B3GT4_HUMAN
ID B3GT4_HUMAN Reviewed; 378 AA.
AC O96024;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
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=GalT4;
DE Short=b3Gal-T4;
DE EC=2.4.1.62 {ECO:0000269|PubMed:9582303};
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|HGNC:HGNC:919}; Synonyms=GALT4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=9582303; DOI=10.1074/jbc.273.21.12770;
RA Amado M., Almeida R., Carneiro F., Levery S.B., Holmes E.H., Nomoto M.,
RA Hollingsworth M.A., Hassan H., Schwientek T., Nielsen P.A., Bennett E.P.,
RA Clausen H.;
RT "A family of human beta3-galactosyltransferases. Characterization of four
RT members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-N-acetyl-
RT galactosamine beta-1,3-galactosyltransferase family.";
RL J. Biol. Chem. 273:12770-12778(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10663566; DOI=10.1007/s002510050012;
RA Shiina T., Kikkawa E., Iwasaki H., Kaneko M., Narimatsu H., Sasaki K.,
RA Bahram S., Inoko H.;
RT "The beta 1,3-galactosyltransferase-4 (b3Gal-T4) gene is located in the
RT centromeric segment of the human MHC class II region.";
RL Immunogenetics 51:75-78(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
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).
CC -!- FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
CC {ECO:0000269|PubMed:9582303}.
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:9582303};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16774;
CC Evidence={ECO:0000269|PubMed:9582303};
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:0000250|UniProtKB:Q9Z0F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48281;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F0};
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:0000250|UniProtKB:Q9Z0F0}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC pancreas and, to a lesser extent, in brain, placenta, kidney, liver and
CC lung. {ECO:0000269|PubMed:10663566, ECO:0000269|PubMed:9582303}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,3-
CC galactosyltransferase 4;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_431";
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DR EMBL; Y15061; CAA75345.1; -; mRNA.
DR EMBL; AL031228; CAA20230.1; -; Genomic_DNA.
DR EMBL; AB026730; BAA88988.1; -; mRNA.
DR EMBL; BC032574; AAH32574.1; -; mRNA.
DR CCDS; CCDS34425.1; -.
DR RefSeq; NP_003773.1; NM_003782.3.
DR AlphaFoldDB; O96024; -.
DR SMR; O96024; -.
DR BioGRID; 114248; 41.
DR IntAct; O96024; 5.
DR MINT; O96024; -.
DR STRING; 9606.ENSP00000390784; -.
DR SwissLipids; SLP:000000772; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; O96024; 1 site.
DR iPTMnet; O96024; -.
DR PhosphoSitePlus; O96024; -.
DR BioMuta; B3GALT4; -.
DR MassIVE; O96024; -.
DR PaxDb; O96024; -.
DR PeptideAtlas; O96024; -.
DR PRIDE; O96024; -.
DR ProteomicsDB; 51215; -.
DR Antibodypedia; 29042; 121 antibodies from 25 providers.
DR DNASU; 8705; -.
DR Ensembl; ENST00000383209.6; ENSP00000372696.5; ENSG00000206285.6.
DR Ensembl; ENST00000415322.4; ENSP00000394876.3; ENSG00000226936.4.
DR Ensembl; ENST00000419471.4; ENSP00000398660.3; ENSG00000235155.4.
DR Ensembl; ENST00000430971.4; ENSP00000414880.3; ENSG00000236802.4.
DR Ensembl; ENST00000451237.3; ENSP00000390784.1; ENSG00000235863.4.
DR GeneID; 8705; -.
DR KEGG; hsa:8705; -.
DR MANE-Select; ENST00000451237.3; ENSP00000390784.1; NM_003782.4; NP_003773.1.
DR CTD; 8705; -.
DR DisGeNET; 8705; -.
DR GeneCards; B3GALT4; -.
DR HGNC; HGNC:919; B3GALT4.
DR HPA; ENSG00000235863; Tissue enhanced (testis).
DR MIM; 603095; gene.
DR neXtProt; NX_O96024; -.
DR OpenTargets; ENSG00000235863; -.
DR PharmGKB; PA25212; -.
DR VEuPathDB; HostDB:ENSG00000235863; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000161798; -.
DR HOGENOM; CLU_036849_1_0_1; -.
DR InParanoid; O96024; -.
DR OMA; RCRVIAW; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; O96024; -.
DR TreeFam; TF318639; -.
DR BioCyc; MetaCyc:HS00059-MON; -.
DR BRENDA; 2.4.1.62; 2681.
DR PathwayCommons; O96024; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; O96024; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8705; 24 hits in 1074 CRISPR screens.
DR ChiTaRS; B3GALT4; human.
DR GeneWiki; B3GALT4; -.
DR GenomeRNAi; 8705; -.
DR Pharos; O96024; Tbio.
DR PRO; PR:O96024; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O96024; protein.
DR Bgee; ENSG00000235863; Expressed in lower esophagus mucosa and 95 other tissues.
DR ExpressionAtlas; O96024; baseline and differential.
DR Genevisible; O96024; HS.
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; IDA:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
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..378
FT /note="Beta-1,3-galactosyltransferase 4"
FT /id="PRO_0000219160"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..19
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 20..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 378 AA; 41537 MW; 4E55DFC72AE96213 CRC64;
MQLRLFRRLL LAALLLVIVW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLIPN
QEACSGPGAP PFLLILVCTA PENLNQRNAI RASWGGLREA RGLRVQTLFL LGEPNAQHPV
WGSQGSDLAS ESAAQGDILQ AAFQDSYRNL TLKTLSGLNW AEKHCPMARY VLKTDDDVYV
NVPELVSELV LRGGRWGQWE RSTEPQREAE QEGGQVLHSE EVPLLYLGRV HWRVNPSRTP
GGRHRVSEEQ WPHTWGPFPP YASGTGYVLS ASAVQLILKV ASRAPLLPLE DVFVGVSARR
GGLAPTQCVK LAGATHYPLD RCCYGKFLLT SHRLDPWKMQ EAWKLVGGSD GERTAPFCSW
FQGVLGILRC RAIAWLQS
