B4GN1_RAT
ID B4GN1_RAT Reviewed; 533 AA.
AC Q10468;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Beta-1,4 N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE EC=2.4.1.92 {ECO:0000269|PubMed:3140234, ECO:0000269|PubMed:7980468};
DE AltName: Full=(N-acetylneuraminyl)-galactosylglucosylceramide;
DE AltName: Full=GA2 synthase {ECO:0000303|PubMed:3140234};
DE EC=2.4.1.- {ECO:0000269|PubMed:3140234};
DE AltName: Full=GD2 synthase {ECO:0000303|PubMed:3140234};
DE EC=2.4.1.- {ECO:0000269|PubMed:3140234};
DE AltName: Full=GM2 synthase {ECO:0000303|PubMed:3140234};
DE EC=2.4.1.92 {ECO:0000269|PubMed:3140234};
DE AltName: Full=GalNAc-T {ECO:0000303|PubMed:1606358, ECO:0000303|PubMed:3140234};
GN Name=B4galnt1 {ECO:0000312|RGD:620490}; Synonyms=Galgt, Galgt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=7980468; DOI=10.1042/bj3030957;
RA Hidari J.K., Ichikawa S., Furukawa K., Yamasaki M., Hirabayashi Y.;
RT "Beta-1,4-N-acetylgalactosaminyltransferase can synthesize both
RT asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and in vivo:
RT isolation and characterization of a beta-1,4-N-
RT acetylgalactosaminyltransferase cDNA clone from rat ascites hepatoma cell
RT line AH7974F.";
RL Biochem. J. 303:957-965(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3140234; DOI=10.1073/pnas.85.19.7044;
RA Pohlentz G., Klein D., Schwarzmann G., Schmitz D., Sandhoff K.;
RT "Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases are
RT single enzymes in Golgi vesicles from rat liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7044-7048(1988).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1606358; DOI=10.1093/glycob/2.2.137;
RA Iber H., Zacharias C., Sandhoff K.;
RT "The c-series gangliosides GT3, GT2 and GP1c are formed in rat liver Golgi
RT by the same set of glycosyltransferases that catalyse the biosynthesis of
RT asialo-, a- and b-series gangliosides.";
RL Glycobiology 2:137-142(1992).
CC -!- FUNCTION: Involved in the biosynthesis of gangliosides GM2, GD2, GT2
CC and GA2 from GM3, GD3, GT3 and GA3, respectively.
CC {ECO:0000269|PubMed:1606358, ECO:0000269|PubMed:3140234,
CC ECO:0000269|PubMed:7980468}.
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:3140234, ECO:0000269|PubMed:7980468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12589;
CC Evidence={ECO:0000269|PubMed:3140234, ECO:0000269|PubMed:7980468};
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:0000269|PubMed:7980468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41817;
CC Evidence={ECO:0000269|PubMed:7980468};
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:0000269|PubMed:1606358, ECO:0000269|PubMed:7980468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43269;
CC Evidence={ECO:0000269|PubMed:1606358, ECO:0000269|PubMed:7980468};
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:0000269|PubMed:7980468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43273;
CC Evidence={ECO:0000269|PubMed:7980468};
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:0000269|PubMed:7980468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43277;
CC Evidence={ECO:0000269|PubMed:7980468};
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:0000269|PubMed:1606358};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47581;
CC Evidence={ECO:0000269|PubMed:1606358};
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:0000269|PubMed:3140234};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47565;
CC Evidence={ECO:0000269|PubMed:3140234};
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:0000269|PubMed:7980468};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43301;
CC Evidence={ECO:0000269|PubMed:7980468};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=117 uM for GM3 {ECO:0000269|PubMed:3140234};
CC KM=68 uM for GD3 {ECO:0000269|PubMed:3140234};
CC KM=437 uM for lactosylceramide {ECO:0000269|PubMed:3140234};
CC KM=47 uM for GM3 {ECO:0000269|PubMed:1606358};
CC KM=45 uM for GT3 {ECO:0000269|PubMed:1606358};
CC Vmax=6.2 nmol/h/mg enzyme toward GM3 {ECO:0000269|PubMed:3140234};
CC Vmax=3.9 nmol/h/mg enzyme toward GD3 {ECO:0000269|PubMed:3140234};
CC Vmax=0.7 nmol/h/mg enzyme toward lactosylceramide
CC {ECO:0000269|PubMed:3140234};
CC Vmax=1.5 nmol/h/mg enzyme toward GM3 {ECO:0000269|PubMed:1606358};
CC Vmax=0.8 nmol/h/mg enzyme toward GT3 {ECO:0000269|PubMed:1606358};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:1606358,
CC ECO:0000269|PubMed:3140234, ECO:0000269|PubMed:7980468}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:1606358, ECO:0000269|PubMed:3140234}; Single-pass
CC type II membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain, testis, spleen, and to
CC a lesser extent in liver. {ECO:0000269|PubMed:1606358,
CC ECO:0000269|PubMed:3140234, ECO:0000269|PubMed:7980468}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; D17809; BAA04632.1; -; mRNA.
