ID   Q5CAS3_DROYA            Unreviewed;       372 AA.
AC   Q5CAS3;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   02-SEP-2026, entry version 68.
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=aglcat2 {ECO:0000313|EMBL:CAI63868.1};
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245 {ECO:0000313|EMBL:CAI63868.1};
RN   [1] {ECO:0000313|EMBL:CAI63868.1}
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|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU363127}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363127}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323,
CC       ECO:0000256|RuleBase:RU363127}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC       {ECO:0000256|ARBA:ARBA00007706, ECO:0000256|RuleBase:RU363127}.
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DR   EMBL; AJ889610; CAI63868.1; -; mRNA.
DR   AlphaFoldDB; Q5CAS3; -.
DR   OrthoDB; 675023at2759; -.
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   GO; GO:0005975; P:carbohydrate metabolic process; IEA:TreeGrafter.
DR   GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd00218; GlcAT-I; 1.
DR   FunFam; 3.90.550.10:FF:000044; 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; GALACTOSYLGALACTOSYLXYLOSYLPROTEIN 3-BETA-GLUCURONOSYLTRANSFERASE BETA-1,3-GLUCURONYLTRANSFERASE; 1.
DR   PANTHER; PTHR10896:SF51; GALACTOSYLGALACTOSYLXYLOSYLPROTEIN 3-BETA-GLUCURONOSYLTRANSFERASE S; 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:CAI63868.1};
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, ECO:0000256|RuleBase:RU363127};
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   ECO:0000256|RuleBase:RU363127};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363127}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363127"
FT   REGION          353..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        281
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605027-1"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605027-3"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605027-6"
SQ   SEQUENCE   372 AA;  42299 MW;  9B16EC8058E3209A CRC64;
     MVRKGGVARR RCLVPLVAGA LFFVAFCYLT LSADTRLALG LGGGAEDSEE LSHHGLDGMN
     FRPLNETVHI CSESYEDRRQ FMQDKPQSEY GQLPVIYFVT PTYPRREQIP ELTRLAHTLL
     HVPRLHWLVA DDQEKCNGFM DTLLYRFGIP FTHMVSPMPS KFRNEKPAPR GVANRRAALQ
     WLRQHNLTNG ILYFGDDDNT YDLRLFSEIR KTQRVSMFPV GLIADYGVSG PVVRKGKVVA
     FLDSWVAGRR WPVDMAGFAV NLEYMAQYPY VNMPYKPGYE EDLFLRSIGL QMNLIEPRGN
     NCTEILVWHT QTKSKKLGMV RLESKYLDDR SNLGALLHNL KLMGVASTTE SEGRDALISK
     NGKEKPHSKI LS
//