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   24-JAN-2024, entry version 81.
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   SMR; Q5R4S2; -.
DR   STRING; 9601.ENSPPYP00000004686; -.
DR   CAZy; GT49; Glycosyltransferase Family 49.
DR   GlyCosmos; Q5R4S2; 2 sites, No reported glycans.
DR   Ensembl; ENSPPYT00000004871.2; ENSPPYP00000004686.2; ENSPPYG00000004108.2.
DR   GeneID; 100173924; -.
DR   KEGG; pon:100173924; -.
DR   CTD; 11041; -.
DR   eggNOG; KOG3765; Eukaryota.
DR   GeneTree; ENSGT00940000157679; -.
DR   InParanoid; Q5R4S2; -.
DR   OMA; HQQFLAM; -.
DR   OrthoDB; 3517330at2759; -.
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: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; BETA-1,4-GLUCURONYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR46420:SF1; BETA-1,4-GLUCURONYLTRANSFERASE 1; 1.
DR   Pfam; PF13896; Glyco_transf_49; 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
//