B4GA1_MOUSE
ID B4GA1_MOUSE Reviewed; 415 AA.
AC Q8BWP8; Q3TY43; Q8BJH9; Q99LW7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Beta-1,4-glucuronyltransferase 1 {ECO:0000250|UniProtKB:O43505};
DE EC=2.4.1.- {ECO:0000269|PubMed:23217742, ECO:0000269|PubMed:25279699};
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver, Spinal ganglion, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP MET-155, AND CATALYTIC ACTIVITY.
RX PubMed=23217742; DOI=10.1016/j.neuron.2012.10.009;
RA Wright K.M., Lyon K.A., Leung H., Leahy D.J., Ma L., Ginty D.D.;
RT "Dystroglycan organizes axon guidance cue localization and axonal
RT pathfinding.";
RL Neuron 76:931-944(2012).
RN [5]
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=25279699; DOI=10.7554/elife.03941;
RA Willer T., Inamori K.I., Venzke D., Harvey C., Morgensen G., Hara Y.,
RA Beltran Valero de Bernabe D., Yu L., Wright K.M., Campbell K.P.;
RT "The glucuronyltransferase B4GAT1 is required for initiation of LARGE-
RT mediated alpha-dystroglycan functional glycosylation.";
RL Elife 3:0-0(2014).
CC -!- FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of
CC alpha-dystroglycan (DAG1) (PubMed:23217742, PubMed:25279699). Transfers
CC a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to
CC produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which
CC is further elongated by LARGE1, during synthesis of phosphorylated O-
CC mannosyl glycan (PubMed:25279699). Phosphorylated O-mannosyl glycan is
CC a carbohydrate structure present in alpha-dystroglycan (DAG1), which is
CC required for binding laminin G-like domain-containing extracellular
CC proteins with high affinity (PubMed:25279699). Required for axon
CC guidance; via its function in O-mannosylation of alpha-dystroglycan
CC (DAG1) (PubMed:23217742). {ECO:0000269|PubMed:23217742,
CC ECO:0000269|PubMed:25279699}.
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:23217742,
CC ECO:0000269|PubMed:25279699};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O43505};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:25279699}.
CC -!- SUBUNIT: Interacts with LARGE1 and LARGE2.
CC {ECO:0000250|UniProtKB:O43505}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23217742}; Single-pass type II membrane protein.
CC Note=Localizes near the trans-Golgi apparatus.
CC {ECO:0000250|UniProtKB:O43505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BWP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BWP8-2; Sequence=VSP_014004, VSP_014005;
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality.
CC {ECO:0000269|PubMed:23217742}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 49 family.
CC {ECO:0000305}.
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DR EMBL; AK050347; BAC34203.1; -; mRNA.
DR EMBL; AK083857; BAC39041.1; -; mRNA.
DR EMBL; AK158899; BAE34720.1; -; mRNA.
DR EMBL; BC002191; AAH02191.1; -; mRNA.
DR EMBL; BC069927; AAH69927.1; -; mRNA.
DR CCDS; CCDS29446.1; -. [Q8BWP8-1]
DR RefSeq; NP_780592.1; NM_175383.2. [Q8BWP8-1]
DR AlphaFoldDB; Q8BWP8; -.
DR BioGRID; 224461; 1.
DR STRING; 10090.ENSMUSP00000062016; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR GlyGen; Q8BWP8; 2 sites.
DR iPTMnet; Q8BWP8; -.
DR PhosphoSitePlus; Q8BWP8; -.
DR SwissPalm; Q8BWP8; -.
DR EPD; Q8BWP8; -.
DR MaxQB; Q8BWP8; -.
DR PaxDb; Q8BWP8; -.
DR PeptideAtlas; Q8BWP8; -.
DR PRIDE; Q8BWP8; -.
DR ProteomicsDB; 273646; -. [Q8BWP8-1]
DR ProteomicsDB; 273647; -. [Q8BWP8-2]
DR DNASU; 108902; -.
DR Ensembl; ENSMUST00000053705; ENSMUSP00000062016; ENSMUSG00000047379. [Q8BWP8-1]
DR Ensembl; ENSMUST00000235776; ENSMUSP00000157645; ENSMUSG00000047379. [Q8BWP8-2]
DR Ensembl; ENSMUST00000236560; ENSMUSP00000158273; ENSMUSG00000117789. [Q8BWP8-1]
DR GeneID; 108902; -.
DR KEGG; mmu:108902; -.
DR UCSC; uc008gbx.1; mouse. [Q8BWP8-1]
DR CTD; 11041; -.
DR MGI; MGI:1919680; B4gat1.
DR VEuPathDB; HostDB:ENSMUSG00000047379; -.
DR VEuPathDB; HostDB:ENSMUSG00000117789; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000157679; -.
DR HOGENOM; CLU_019238_5_0_1; -.
DR InParanoid; Q8BWP8; -.
DR OMA; HQQFLAM; -.
DR OrthoDB; 729091at2759; -.
DR PhylomeDB; Q8BWP8; -.
DR TreeFam; TF319168; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-5173105; O-linked glycosylation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 108902; 1 hit in 71 CRISPR screens.
DR ChiTaRS; B4gat1; mouse.
DR PRO; PR:Q8BWP8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BWP8; protein.
DR Bgee; ENSMUSG00000047379; Expressed in hypothalamus and 81 other tissues.
DR Genevisible; Q8BWP8; MM.
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; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; IMP:MGI.
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 Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..415
FT /note="Beta-1,4-glucuronyltransferase 1"
FT /id="PRO_0000080556"
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 VAR_SEQ 353..379
FT /note="ACELHVAGFNFEVLNEGFLVHKGFKEA -> VLKRERACRTKTGGVSGVKWP
FT LVERRQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014004"
FT VAR_SEQ 380..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014005"
FT MUTAGEN 155
FT /note="M->T: Mild muscular dystrophy phenotype of variable
FT penetrance due to defects in axon guidance. Mislocalization
FT to the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:23217742"
FT CONFLICT 175..176
FT /note="EF -> RV (in Ref. 2; AAH02191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47384 MW; 7B74BEB591EAA4DC CRC64;
MQMSYAIRCA FYQLLLAALM LVAMLQLLYL SLLSGLHGQE EQEQYFEFFP PSPRSVDQVK
SQLRTALASG GVLDASGDYR VYRGLLKTTM DPNDVILATH ASVDNLLHLS GLLERWEGPL
SVSVFAATKE EAQLATVLAY ALSSHCPEMR ARVAMHLVCP SRYEAAVPDP REPGEFALLR
SCQEVFDKLA RVAQPGINYA LGTNTSYPNN LLRNLAREEA NYALVIDVDM VPSEGLWRGL
REMLDQSNHW DGTALVVPAF EIRRSRRMPM NKNELVQLYQ VGEVRPFYYG LCTPCHAPTN
YSRWVNLPEE SLLRPAYVVP WRDPWEPFYV AGGKVPTFDE RFRQYGFNRI SQACELHVAG
FNFEVLNEGF LVHKGFKEAL KFHPQKEAEN QRNKILYRQF KQELKARYPN SPHRC
