B3G2P_DROME
ID B3G2P_DROME Reviewed; 479 AA.
AC Q9VTG7; Q5BI43; Q8MSC2; Q95RU4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase P;
DE EC=2.4.1.135 {ECO:0000269|PubMed:12511570};
DE AltName: Full=Beta-1,3-glucuronyltransferase P;
DE AltName: Full=Glucuronosyltransferase P;
DE Short=GlcAT-P;
DE AltName: Full=UDP-glucuronosyltransferase P;
DE Short=DmGlcAT-BSII;
GN Name=GlcAT-P; Synonyms=GLCAT-BSII; ORFNames=CG6207;
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:AAM50785.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), 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 [2] {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 [3] {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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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=A {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VTG7-1; Sequence=Displayed;
CC Name=C {ECO:0000303|PubMed:10731132}; Synonyms=B;
CC IsoId=Q9VTG7-2; Sequence=VSP_050626;
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=AAL28683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB080697; BAC65097.1; -; mRNA.
DR EMBL; AE014296; AAF50082.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11882.2; -; Genomic_DNA.
DR EMBL; AY061135; AAL28683.1; ALT_INIT; mRNA.
DR EMBL; AY118925; AAM50785.1; -; mRNA.
DR EMBL; BT021381; AAX33529.1; -; mRNA.
DR RefSeq; NP_001014581.1; NM_001014581.3. [Q9VTG7-2]
DR RefSeq; NP_001246713.1; NM_001259784.2. [Q9VTG7-1]
DR RefSeq; NP_001246714.1; NM_001259785.2. [Q9VTG7-2]
DR RefSeq; NP_648448.1; NM_140191.3. [Q9VTG7-1]
DR RefSeq; NP_729685.2; NM_168451.4. [Q9VTG7-2]
DR AlphaFoldDB; Q9VTG7; -.
DR SMR; Q9VTG7; -.
DR BioGRID; 64634; 3.
DR IntAct; Q9VTG7; 1.
DR STRING; 7227.FBpp0075919; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; Q9VTG7; 5 sites.
DR PaxDb; Q9VTG7; -.
DR DNASU; 39262; -.
DR EnsemblMetazoa; FBtr0076189; FBpp0075919; FBgn0036144. [Q9VTG7-1]
DR EnsemblMetazoa; FBtr0076190; FBpp0075920; FBgn0036144. [Q9VTG7-2]
DR EnsemblMetazoa; FBtr0100422; FBpp0099840; FBgn0036144. [Q9VTG7-2]
DR EnsemblMetazoa; FBtr0306254; FBpp0297364; FBgn0036144. [Q9VTG7-1]
DR EnsemblMetazoa; FBtr0306255; FBpp0297365; FBgn0036144. [Q9VTG7-2]
DR GeneID; 39262; -.
DR KEGG; dme:Dmel_CG6207; -.
DR UCSC; CG6207-RA; d. melanogaster. [Q9VTG7-1]
DR CTD; 39262; -.
DR FlyBase; FBgn0036144; GlcAT-P.
DR VEuPathDB; VectorBase:FBgn0036144; -.
DR eggNOG; KOG1476; Eukaryota.
DR HOGENOM; CLU_045177_3_2_1; -.
DR InParanoid; Q9VTG7; -.
DR OMA; HVYLATT; -.
DR PhylomeDB; Q9VTG7; -.
DR Reactome; R-DME-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 39262; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39262; -.
DR PRO; PR:Q9VTG7; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036144; Expressed in embryonic/larval hemocyte (Drosophila) and 51 other tissues.
DR ExpressionAtlas; Q9VTG7; baseline and differential.
DR Genevisible; Q9VTG7; DM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
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:0015020; F: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:0052695; P:cellular glucuronidation; IDA:FlyBase.
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:0007422; P:peripheral nervous system development; IMP: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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..479
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase P"
FT /id="PRO_0000195180"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..50
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..479
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 94..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 68..230
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12511570, ECO:0000303|PubMed:12537569,
FT ECO:0000303|Ref.5"
FT /id="VSP_050626"
SQ SEQUENCE 479 AA; 52556 MW; CA40D003D1303CB2 CRC64;
MKGGNYTSLG TCSGINVSGN VAGTRKMSLG KSIKMYLTIF ILTTCIYMAL YQYHISREPF
AASEVVKHQE KSSSYIASYL WSPISLLMAN SSSNTNNNST TTSTTTTTAP TTPTTTTTTT
VGSVGQKLGA SSISSIRMVS LAATIPSFKS TLSESRSVSL GGHQKTATVK TSTTITTRTT
ASGLATTKLS ATTRTTAKTS AKLSAATTPT ASHMENGYKT RPTFVAASLP PPLYIITPTY
RRPEQLAELT RLGYTLKHVV NLLWLVIEDA NKTNPLVGHT LDRIGVPYEY MVAPMPEKYK
QTKKAKPRGV SNRNRGLEYL REHATEGVLY FADDDNTYDI SIFEQMRYIS KVAMWPVGLV
TKTGVSSPII QAGKLVGYYD GWIGGRKYPV DMAGFAVSVK FLKERPNAQM PFKPGYEEDG
FLRSLAPLDD AEIELLADEC RDILTWHTQT KKNAPAQALN RTRYKNTNLE HIDRLLVRP