DR EMBL; BC081799; AAH81799.1; -; mRNA.
DR PIR; S53320; S53320.
DR RefSeq; NP_074051.1; NM_022860.2.
DR RefSeq; XP_017450589.1; XM_017595100.1.
DR AlphaFoldDB; Q10468; -.
DR STRING; 10116.ENSRNOP00000048586; -.
DR SwissLipids; SLP:000000769; -.
DR CAZy; GT12; Glycosyltransferase Family 12.
DR GlyGen; Q10468; 2 sites.
DR PaxDb; Q10468; -.
DR GeneID; 64828; -.
DR KEGG; rno:64828; -.
DR UCSC; RGD:620490; rat.
DR CTD; 2583; -.
DR RGD; 620490; B4galnt1.
DR VEuPathDB; HostDB:ENSRNOG00000004839; -.
DR eggNOG; ENOG502QTK7; Eukaryota.
DR HOGENOM; CLU_036051_0_0_1; -.
DR InParanoid; Q10468; -.
DR OMA; RRFYPTI; -.
DR PhylomeDB; Q10468; -.
DR TreeFam; TF332297; -.
DR BRENDA; 2.4.1.92; 5301.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR PRO; PR:Q10468; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004839; Expressed in thymus and 20 other tissues.
DR Genevisible; Q10468; RN.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0003947; F:(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IDA:UniProtKB.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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_0000059102"
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 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"
SQ SEQUENCE 533 AA; 59279 MW; 43EF653FB07EA651 CRC64;
MRLDRRALYA LVLLLACASL GLLYASTRDA PGLPNPLALW SPPQGPPRLD LLDLATEPRY
AHIPVRIKEQ VVGLLAQNNC SCESSGGRFA LPFLRQVRAI DFTKAFDAEE LRAVSISREQ
EYQAFLARSR SLADQLLIAP ANSPLQYPLQ GVEVQPLRSI LVPGLSLQEA SVQEIYQVNL
IASLGTWDVA GEVTGVTLTG EGQSDLTLAS PILDKLNRQL QLVTYSSRSY QANTADTVRF
STKGHEVAFT ILIRHPPNPR LYPPSSLPQG AQYNISALVT VATKTFLRYD RLRALIASIR
RFYPTVTIVI ADDSDKPERI SDPHVEHYFM PFGKGWFAGR NLAVSQVTTK YVLWVDDDFV
FTARTRLEKL VDVLERTPLD LVGGAVREIS GYATTYRQLL SVEPGAPGFG NCLRQKQGFH
HELAGFPNCV VTDGVVNFFL ARTDKVRQVG FDPRLNRVAH LEFFLDGLGS LRVGSCSDVV
VDHASKVKLP WTSKDPGAEL YARYRYPGSL DQSQVAKHRL LFFKHRLQCM TAE
