B3G2S_DROME
ID B3G2S_DROME Reviewed; 409 AA.
AC Q9VLA1; Q868Q3; Q8IPE6; Q95U07;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase S;
DE EC=2.4.1.135 {ECO:0000269|PubMed:12511570};
DE AltName: Full=Beta-1,3-glucuronyltransferase S;
DE AltName: Full=Glucuronosyltransferase S;
DE Short=GlcAT-S;
DE AltName: Full=UDP-glucuronosyltransferase S;
DE Short=DmGlcAT-BSI;
GN Name=GlcAT-S; Synonyms=GLCAT-BSI; ORFNames=CG3881;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF52795.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-409 (ISOFORM B), FUNCTION, COFACTOR, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12511570; DOI=10.1074/jbc.m209344200;
RA Kim B.-T., Tsuchida K., Lincecum J., Kitagawa K., Bernfield M.,
RA Sugahara K.;
RT "Identification and characterization of three Drosophila melanogaster
RT glucuronyltransferases responsible for the synthesis of the conserved
RT glycosaminoglycan-protein linkage region of proteoglycans: two novel
RT homologs exhibit broad specificity toward oligosaccharides from
RT proteoglycans, glycoproteins, and glycosphingolipids.";
RL J. Biol. Chem. 278:9116-9124(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; THR-11; SER-12 AND SER-32,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope
CC on both glycolipids and glycoproteins. Enzyme has a broad specificity.
CC {ECO:0000269|PubMed:12511570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571,
CC Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093;
CC EC=2.4.1.135; Evidence={ECO:0000269|PubMed:12511570};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12511570};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VLA1-1; Sequence=Displayed;
CC Name=a {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VLA1-2; Sequence=VSP_050624, VSP_050625;
CC -!- DEVELOPMENTAL STAGE: Expressed from early embryos to adults; maximal
CC expression in third instar larvae through to adulthood.
CC {ECO:0000269|PubMed:12511570}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65096.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF52795.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF52794.2; -; Genomic_DNA.
DR EMBL; AY058399; AAL13628.1; -; mRNA.
DR EMBL; AB080696; BAC65096.1; ALT_FRAME; mRNA.
DR RefSeq; NP_609303.1; NM_135459.4. [Q9VLA1-1]
DR RefSeq; NP_723476.1; NM_164864.2. [Q9VLA1-2]
DR AlphaFoldDB; Q9VLA1; -.
DR SMR; Q9VLA1; -.
DR IntAct; Q9VLA1; 1.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; Q9VLA1; 3 sites.
DR iPTMnet; Q9VLA1; -.
DR PaxDb; Q9VLA1; -.
DR DNASU; 34282; -.
DR EnsemblMetazoa; FBtr0079841; FBpp0079438; FBgn0032135. [Q9VLA1-2]
DR EnsemblMetazoa; FBtr0079842; FBpp0079439; FBgn0032135. [Q9VLA1-1]
DR GeneID; 34282; -.
DR KEGG; dme:Dmel_CG3881; -.
DR UCSC; CG3881-RA; d. melanogaster. [Q9VLA1-1]
DR CTD; 34282; -.
DR FlyBase; FBgn0032135; GlcAT-S.
DR VEuPathDB; VectorBase:FBgn0032135; -.
DR eggNOG; KOG1476; Eukaryota.
DR InParanoid; Q9VLA1; -.
DR OMA; WIVADDT; -.
DR PhylomeDB; Q9VLA1; -.
DR Reactome; R-DME-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 34282; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34282; -.
DR PRO; PR:Q9VLA1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032135; Expressed in second segment of antenna (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q9VLA1; baseline and differential.
DR Genevisible; Q9VLA1; DM.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046988; F:asioloorosomucoid beta-1,3-glucuronosyltransferase activity; IDA:FlyBase.
DR GO; GO:0046989; F:galactosyl beta-1,3 N-acetylgalactosamine beta-1,3-glucuronosyltransferase activity; IDA:FlyBase.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046987; F:N-acetyllactosamine beta-1,3-glucuronosyltransferase activity; IDA:FlyBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; NAS:FlyBase.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; NAS:FlyBase.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; NAS:FlyBase.
DR CDD; cd00218; GlcAT-I; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..409
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase S"
FT /id="PRO_0000195181"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..409
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_050624"
FT VAR_SEQ 83..93
FT /note="EDSEEGSHHGL -> MNLFENENKVK (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_050625"
SQ SEQUENCE 409 AA; 46711 MW; D3CB9DBD5C666A3B CRC64;
MSSARLLESQ TSDEDNEDIE RRPHQSHSRS CSNNTTPTHP PHPMVRKGGV ARRICLIGGA
LFLLLVALCY LTLSGDTRLG GSEDSEEGSH HGLDSMNFRP LNETVHICSE SYEDRRQFMQ
DKPQSDYVQL PVIYFVTPTY PRREQIPELT RLAHTLLHIP RLHWLVADDQ EKCNDYMDTL
LYRFGMPFTH MVSPMPSKFR NEKPAPRGVA NRRAALQWIR QHNLTNGILY FGDDDNTYDL
RLFSEIRKTQ RVSMFPVGLI ADYGVSGPVV RKGKVVAFLD SWVAGRRWPV DMAGFAVNLE
YMAQYPYVNM PYKPGYEEDL FLRSIGLQMN LIEPRGNNCT EILVWHTQTK SKKLGMVRLE
SKYLDDRSNL GALLHNLKLM GVTSTTESEG RNALISKNGR ENPHSKILS
