B4GA1_DANRE
ID B4GA1_DANRE Reviewed; 431 AA.
AC L7YAI7; F1Q7L2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Beta-1,4-glucuronyltransferase 1 {ECO:0000250|UniProtKB:O43505};
DE EC=2.4.1.- {ECO:0000269|PubMed:23359570};
DE AltName: Full=I-beta-1,3-N-acetylglucosaminyltransferase;
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;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC
RP ACTIVITY.
RX PubMed=23359570; DOI=10.1093/hmg/ddt021;
RA Buysse K., Riemersma M., Powell G., van Reeuwijk J., Chitayat D.,
RA Roscioli T., Kamsteeg E.J., van den Elzen C., van Beusekom E., Blaser S.,
RA Babul-Hirji R., Halliday W., Wright G.J., Stemple D.L., Lin Y.Y.,
RA Lefeber D.J., van Bokhoven H.;
RT "Missense mutations in beta-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1)
RT cause Walker-Warburg syndrome.";
RL Hum. Mol. Genet. 22:1746-1754(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of
CC alpha-dystroglycan (DAG1) (PubMed:23359570). Transfers a glucuronic
CC acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the
CC glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further
CC elongated by LARGE, during synthesis of phosphorylated O-mannosyl
CC glycan (By similarity). Phosphorylated O-mannosyl glycan is a
CC carbohydrate structure present in alpha-dystroglycan (DAG1), which is
CC required for binding laminin G-like domain-containing extracellular
CC proteins with high affinity (By similarity). Required for axon
CC guidance; via its function in O-mannosylation of alpha-dystroglycan
CC (DAG1) (By similarity). {ECO:0000250|UniProtKB:O43505,
CC ECO:0000250|UniProtKB:Q8BWP8, ECO:0000269|PubMed:23359570}.
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:0000269|PubMed:23359570};
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 -!- 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 -!- DISRUPTION PHENOTYPE: Muscular defects and reduced alpha-dystroglycan
CC (dag1) glycosylation. {ECO:0000269|PubMed:23359570}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 49 family.
CC {ECO:0000305}.
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DR EMBL; KC136354; AGD94656.1; -; mRNA.
DR EMBL; BX324230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001265757.1; NM_001278828.1.
DR AlphaFoldDB; L7YAI7; -.
DR STRING; 7955.ENSDARP00000103038; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR PaxDb; L7YAI7; -.
DR Ensembl; ENSDART00000111708; ENSDARP00000103038; ENSDARG00000077583.
DR Ensembl; ENSDART00000182592; ENSDARP00000157274; ENSDARG00000111962.
DR GeneID; 101669768; -.
DR KEGG; dre:101669768; -.
DR CTD; 11041; -.
DR ZFIN; ZDB-GENE-121001-5; b4gat1.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000157679; -.
DR HOGENOM; CLU_019238_5_0_1; -.
DR OMA; HQQFLAM; -.
DR OrthoDB; 729091at2759; -.
DR TreeFam; TF319168; -.
DR Reactome; R-DRE-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-DRE-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR PRO; PR:L7YAI7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000077583; Expressed in presomitic mesoderm and 18 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:0006486; P:protein glycosylation; IMP:ZFIN.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR InterPro; IPR043189; B4GAT1.
DR PANTHER; PTHR46420; PTHR46420; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..431
FT /note="Beta-1,4-glucuronyltransferase 1"
FT /id="PRO_0000424020"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..431
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O43505"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O43505"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 431 AA; 49261 MW; 1EBEA1C01603F2C9 CRC64;
MHFSKKCSVF KVVLSALLIV ALLQLLYLSF LSKLHGKQQR YKYSELFGSK KNANQGEKNP
RREHLRYSLS TGGIFDGSGQ YRVYKNLIKS DFSTNQKPGA DPRSHHLALA THTTINNLHH
LESLLERWKN PISVAIFANG EDVKFATAII YALSLFCPQV QALVDFHLVC HSGEMATFPD
QDREHFVGLQ EMGCPAVFAK LESHRDKYKN YAIGSNVSYP NNLLRNVARG GTDAAYILVI
DIDMIPSANL HHQFVTMLMK REPAADEVLV LPAFEIRHIR KMPASKPELV QLYQVGEVRP
FYDELCSRCQ APTNYSLWVN LASKSSGPLE VSYTINWVDP WEPFYIGARS VPLYDESFRQ
YGFNRISQAC ELHIAGYRFS VVSNAFLLHK GFKVQGEFHS RKDEENRKNR ILFRSFKESL
KAKYPTSPRR C
