B4GA1_PONAB
ID B4GA1_PONAB Reviewed; 415 AA.
AC Q5R4S2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Beta-1,4-glucuronyltransferase 1 {ECO:0000250|UniProtKB:O43505};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:O43505};
DE AltName: Full=I-beta-1,3-N-acetylglucosaminyltransferase;
DE Short=iGnT;
DE AltName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase;
DE AltName: Full=Poly-N-acetyllactosamine extension enzyme;
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1;
GN Name=B4GAT1 {ECO:0000250|UniProtKB:O43505}; Synonyms=B3GNT1, B3GNT6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of
CC alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue
CC onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-
CC beta disaccharide primer, which is further elongated by LARGE1, during
CC synthesis of phosphorylated O-mannosyl glycan. Phosphorylated O-
CC mannosyl glycan is a carbohydrate structure present in alpha-
CC dystroglycan (DAG1), which is required for binding laminin G-like
CC domain-containing extracellular proteins with high affinity. Required
CC for axon guidance; via its function in O-mannosylation of alpha-
CC dystroglycan (DAG1). {ECO:0000250|UniProtKB:O43505,
CC ECO:0000250|UniProtKB:Q8BWP8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-
CC alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-
CC ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-
CC alpha-D-Man)]-Thr-[protein] + H(+) + UDP; Xref=Rhea:RHEA:46860,
CC Rhea:RHEA-COMP:15023, Rhea:RHEA-COMP:17482, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:142405,
CC ChEBI:CHEBI:177336; Evidence={ECO:0000250|UniProtKB:O43505};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O43505};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:O43505, ECO:0000250|UniProtKB:Q8BWP8}.
CC -!- SUBUNIT: Interacts with LARGE1 and LARGE2.
CC {ECO:0000250|UniProtKB:O43505}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O43505, ECO:0000250|UniProtKB:Q8BWP8}; Single-
CC pass type II membrane protein. Note=Localizes near the trans-Golgi
CC apparatus. {ECO:0000250|UniProtKB:O43505}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 49 family.
CC {ECO:0000305}.
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DR EMBL; CR861172; CAH93244.1; -; mRNA.
DR RefSeq; NP_001126908.1; NM_001133436.1.
DR AlphaFoldDB; Q5R4S2; -.
DR STRING; 9601.ENSPPYP00000004686; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR Ensembl; ENSPPYT00000004871; ENSPPYP00000004686; ENSPPYG00000004108.
DR GeneID; 100173924; -.
DR KEGG; pon:100173924; -.
DR CTD; 11041; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000157679; -.
DR InParanoid; Q5R4S2; -.
DR OrthoDB; 729091at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR InterPro; IPR043189; B4GAT1.
DR PANTHER; PTHR46420; PTHR46420; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..415
FT /note="Beta-1,4-glucuronyltransferase 1"
FT /id="PRO_0000080557"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..415
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O43505"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O43505"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 47149 MW; E73C1299D8F34CE2 CRC64;
MQMSYAIRCA FYQLLLAALM LVAMLQLLYL SLLSGLHGQE EQDQYFEFFP PSPRSVDQVK
TQLRTALASG GVLDASGDYR VYRGLLKTTM DPNDVILATH ASVDNLLHLS GLLERWEGPL
SVSVFAATKE EAQLATVLAY ALSSHCPDMR ARVAMHLVCP SRYEAAVPDP REPGEFALLR
SCQEVFDKLA RVAQPGINYA LGTNVSYPNN LLRNLAREGA NYALVIDVDM VPSEGLWRGL
REMLDQSNQW GGTALVVPAF EIRRARRMPM NKNELVQLYQ VGEVRPFYYG LCTPCQAPTN
YSRWVNLPEE SLLRPAYVVP WQDPWEPFYV AGGKVPTFDE RFRQYGFNRI SQACELHVAG
FDFEVLNEGF LVHKGFKEAL KFHPQKEAEN QHNKILYRQF KQELKAKYPN SPRRC
