B3GA3_MOUSE
ID B3GA3_MOUSE Reviewed; 335 AA.
AC P58158;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3;
DE EC=2.4.1.135 {ECO:0000250|UniProtKB:O94766};
DE AltName: Full=Beta-1,3-glucuronyltransferase 3;
DE AltName: Full=Glucuronosyltransferase I;
DE Short=GlcAT-I;
DE AltName: Full=UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase;
DE Short=GlcUAT-I;
GN Name=B3gat3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=21763480; DOI=10.1016/j.ajhg.2011.05.021;
RA Baasanjav S., Al-Gazali L., Hashiguchi T., Mizumoto S., Fischer B.,
RA Horn D., Seelow D., Ali B.R., Aziz S.A., Langer R., Saleh A.A., Becker C.,
RA Nurnberg G., Cantagrel V., Gleeson J.G., Gomez D., Michel J.B.,
RA Stricker S., Lindner T.H., Nurnberg P., Sugahara K., Mundlos S.,
RA Hoffmann K.;
RT "Faulty initiation of proteoglycan synthesis causes cardiac and joint
RT defects.";
RL Am. J. Hum. Genet. 89:15-27(2011).
CC -!- FUNCTION: Glycosaminoglycans biosynthesis. Involved in forming the
CC linkage tetrasaccharide present in heparan sulfate and chondroitin
CC sulfate. Transfers a glucuronic acid moiety from the uridine
CC diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region
CC trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser
CC residue at the glycosaminylglycan attachment site of proteoglycans. Can
CC also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope
CC on glycoproteins. Stimulates 2-phosphoxylose phosphatase activity of
CC PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA)
CC during completion of linkage region formation.
CC {ECO:0000250|UniProtKB:O94766}.
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:0000250|UniProtKB:O94766};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PXYLP1; the
CC interaction increases the 2-phosphoxylose phosphatase activity of
CC PXYLP1 during completion of linkage region formation in a B3GAT3-
CC mediated manner. {ECO:0000250|UniProtKB:O94766}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O94766}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O94766}. Golgi apparatus, cis-Golgi network
CC {ECO:0000250|UniProtKB:O94766}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, aorta, bone, and also in
CC osteoblasts. {ECO:0000269|PubMed:21763480}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC002103; AAH02103.1; -; mRNA.
DR EMBL; BC004038; AAH04038.1; -; mRNA.
DR EMBL; BC012930; AAH12930.1; -; mRNA.
DR CCDS; CCDS29558.1; -.
DR RefSeq; NP_077218.1; NM_024256.2.
DR AlphaFoldDB; P58158; -.
DR SMR; P58158; -.
DR STRING; 10090.ENSMUSP00000093962; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; P58158; 1 site.
DR PhosphoSitePlus; P58158; -.
DR EPD; P58158; -.
DR MaxQB; P58158; -.
DR PaxDb; P58158; -.
DR PeptideAtlas; P58158; -.
DR PRIDE; P58158; -.
DR ProteomicsDB; 277144; -.
DR Antibodypedia; 28557; 134 antibodies from 20 providers.
DR DNASU; 72727; -.
DR Ensembl; ENSMUST00000096243; ENSMUSP00000093962; ENSMUSG00000071649.
DR GeneID; 72727; -.
DR KEGG; mmu:72727; -.
DR UCSC; uc008gob.1; mouse.
DR CTD; 26229; -.
DR MGI; MGI:1919977; B3gat3.
DR VEuPathDB; HostDB:ENSMUSG00000071649; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000156954; -.
DR HOGENOM; CLU_045177_0_1_1; -.
DR InParanoid; P58158; -.
DR OMA; LMYALLQ; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; P58158; -.
DR TreeFam; TF313522; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 72727; 7 hits in 78 CRISPR screens.
DR ChiTaRS; B3gat3; mouse.
DR PRO; PR:P58158; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P58158; protein.
DR Bgee; ENSMUSG00000071649; Expressed in superior frontal gyrus and 254 other tissues.
DR ExpressionAtlas; P58158; baseline and differential.
DR Genevisible; P58158; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072542; F:protein phosphatase activator activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0050651; P:dermatan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 Disulfide bond; Glycoprotein; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..335
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 3"
FT /id="PRO_0000195177"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..335
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 243..252
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT REGION 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 82..84
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 308..310
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT SITE 227
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT SITE 318
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 37067 MW; 906EED2AB672F1EC CRC64;
MKLKLKNVFL AYFLVSIAGL LYALVQLGQP CDCLPPLRAA AEQLRQKDLR ISQLQADLRR
PPPVPAQPPE PEALPTIYVI TPTYARLVQK AELVRLSQTL SLVPRLHWLL VEDAESPTPL
VSGLLAASGL LFTHLAVLTP KAQRLREGEP GWVRPRGVEQ RNKALDWLRG KGGAVGGEKD
PPPPGTQGVV YFADDDNTYS RELFKEMRWT RGVSVWPVGL VGGLRFEGPQ VQDGRVVGFH
TAWEPNRPFP LDMAGFAVAL PLLLAKPNAQ FDATAPRGHL ESSLLSHLVD PKDLEPRAAN
CTQVLVWHTR TEKPKMKQEE QLQRQGQGSD PAIEV
