B3GA1_CANLF
ID B3GA1_CANLF Reviewed; 335 AA.
AC Q5CB03;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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; AJ888975; CAI62040.1; -; mRNA.
DR RefSeq; NP_001026804.1; NM_001031634.1.
DR AlphaFoldDB; Q5CB03; -.
DR SMR; Q5CB03; -.
DR STRING; 9615.ENSCAFP00000031586; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GeneID; 489265; -.
DR KEGG; cfa:489265; -.
DR CTD; 27087; -.
DR InParanoid; Q5CB03; -.
DR OrthoDB; 901158at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; 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..335
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 1"
FT /id="PRO_0000195166"
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..335
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 246..255
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT ACT_SITE 285
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 92..94
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 196..198
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 312..314
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT SITE 229
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT SITE 322
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 335 AA; 38361 MW; 194B8FE05DBE4864 CRC64;
MPKRRDILAI VLIVLPWTLL VTVWHQSTIA PLLTTHKGEP LTDSRREAAP GADPREYCMS
DRDIVEVVRT EYVYTRPPPW SDTLPTIHVV TPTYSRPVQK AELTRMANTL LHVPNLHWLV
VEDAPRRTPL TARLLRDTGL NYTHLHVETP RNYKLRGDAR DPRIPRGTMQ RNLALRWLRE
TFPRNSSQPG VVYFADDDNT YSLELFEEMR STRRVSVWPV AFVGGLRYEA PRVNGAGKVV
GWKTVFDPHR PFAIDMAGFA VNLRLILQRS QAYFKLRGVK GGYQESSLLR ELVTLNDLEP
KAANCTKILV WHTRTEKPVL VNEGKKGFTD PTVEI
