B3GA2_CANLF
ID B3GA2_CANLF Reviewed; 329 AA.
AC Q5CAZ6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2;
DE EC=2.4.1.135 {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=Beta-1,3-glucuronyltransferase 2;
DE AltName: Full=GlcAT-D;
DE AltName: Full=UDP-glucuronosyltransferase S;
DE Short=GlcAT-S;
DE Short=Glucuronosyltransferase S;
GN Name=B3GAT2;
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 both glycolipids and glycoproteins. {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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AJ888982; CAI62047.1; -; mRNA.
DR RefSeq; NP_001013437.1; NM_001013419.1.
DR AlphaFoldDB; Q5CAZ6; -.
DR SMR; Q5CAZ6; -.
DR STRING; 9612.ENSCAFP00000003803; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR PaxDb; Q5CAZ6; -.
DR Ensembl; ENSCAFT00030032834; ENSCAFP00030028641; ENSCAFG00030017777.
DR Ensembl; ENSCAFT00845017711; ENSCAFP00845013793; ENSCAFG00845010055.
DR GeneID; 481875; -.
DR KEGG; cfa:481875; -.
DR CTD; 135152; -.
DR VEuPathDB; HostDB:ENSCAFG00845010055; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000159583; -.
DR HOGENOM; CLU_045177_2_0_1; -.
DR InParanoid; Q5CAZ6; -.
DR OMA; TRGVSIW; -.
DR OrthoDB; 901158at2759; -.
DR TreeFam; TF313522; -.
DR Reactome; R-CFA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Chromosome 12.
DR Bgee; ENSCAFG00000002616; Expressed in temporal lobe and 46 other tissues.
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: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 Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..329
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 2"
FT /id="PRO_0000195171"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..329
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 45..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..249
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT COMPBIAS 62..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 93..95
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 124
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 166
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 191..193
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 306..308
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT SITE 224
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT SITE 316
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 329 AA; 37561 MW; 45DF20A242CD1F72 CRC64;
MKSALFSRFF ILLPWILIVI IMLDVDTRRP APPLTPRPYF SPYAVGRGGA RLPPRRGGPD
SGPGRGWEKR NESRPHARPR PEPPLPTIYA ITPTYSRPVQ KAELTRLANT FRQVAQLHWI
LVEDAAARSE LVSRFLARAG LPSTHLHVPT PRRYKRPGLP RATEQRNAGL AWLRQRHQHQ
RAQPGVLFFA DDDNTYSLEL FQEMRTTRKV SVWPVGLVGG RRYERPLVEN GKVVGWYTGW
RADRPFAIDM AGFAVSLQVI LSNPKAVFKR RGSQPGMQES DFLKQITTVE ELEPKANNCT
KVLVWHTRTE KVNLANEPKY RLDTVKIEV
