B3GA2_RAT
ID B3GA2_RAT Reviewed; 324 AA.
AC Q9Z137;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
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; Synonyms=Glcats;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10082676; DOI=10.1006/bbrc.1999.0151;
RA Seiki T., Oka S., Terayama K., Imiya K., Kawasaki T.;
RT "Molecular cloning and expression of a second glucuronyltransferase
RT involved in the biosynthesis of the HNK-1 carbohydrate epitope.";
RL Biochem. Biophys. Res. Commun. 255:182-187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Embryonic brain;
RX PubMed=10358066; DOI=10.1074/jbc.274.24.17115;
RA Shimoda Y., Tajima Y., Nagase T., Harii K., Osumi N., Sanai Y.;
RT "Cloning and expression of a novel galactoside beta1,3-
RT glucuronyltransferase involved in the biosynthesis of HNK-1 epitope.";
RL J. Biol. Chem. 274:17115-17122(1999).
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope
CC on both glycolipids and glycoproteins. Substrates include asialo-
CC orosomucoid (ASOR), paragloboside (lacto-N-neotetraosylceramide), Gal-
CC beta-1,4-GlcNAc-beta-1,3-Gal-beta-1,4-Glc-pyridylamine and Gal-beta-
CC 1,3-GlcNAc-beta-1,3-Gal-beta-1,4-Glc-pyridylamine.
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex, cerebellum and
CC whole brain.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AB010441; BAA75219.1; -; mRNA.
DR EMBL; AF106624; AAD29576.1; -; mRNA.
DR PIR; JG0163; JG0163.
DR RefSeq; NP_072131.1; NM_022609.2.
DR AlphaFoldDB; Q9Z137; -.
DR SMR; Q9Z137; -.
DR STRING; 10116.ENSRNOP00000063982; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; Q9Z137; 2 sites.
DR PaxDb; Q9Z137; -.
DR PRIDE; Q9Z137; -.
DR Ensembl; ENSRNOT00000075592; ENSRNOP00000063982; ENSRNOG00000046852.
DR GeneID; 64544; -.
DR KEGG; rno:64544; -.
DR CTD; 135152; -.
DR RGD; 620903; B3gat2.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000159583; -.
DR InParanoid; Q9Z137; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q9Z137; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9Z137; -.
DR Proteomes; UP000002494; Chromosome 9.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IMP:RGD.
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 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..324
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 2"
FT /id="PRO_0000195174"
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..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 34..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 324 AA; 37220 MW; 6283C29535B5D00E CRC64;
MKSALCNRFF ILLPWILIVI IMLDVDPRRP APQLTSRPYF SPHTVGCGGS RVPLRRSSPG
RDAAEKRNES RPQLQPEPRL PTIYAITPTY SRPVQKAELT RLANTFRQVA QLHWILVEDR
ATRSELVSSF LARAGLPNTH LHVPTPRRYK RPWLPRATEQ RNAGLAWLRQ RHQHQSAQPG
VLFFADDDNT YSLELFQEMR TTRKVSVWPV GLVGGRRYER PLVKNGKVVG WYTGWREDRP
FAIDMAGFAV SLQVILSNPK AVFKRRGSQP GMQESDFLKQ ITTVDELEPK ANNCTKVLVW
HTRTEKVNLA NEPKYHMDTV NIEV
