B4GN1_MOUSE
ID B4GN1_MOUSE Reviewed; 533 AA.
AC Q09200;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Beta-1,4 N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE EC=2.4.1.92 {ECO:0000269|PubMed:8855236};
DE AltName: Full=(N-acetylneuraminyl)-galactosylglucosylceramide;
DE AltName: Full=GM2/GD2 synthase {ECO:0000303|PubMed:8855236};
DE AltName: Full=GalNAc-T;
GN Name=B4galnt1 {ECO:0000312|MGI:MGI:1342057}; Synonyms=Galgt, Galgt1, Ggm2;
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 [MRNA].
RX PubMed=7821435; DOI=10.1016/0014-5793(94)01395-h;
RA Takamiya K., Yamamoto A., Yamashiro S., Furukawa K., Haraguchi M.,
RA Okada M., Ikeda T., Shiku H., Furukawa K.;
RT "T cell receptor-mediated stimulation of mouse thymocytes induces up-
RT regulation of the GM2/GD2 synthase gene.";
RL FEBS Lett. 358:79-83(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Neonatal brain;
RX PubMed=7558008; DOI=10.1006/geno.1995.1058;
RA Sango K., Johnson O.N., Kozak C.A., Proia R.L.;
RT "Beta-1,4-N-acetylgalactosaminyltransferase involved in ganglioside
RT synthesis: cDNA sequence, expression, and chromosome mapping of the mouse
RT gene.";
RL Genomics 27:362-365(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
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 [4]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8855236; DOI=10.1073/pnas.93.20.10662;
RA Takamiya K., Yamamoto A., Furukawa K., Yamashiro S., Shin M., Okada M.,
RA Fukumoto S., Haraguchi M., Takeda N., Fujimura K., Sakae M., Kishikawa M.,
RA Shiku H., Furukawa K., Aizawa S.;
RT "Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides but
RT exhibit only subtle defects in their nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10662-10667(1996).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15953602; DOI=10.1016/j.expneurol.2005.04.017;
RA Pan B., Fromholt S.E., Hess E.J., Crawford T.O., Griffin J.W., Sheikh K.A.,
RA Schnaar R.L.;
RT "Myelin-associated glycoprotein and complementary axonal ligands,
RT gangliosides, mediate axon stability in the CNS and PNS: neuropathology and
RT behavioral deficits in single- and double-null mice.";
RL Exp. Neurol. 195:208-217(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Spleen;
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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=21483489; DOI=10.1371/journal.ppat.1002008;
RA Peng L., Tepp W.H., Johnson E.A., Dong M.;
RT "Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides
RT as receptors.";
RL PLoS Pathog. 7:E1002008-E1002008(2011).
CC -!- FUNCTION: Involved in the biosynthesis of gangliosides GM2, GD2 and
CC GA2. {ECO:0000269|PubMed:8855236}.
CC -!- FUNCTION: Involved in the biosynthesis of gangliosides GM2, GD2, GT2
CC and GA2 from GM3, GD3, GT3 and GA3, respectively.
CC {ECO:0000250|UniProtKB:Q10468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = ganglioside GM2 (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:12588, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60065, ChEBI:CHEBI:67138, ChEBI:CHEBI:71502; EC=2.4.1.92;
CC Evidence={ECO:0000269|PubMed:8855236};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12589;
CC Evidence={ECO:0000305|PubMed:8855236};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = ganglioside GD2 (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:41816, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:78436, ChEBI:CHEBI:78542;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41817;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM3 + UDP-N-acetyl-alpha-D-galactosamine =
CC ganglioside GM2 + H(+) + UDP; Xref=Rhea:RHEA:43268,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:79210, ChEBI:CHEBI:79218;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43269;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD3 + UDP-N-acetyl-alpha-D-galactosamine =
CC ganglioside GD2 + H(+) + UDP; Xref=Rhea:RHEA:43272,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:79214, ChEBI:CHEBI:79220;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43273;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1a + UDP-N-acetyl-alpha-D-galactosamine =
CC ganglioside GalNAc-GD1a + H(+) + UDP; Xref=Rhea:RHEA:43276,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:82637, ChEBI:CHEBI:82945;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43277;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GT3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = ganglioside GT2 (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:47580, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:78438, ChEBI:CHEBI:87788;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47581;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-
CC acetyl-alpha-D-galactosamine = ganglioside GA2 (d18:1(4E)) + H(+) +
CC UDP; Xref=Rhea:RHEA:47564, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:27731, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47565;
CC Evidence={ECO:0000250|UniProtKB:Q00973,
CC ECO:0000250|UniProtKB:Q10468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC glucosyl-(1<->1')-ceramide + UDP-N-acetyl-alpha-D-galactosamine =
CC H(+) + N-acetyl-beta-D-galactosaminyl-(1->4)-[alpha-N-
CC glycoloylneuraminosyl-(2->3)]-beta-D-galactosyl-(1->4)-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-ceramide + UDP; Xref=Rhea:RHEA:43300, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:82950,
CC ChEBI:CHEBI:82951; Evidence={ECO:0000250|UniProtKB:Q10468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43301;
CC Evidence={ECO:0000250|UniProtKB:Q10468};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:8855236}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q10468}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Most abundant in brain, liver, lung, spleen and
CC testis. {ECO:0000269|PubMed:7558008}.
