Reviewed, UniProtKB/Swiss-Prot Q9VTG7 (B3G2P_DROME)

Names and origin

Protein names

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

Gene names

Name:	GlcAT-P
Synonyms:	GLCAT-BSII
ORF Names:	CG6207

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	479 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.

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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycoprotein biosynthetic process Ref.1 Non-traceable author statement. Source: FlyBase glycosphingolipid biosynthetic process Ref.1 Non-traceable author statement. Source: FlyBase proteoglycan biosynthetic process Ref.1 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.1 Inferred from direct assay. Source: FlyBase asioloorosomucoid beta-1,3-glucuronosyltransferase activity Ref.1 Inferred from direct assay. Source: FlyBase galactosyl beta-1,3 N-acetylgalactosamine beta-1,3-glucuronosyltransferase activity Ref.1 Inferred from direct assay. Source: FlyBase galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Ref.1 Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopantetheine binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform A (identifier: Q9VTG7-1)

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.

Notes: No experimental confirmation available.

Isoform C (identifier: Q9VTG7-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     68-230: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase P		PRO_0000195180
Regions
	Topological domain	1 – 34	34	Cytoplasmic Potential
	Transmembrane	35 – 50	16	Signal-anchor for type II membrane protein Potential
	Topological domain	51 – 479	429	Lumenal Potential
Sites
	Active site	418	1	Proton acceptor By similarity
	Metal binding	335	1	Manganese By similarity
Amino acid modifications
	Glycosylation	90	1	N-linked (GlcNAc...) Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	271	1	N-linked (GlcNAc...) Potential
	Glycosylation	460	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	68 – 230	163	Missing in isoform C.		VSP_050626

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified May 1, 2000. Version 1. Checksum: CA40D003D1303CB2	FASTA	479	52,556
	10 20 30 40 50 60 MKGGNYTSLG TCSGINVSGN VAGTRKMSLG KSIKMYLTIF ILTTCIYMAL YQYHISREPF 70 80 90 100 110 120 AASEVVKHQE KSSSYIASYL WSPISLLMAN SSSNTNNNST TTSTTTTTAP TTPTTTTTTT 130 140 150 160 170 180 VGSVGQKLGA SSISSIRMVS LAATIPSFKS TLSESRSVSL GGHQKTATVK TSTTITTRTT 190 200 210 220 230 240 ASGLATTKLS ATTRTTAKTS AKLSAATTPT ASHMENGYKT RPTFVAASLP PPLYIITPTY 250 260 270 280 290 300 RRPEQLAELT RLGYTLKHVV NLLWLVIEDA NKTNPLVGHT LDRIGVPYEY MVAPMPEKYK 310 320 330 340 350 360 QTKKAKPRGV SNRNRGLEYL REHATEGVLY FADDDNTYDI SIFEQMRYIS KVAMWPVGLV 370 380 390 400 410 420 TKTGVSSPII QAGKLVGYYD GWIGGRKYPV DMAGFAVSVK FLKERPNAQM PFKPGYEEDG 430 440 450 460 470 FLRSLAPLDD AEIELLADEC RDILTWHTQT KKNAPAQALN RTRYKNTNLE HIDRLLVRP
	Isoform C (B) [UniParc]. Checksum: B24A65C392D8DAC8		316	35,826
	10 20 30 40 50 60 MKGGNYTSLG TCSGINVSGN VAGTRKMSLG KSIKMYLTIF ILTTCIYMAL YQYHISREPF 70 80 90 100 110 120 AASEVVKPPL YIITPTYRRP EQLAELTRLG YTLKHVVNLL WLVIEDANKT NPLVGHTLDR 130 140 150 160 170 180 IGVPYEYMVA PMPEKYKQTK KAKPRGVSNR NRGLEYLREH ATEGVLYFAD DDNTYDISIF 190 200 210 220 230 240 EQMRYISKVA MWPVGLVTKT GVSSPIIQAG KLVGYYDGWI GGRKYPVDMA GFAVSVKFLK 250 260 270 280 290 300 ERPNAQMPFK PGYEEDGFLR SLAPLDDAEI ELLADECRDI LTWHTQTKKN APAQALNRTR 310 YKNTNLEHID RLLVRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM C), FUNCTION, COFACTOR, DEVELOPMENTAL STAGE.
[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, ALTERNATIVE SPLICING.
[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] (ISOFORMS A AND C). Strain: Berkeley. Tissue: Embryo.
[5]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C). Strain: Berkeley. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB080697 mRNA. Translation: BAC65097.1. AE014296 Genomic DNA. Translation: AAF50082.1. AE014296 Genomic DNA. Translation: AAN11882.2. AY061135 mRNA. Translation: AAL28683.1. Different initiation. AY118925 mRNA. Translation: AAM50785.1. BT021381 mRNA. Translation: AAX33529.1.
RefSeq	NP_648448.1. NP_729685.2.
UniGene	Dm.3710
3D structure databases
HSSP	HSSP built from PDB template 1KWS based on UniProtKB O94766.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VTG7.
Genome annotation databases
Ensembl	CG6207. Drosophila melanogaster. [Contig view]
GeneID	39262.
Organism-specific databases
FlyBase	FBgn0036144. GlcAT-P.
Phylogenomic databases
HOGENOM	Q9VTG7.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-016214-MON. DMEL-XXX-02:DMEL-XXX-02-016215-MON.
Gene expression databases
ArrayExpress	Q9VTG7.
GermOnline	CG6207. Drosophila melanogaster.
Family and domain databases
InterPro	IPR005027. Glyco_trans_43. IPR006162. Ppantne_S. [Graphical view]
PANTHER	PTHR10896. Glyco_trans_43. 1 hit.
Pfam	PF03360. Glyco_transf_43. 1 hit. [Graphical view]
PROSITE	PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	812772.

Entry information

Entry name

B3G2P_DROME

Accession

Primary (citable) accession number: Q9VTG7
Secondary accession number(s): Q5BI43, Q8MSC2, Q95RU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	May 1, 2000
Last modified:	November 25, 2008
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project