AE014134 Genomic DNA. Translation: AAF52794.2. AY058399 mRNA. Translation: AAL13628.1. AB080696 mRNA. Translation: BAC65096.1. Frameshift.
RefSeq	NP_609303.1. NP_723476.1.
UniGene	Dm.2664 Dm.370
3D structure databases
HSSP	HSSP built from PDB template 1KWS based on UniProtKB O94766.
ModBase	Search...
Genome annotation databases
Ensembl	CG3881. Drosophila melanogaster. [Contig view]
GeneID	34282.
KEGG	dme:Dmel_CG3881.
Organism-specific databases
FlyBase	FBgn0032135. GlcAT-S.
Phylogenomic databases
HOGENOM	Q9VLA1.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-008189-MON.
Gene expression databases
ArrayExpress	Q9VLA1.
GermOnline	CG3881. Drosophila melanogaster.
Family and domain databases
InterPro	IPR005027. Glyco_trans_43. [Graphical view]
PANTHER	PTHR10896. Glyco_trans_43. 1 hit.
Pfam	PF03360. Glyco_transf_43. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	787733.

Entry information

Entry name

B3G2S_DROME

Accession

Primary (citable) accession number: Q9VLA1
Secondary accession number(s): Q868Q3, Q8IPE6, Q95U07

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	October 1, 2002
Last modified:	November 25, 2008
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project