B3GA1_PANTR
ID B3GA1_PANTR Reviewed; 332 AA.
AC Q5CB04;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 {ECO:0000250|UniProtKB:Q9P2W7};
DE EC=2.4.1.135 {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=Beta-1,3-glucuronyltransferase 1;
DE AltName: Full=Glucuronosyltransferase P;
DE Short=GlcAT-P {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase;
DE Short=GlcUAT-P;
GN Name=B3GAT1 {ECO:0000250|UniProtKB:Q9P2W7};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ouzzine M., Magdalou J., Fournel-Gigleux S., Mollicone R., Oriol R.;
RT "Phylogeny of beta3-glucuronyltransferases.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope
CC on glycoproteins. Can also play a role in glycosaminoglycan
CC biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-
CC fetuin, and asialo-neural cell adhesion molecule. Requires
CC sphingomyelin for activity: stearoyl-sphingomyelin was the most
CC effective, followed by palmitoyl-sphingomyelin and lignoceroyl-
CC sphingomyelin. Activity was demonstrated only for sphingomyelin with a
CC saturated fatty acid and not for that with an unsaturated fatty acid,
CC regardless of the length of the acyl group.
CC {ECO:0000250|UniProtKB:O35789}.
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:O35789};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O35789};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer. Interacts with SAR1A.
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O35789}. Secreted
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250|UniProtKB:O35789}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AJ888974; CAI62039.1; -; mRNA.
DR RefSeq; NP_001026790.1; NM_001031619.1.
DR AlphaFoldDB; Q5CB04; -.
DR SMR; Q5CB04; -.
DR STRING; 9598.ENSPTRP00000054150; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR PaxDb; Q5CB04; -.
DR GeneID; 466859; -.
DR KEGG; ptr:466859; -.
DR CTD; 27087; -.
DR eggNOG; KOG1476; Eukaryota.
DR InParanoid; Q5CB04; -.
DR OrthoDB; 901158at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 Glycoprotein; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..332
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 1"
FT /id="PRO_0000195169"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..332
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 3..5
FT /note="Essential for transport from endoplasmic reticulum
FT to Golgi apparatus and interaction with SAR1A"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT REGION 243..252
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT ACT_SITE 282
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 91..93
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 309..311
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT SITE 226
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT SITE 319
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 332 AA; 38005 MW; 6ECBA46DB961D149 CRC64;
MPKRRDILAI VLIVLPWTLL ITVWHQSTLA PLLAVHKDEG SDPRRETPPG ADPREYCMSD
RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA ELTRMANTLL HVPNLHWLVV
EDAPRRTPLT ARLLRDTGLN YTHLHVETPR NYKLRGDARD PRIPRGTMQR NLALRWLRET
FPRNSSQPGV VYFADDDNPY SLELFQKVTR RVSVWPVAFV GGLRYEAPRV NGAGKVVGWK
TVFDPHRPFA IDMAGFAVNL RLILQRSQAY FKLRGVKGGY QESSLLRELV TLNDLEPKAA
NCTKILVWHT RTEKPVLVNE GKKGFTDPSV EI
