B4GA1_BOVIN
ID B4GA1_BOVIN Reviewed; 415 AA.
AC Q5EA01; Q3MHK2; Q58DG2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 109.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46482.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT020768; AAX08785.1; -; mRNA.
DR EMBL; BT021635; AAX46482.1; ALT_FRAME; mRNA.
DR EMBL; BC105206; AAI05207.1; -; mRNA.
DR RefSeq; NP_001029980.1; NM_001034808.1.
DR AlphaFoldDB; Q5EA01; -.
DR STRING; 9913.ENSBTAP00000030011; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR PaxDb; Q5EA01; -.
DR PRIDE; Q5EA01; -.
DR Ensembl; ENSBTAT00000030023; ENSBTAP00000030011; ENSBTAG00000022238.
DR GeneID; 618055; -.
DR KEGG; bta:618055; -.
DR CTD; 11041; -.
DR VEuPathDB; HostDB:ENSBTAG00000022238; -.
DR VGNC; VGNC:26395; B4GAT1.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000157679; -.
DR HOGENOM; CLU_019238_5_0_1; -.
DR InParanoid; Q5EA01; -.
DR OMA; HQQFLAM; -.
DR OrthoDB; 729091at2759; -.
DR TreeFam; TF319168; -.
DR Reactome; R-BTA-2022854; Keratan sulfate biosynthesis.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000022238; Expressed in Ammon's horn and 102 other tissues.
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_0000080554"
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"
FT CONFLICT 178
FT /note="L -> P (in Ref. 1; AAI05207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47231 MW; 1B0FB74C8F8266C2 CRC64;
MQMSYAIRCA FYQLLLAALM LVAMLQLLYL SLLSGLHGQE EQDQYFEFFP PSPRSVDQVK
AQLRTALASG GVLDASGDYR VYRGLLKTTM DPNDVILATH ASVDNLLHLS GLLERWEGPL
SVSVFAATKE EAQLATVLTY ALSSHCPDMR ARVAMHLVCP SRYEAAVPDP REPGEFALLR
SCQEVFDKLA RVAQPGVNYA LGTNVSYPNN LLRNLAREGA NYALVIDVDM VPSEGLWRSL
REMLDQSKQW AGTALVVPAF EIRRARRMPM NKNELLQLYQ VGEVRPFYYG LCTPCQAPTN
YSRWVNLPEE TLLRPAYVVP WQDPWEPFYV AGGKVPTFDE RFRQYGFNRI SQACELHVAG
FDFEVLNEGF LVHKGFKEVL KFHPQKEAEN QHNKILYRQF KQELKAKYPD SPRHC
