ID Q5CAS7_CHICK Unreviewed; 304 AA. AC Q5CAS7; DT 12-APR-2005, integrated into UniProtKB/TrEMBL. DT 12-APR-2005, sequence version 1. DT 04-NOV-2026, entry version 102. DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase {ECO:0000256|ARBA:ARBA00012641, ECO:0000256|RuleBase:RU363127}; DE EC=2.4.1.135 {ECO:0000256|ARBA:ARBA00012641, ECO:0000256|RuleBase:RU363127}; GN Name=B3GAT2 {ECO:0000313|EMBL:CAI63864.1}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:CAI63864.1}; RN [1] {ECO:0000313|EMBL:CAI63864.1} RP NUCLEOTIDE SEQUENCE. 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 -!- 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] + UDP + H(+); 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:0000256|ARBA:ARBA00047979, CC ECO:0000256|RuleBase:RU363127}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936, CC ECO:0000256|PIRSR:PIRSR605027-3, ECO:0000256|RuleBase:RU363127}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|RuleBase:RU363127}. CC -!- SUBCELLULAR LOCATION: Endomembrane system CC {ECO:0000256|ARBA:ARBA00060399}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00060399}. Golgi apparatus membrane CC {ECO:0000256|RuleBase:RU363127}; Single-pass type II membrane protein CC {ECO:0000256|RuleBase:RU363127}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family. CC {ECO:0000256|ARBA:ARBA00007706, ECO:0000256|RuleBase:RU363127}. 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; AJ889606; CAI63864.1; -; mRNA. DR AlphaFoldDB; Q5CAS7; -. DR GlyCosmos; Q5CAS7; 1 site, No reported glycans. DR VEuPathDB; HostDB:geneid_428638; -. DR OrthoDB; 675023at2759; -. DR PhylomeDB; Q5CAS7; -. DR UniPathway; UPA00378; -. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IEA:UniProtKB-UniRule. DR CDD; cd00218; GlcAT-I; 1. DR FunFam; 3.90.550.10:FF:000010; Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase; 1. DR Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1. DR InterPro; IPR005027; Glyco_trans_43. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR10896:SF8; GALACTOSYLGALACTOSYLXYLOSYLPROTEIN 3-BETA-GLUCURONOSYLTRANSFERASE 2; 1. DR PANTHER; PTHR10896; GALACTOSYLGALACTOSYLXYLOSYLPROTEIN 3-BETA-GLUCURONOSYLTRANSFERASE BETA-1,3-GLUCURONYLTRANSFERASE; 1. DR Pfam; PF03360; Glyco_transf_43; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 2: Evidence at transcript level; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR605027- KW 6}; Glycosyltransferase {ECO:0000313|EMBL:CAI63864.1}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034, KW ECO:0000256|RuleBase:RU363127}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR605027-3}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR605027-3}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968, KW ECO:0000256|RuleBase:RU363127}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363127}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT REGION 1..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 254 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-1" FT BINDING 67..69 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-2" FT BINDING 98 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-2" FT BINDING 135 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-2" FT BINDING 140 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-2" FT BINDING 166..168 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-2" FT BINDING 168 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-3" FT BINDING 281..283 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-2" FT SITE 199 FT /note="Interaction with galactose moiety of substrate FT glycoprotein" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-4" FT SITE 291 FT /note="Interaction with galactose moiety of substrate FT glycoprotein" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-4" FT CARBOHYD 273 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR605027-6" SQ SEQUENCE 304 AA; 34619 MW; 5C45DF677FEEA624 CRC64; MRAEQKGKEQ LQRRRLREDA IDVSNPHHSH PMFSDESPPF LNPSGPRVAS PPRRPNATLP TIYAITPTYS RPVFTAELTR LANTLRQVAR LHWILVEDAA TRSELVSRFV AGAGLPCTHL HVPTPRRYKR PGLPRATEQR NAGLAWLRQR HQHLPAPQPG VLFFADDDNT YSLELFHEMR TTRKVSVWPV GLVGGRRYER PVVENGKVVG WYTGWRADRP FAIDMAGFAV SLQVILSHPK AVFKRRGSQP GMQESDFLKQ ITTVEELEPK ANNCTKVLVW HTRTEKVNLA NEPKYHLDTV NIEV //