B3GA3_CRIGR
ID B3GA3_CRIGR Reviewed; 335 AA.
AC Q9WU47;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10075678; DOI=10.1074/jbc.274.12.7857;
RA Wei G., Bai X., Sarkar A.K., Esko J.D.;
RT "Formation of HNK-1 determinants and the glycosaminoglycan tetrasaccharide
RT linkage region by UDP-GlcUA:Galactose beta1, 3-glucuronosyltransferases.";
RL J. Biol. Chem. 274:7857-7864(1999).
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. Highest activity seen with Gal-beta-1,3-Gal-beta-O-R
CC (where R=naphthalenemethanol or benzyl alcohol). Stimulates 2-
CC phosphoxylose phosphatase activity of PXYLP1 in presence of uridine
CC diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage
CC region formation. {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;
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: Liver, brain and heart. Moderate expression seen in
CC lung, skeletal muscle, kidney and testis.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AF113703; AAD22007.1; -; mRNA.
DR RefSeq; NP_001233613.1; NM_001246684.1.
DR AlphaFoldDB; Q9WU47; -.
DR SMR; Q9WU47; -.
DR STRING; 10029.NP_001233613.1; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR Ensembl; ENSCGRT00001029899; ENSCGRP00001025653; ENSCGRG00001023184.
DR GeneID; 100689419; -.
DR KEGG; cge:100689419; -.
DR CTD; 26229; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000156954; -.
DR OrthoDB; 901158at2759; -.
DR BRENDA; 2.4.1.135; 1309.
DR UniPathway; UPA00378; -.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IEA:UniProtKB-EC.
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: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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..335
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 3"
FT /id="PRO_0000195175"
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 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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; 37095 MW; B4FD1D1645BDCD1C CRC64;
MKLKLKNVFL AYFLVSIAGL LYALVQLGQP CDCLPPLRAA AEQLRQKDLR ISQLQADLRR
PPPVPAQPPE PEALPTIYVI TPTYARLVQK AELVRLSQTL SLVPRLHWLL VEDAESPTPL
VSGLLAASGL LFTHLAVLTP KAQRLREGEP GWVRPRGVEQ RNKALDWLRG KGGAVGGEKD
PPPPGTQGVV YFADDDNTYS RELFKEMRWT RGVSVWPVGL VGGLRFEGPR VQDGRVVGFH
TAWEPNRPFP LDMAGFAVAL PLLLAKPNAQ FDATAPRGHL ESSLLSHLVD PKDLEPRAAN
CTQVLVWHTR TEKPKMKQEE QLQRQGQGSD PAIEV
