B3GT4_MOUSE
ID B3GT4_MOUSE Reviewed; 371 AA.
AC Q9Z0F0; Q91VC1; Q920U8; Q920U9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Beta-1,3-galactosyltransferase 4 {ECO:0000305};
DE Short=Beta-1,3-GalTase 4;
DE Short=Beta3Gal-T4;
DE Short=Beta3GalT4;
DE Short=b3Gal-T4;
DE EC=2.4.1.62 {ECO:0000269|PubMed:10502288};
DE AltName: Full=Gal-T2;
DE AltName: Full=Ganglioside galactosyltransferase;
DE AltName: Full=UDP-galactose:beta-N-acetyl-galactosamine-beta-1,3-galactosyltransferase;
GN Name=B3galt4 {ECO:0000312|MGI:MGI:1859517};
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetus;
RX PubMed=10502288;
RX DOI=10.1002/(sici)1097-4547(19991015)58:2<318::aid-jnr12>3.0.co;2-u;
RA Daniotti J.L., Martina J.A., Zurita A.R., Maccioni H.J.F.;
RT "Mouse beta 1,3-galactosyltransferase (GA1/GM1/GD1b synthase): protein
RT characterization, tissue expression, and developmental regulation in neural
RT retina.";
RL J. Neurosci. Res. 58:318-327(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M.,
RA Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.;
RT "Sequence of the mouse major histocompatibility complex class II region.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-370.
RC STRAIN=BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/EiJ, HMI/Msf, MSM/Msf,
RC NJL/Msf, Pgn2, and SWN/Msf;
RA Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.;
RT "Conspicuous differences among gene genealogies of 21 nuclear genes of five
RT Mus musculus subspecies.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
CC {ECO:0000269|PubMed:10502288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 (d18:1(4E)) + UDP-alpha-D-galactose =
CC ganglioside GM1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16773,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:71502, ChEBI:CHEBI:77709; EC=2.4.1.62;
CC Evidence={ECO:0000269|PubMed:10502288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16774;
CC Evidence={ECO:0000305|PubMed:10502288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 + UDP-alpha-D-galactose = ganglioside GM1 +
CC H(+) + UDP; Xref=Rhea:RHEA:48280, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:79218,
CC ChEBI:CHEBI:82639; Evidence={ECO:0000269|PubMed:10502288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48281;
CC Evidence={ECO:0000305|PubMed:10502288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD2 (d18:1(4E)) + UDP-alpha-D-galactose =
CC ganglioside GD1b (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:47568,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:78542, ChEBI:CHEBI:87785;
CC Evidence={ECO:0000250|UniProtKB:O88178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47569;
CC Evidence={ECO:0000250|UniProtKB:O88178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA2 (d18:1(4E)) + UDP-alpha-D-galactose =
CC ganglioside GA1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41960,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27731, ChEBI:CHEBI:27938,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914;
CC Evidence={ECO:0000250|UniProtKB:O88178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41961;
CC Evidence={ECO:0000250|UniProtKB:O88178};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:10502288}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, kidney, lung and
CC testis. {ECO:0000269|PubMed:10502288}.
CC -!- DEVELOPMENTAL STAGE: First expressed at embryonic day 3. Maintained at
CC high levels between days 4 and 7 and declines thereafter to stabilize
CC at low levels after day 10. {ECO:0000269|PubMed:10502288}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b3GalT4;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_457";
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DR EMBL; AF082504; AAC69622.1; -; mRNA.
DR EMBL; AF110520; AAC97977.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69897.1; -; Genomic_DNA.
DR EMBL; AB039164; BAB68688.1; -; Genomic_DNA.
DR EMBL; AB039165; BAB68689.1; -; Genomic_DNA.
DR EMBL; AB039167; BAB68691.1; -; Genomic_DNA.
DR EMBL; AB039168; BAB68692.1; -; Genomic_DNA.
DR EMBL; AB039170; BAB68694.1; -; Genomic_DNA.
DR EMBL; AB039171; BAB68695.1; -; Genomic_DNA.
DR EMBL; AB039172; BAB68696.1; -; Genomic_DNA.
DR EMBL; AB039169; BAB68693.1; -; Genomic_DNA.
DR EMBL; AB039166; BAB68690.1; -; Genomic_DNA.
DR CCDS; CCDS28638.1; -.
DR RefSeq; NP_062293.1; NM_019420.2.
DR AlphaFoldDB; Q9Z0F0; -.
DR SMR; Q9Z0F0; -.
DR STRING; 10090.ENSMUSP00000084823; -.
DR SwissLipids; SLP:000001417; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9Z0F0; 1 site.
DR PhosphoSitePlus; Q9Z0F0; -.
DR MaxQB; Q9Z0F0; -.
DR PaxDb; Q9Z0F0; -.
DR PRIDE; Q9Z0F0; -.
DR ProteomicsDB; 277169; -.
DR Antibodypedia; 29042; 121 antibodies from 25 providers.
DR DNASU; 54218; -.
DR Ensembl; ENSMUST00000087543; ENSMUSP00000084823; ENSMUSG00000067370.
DR GeneID; 54218; -.
DR KEGG; mmu:54218; -.
DR UCSC; uc008caj.2; mouse.
DR CTD; 8705; -.
DR MGI; MGI:1859517; B3galt4.
DR VEuPathDB; HostDB:ENSMUSG00000067370; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000161798; -.
DR HOGENOM; CLU_036849_1_0_1; -.
DR InParanoid; Q9Z0F0; -.
DR OMA; RCRVIAW; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q9Z0F0; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.62; 3474.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 54218; 10 hits in 76 CRISPR screens.
DR PRO; PR:Q9Z0F0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z0F0; protein.
DR Bgee; ENSMUSG00000067370; Expressed in pyloric antrum and 172 other tissues.
DR ExpressionAtlas; Q9Z0F0; baseline and differential.
DR Genevisible; Q9Z0F0; MM.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047915; F:ganglioside galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0001574; P:ganglioside biosynthetic process; ISO:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..371
FT /note="Beta-1,3-galactosyltransferase 4"
FT /id="PRO_0000219161"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..371
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 248
FT /note="W -> R (in strain: pgn2)"
FT VARIANT 344
FT /note="G -> W (in strain: BLG2/Msf)"
SQ SEQUENCE 371 AA; 41236 MW; 323A7FFA56B723B3 CRC64;
MPLSLFRRVL LAVLLLVIIW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLISN
SHACGGSGPP PFLLILVCTA PEHLNQRNAI RASWGAIREA RGFRVQTLFL LGKPRRQQLA
DLSSESAAHR DILQASFQDS YRNLTLKTLS GLNWVNKYCP MARYILKTDD DVYVNVPELV
SELIQRGGPS EQWQKGKEAQ EETTAIHEEH RGQAVPLLYL GRVHWRVRPT RTPESRHHVS
EELWPENWGP FPPYASGTGY VLSISAVQLI LKVASRAPPL PLEDVFVGVS ARRGGLAPTH
CVKLAGATHY PLDRCCYGKF LLTSHKVDPW QMQEAWKLVS GMNGERTAPF CSWLQGFLGT
LRCRFIAWFS S