CC -!- DEVELOPMENTAL STAGE: Highest at day 7 of embryonic development after
CC which it declines to its lowest levels at day 11 before increasing
CC again. {ECO:0000269|PubMed:7558008}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, excepting a slight decrease
CC in neural conduction velocity from the tibial nerve to the
CC somatosensory cortex (PubMed:8855236). Mutant mice display impaired
CC motor coordination and balance (PubMed:15953602). Sciatic nerves from
CC over three month old mutant mice show signs of Wallerian degeneration,
CC with redundant myelin, degeneration of myelinated fibers, axon
CC dysmyelination, and an apparent decrease in the diameter of myelinated
CC axons (PubMed:15953602). The distances between neurofilaments in
CC myelinated axons from over 3 month old mice are shorter than normal
CC (PubMed:15953602). Mice are less sensitive to C.botulinum neurotoxin
CC type C (BoNT/C), C.botulinum neurotoxin type D (BoNT/D, botD) and
CC C.botulinum neurotoxin type F (BoNT/F, botF) (PubMed:21483489).
CC {ECO:0000269|PubMed:15953602, ECO:0000269|PubMed:21483489,
CC ECO:0000269|PubMed:8855236}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4
CC N-acetylgalactosaminyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_506";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L25885; AAA65027.1; -; mRNA.
DR EMBL; U18975; AAA85496.1; -; mRNA.
DR EMBL; BC036996; AAH36996.1; -; mRNA.
DR EMBL; BC057199; AAH57199.1; -; mRNA.
DR CCDS; CCDS24230.1; -.
DR PIR; S78529; S78529.
DR RefSeq; NP_032106.1; NM_008080.5.
DR RefSeq; NP_082015.2; NM_027739.2.
DR RefSeq; XP_006513282.1; XM_006513219.3.
DR AlphaFoldDB; Q09200; -.
DR BioGRID; 199818; 1.
DR IntAct; Q09200; 1.
DR STRING; 10090.ENSMUSP00000006914; -.
DR CAZy; GT12; Glycosyltransferase Family 12.
DR GlyGen; Q09200; 3 sites.
DR iPTMnet; Q09200; -.
DR PhosphoSitePlus; Q09200; -.
DR EPD; Q09200; -.
DR PaxDb; Q09200; -.
DR PeptideAtlas; Q09200; -.
DR PRIDE; Q09200; -.
DR ProteomicsDB; 273590; -.
DR Antibodypedia; 2458; 258 antibodies from 30 providers.
DR DNASU; 14421; -.
DR Ensembl; ENSMUST00000006914; ENSMUSP00000006914; ENSMUSG00000006731.
DR GeneID; 14421; -.
DR KEGG; mmu:14421; -.
DR UCSC; uc007hic.2; mouse.
DR CTD; 2583; -.
DR MGI; MGI:1342057; B4galnt1.
DR VEuPathDB; HostDB:ENSMUSG00000006731; -.
DR eggNOG; ENOG502QTK7; Eukaryota.
DR GeneTree; ENSGT00390000006679; -.
DR HOGENOM; CLU_036051_0_0_1; -.
DR InParanoid; Q09200; -.
DR OMA; RRFYPTI; -.
DR OrthoDB; 363090at2759; -.
DR PhylomeDB; Q09200; -.
DR TreeFam; TF332297; -.
DR BRENDA; 2.4.1.92; 3474.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR BioGRID-ORCS; 14421; 6 hits in 77 CRISPR screens.
DR ChiTaRS; B4galnt1; mouse.
DR PRO; PR:Q09200; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q09200; protein.
DR Bgee; ENSMUSG00000006731; Expressed in small intestine Peyer's patch and 193 other tissues.
DR ExpressionAtlas; Q09200; baseline and differential.
DR Genevisible; Q09200; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003947; F:(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase activity; IMP:UniProtKB.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0019915; P:lipid storage; IGI:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR011143; GM2_synthase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR PIRSF; PIRSF000474; GM2_GD2_synthase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..533
FT /note="Beta-1,4 N-acetylgalactosaminyltransferase 1"
FT /id="PRO_0000059101"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..533
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80
FT /note="Interchain (with C-412)"
FT /evidence="ECO:0000250|UniProtKB:Q00973"
FT DISULFID 82
FT /note="Interchain (with C-529)"
FT /evidence="ECO:0000250|UniProtKB:Q00973"
FT DISULFID 412
FT /note="Interchain (with C-80)"
FT /evidence="ECO:0000250|UniProtKB:Q00973"
FT DISULFID 429..476
FT /evidence="ECO:0000250|UniProtKB:Q00973"
FT DISULFID 529
FT /note="Interchain (with C-82)"
FT /evidence="ECO:0000250|UniProtKB:Q00973"
FT CONFLICT 73
FT /note="G -> E (in Ref. 2; AAA85496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59212 MW; 6A15D81D2A68A28F CRC64;
MRLDRRALYA LVLLLACASL GLLYSSTRNA PSLPNPLALW SPPQGPPRLD LLDLAPEPRY
AHIPVRIKEQ VVGLLAQNNC SCESKGGSLP LPFLRQVRAV DLTKAFDAEE LRAVSVAREQ
EYQAFLARSR SLADQLLIAP ANSPLQYPLQ GVEVQPLRSI LVPGLSLQEA SVQEIYQVNL
SASLGTWDVA GEVTGVTLTG EGQPDLTLAS PVLDKLNRQL QLVTYSSRSY QANTADTVRF
STKGHEVAFT ILVRHPPNPR LYPPSSLPQG AEYNISALVT IATKTFLRYD RLRTLIASIR
RFYPTVTIVI ADDSDKPERI SDPHVEHYFM PFGKGWFAGR NLAVSQVTTK YVLWVDDDFV
FTARTRLEKL VDVLEKTPLD LVGGAVREIS GYATTYRQLL SVEPGAPGLG NCFRQKQGFH
HELVGFPSCV VTDGVVNFFL ARTDKVRQVG FDPRLNRVAH LEFFLDGLGF LRVGSCSDVV
VDHASKVKLP WTAKDPGAET YARYRYPGSL DQSQVAKHRL LFFKHRLQCM TAE
