B3GT1_HUMAN
ID B3GT1_HUMAN Reviewed; 326 AA.
AC Q9Y5Z6; D3DPB8; Q53SS2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Beta-1,3-galactosyltransferase 1 {ECO:0000305};
DE Short=Beta-1,3-GalTase 1;
DE Short=Beta3Gal-T1;
DE Short=Beta3GalT1;
DE EC=2.4.1.86 {ECO:0000269|PubMed:9582303};
DE AltName: Full=UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1;
GN Name=B3GALT1 {ECO:0000312|HGNC:HGNC:916};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=10356986; DOI=10.1016/s0014-5793(99)00547-5;
RA Bardoni A., Valli M., Trinchera M.;
RT "Differential expression of beta1,3galactosyltransferases in human colon
RT cells derived from adenocarcinomas or normal mucosa.";
RL FEBS Lett. 451:75-80(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC UDP-alpha-D-galactose to substrates with a terminal beta-N-
CC acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis
CC of the carbohydrate moieties of glycolipids and glycoproteins. Inactive
CC towards substrates with terminal alpha-N-acetylglucosamine (alpha-
CC GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues.
CC {ECO:0000269|PubMed:9582303}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133506; EC=2.4.1.86;
CC Evidence={ECO:0000269|PubMed:9582303};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433;
CC Evidence={ECO:0000269|PubMed:9582303};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC Cer(d18:1(4E)) + UDP-alpha-D-galactose = a beta-D-Gal-(1->3)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) +
CC H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914; EC=2.4.1.86;
CC Evidence={ECO:0000269|PubMed:9582303};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046;
CC Evidence={ECO:0000269|PubMed:9582303};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9582303};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain and colon mucosa and to a lesser
CC extent in colon adenocarcinoma cells. {ECO:0000269|PubMed:10356986,
CC 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 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_429";
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DR EMBL; AF117222; AAD23451.1; -; mRNA.
DR EMBL; AB041407; BAA94492.1; -; Genomic_DNA.
DR EMBL; AC016723; AAY15002.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11307.1; -; Genomic_DNA.
DR EMBL; BC101545; AAI01546.1; -; mRNA.
DR EMBL; BC104813; AAI04814.1; -; mRNA.
DR CCDS; CCDS2227.1; -.
DR RefSeq; NP_066191.1; NM_020981.3.
DR RefSeq; XP_005246988.1; XM_005246931.3.
DR RefSeq; XP_006712882.1; XM_006712819.3.
DR RefSeq; XP_011510387.1; XM_011512085.2.
DR AlphaFoldDB; Q9Y5Z6; -.
DR SMR; Q9Y5Z6; -.
DR BioGRID; 114251; 2.
DR STRING; 9606.ENSP00000376456; -.
DR BindingDB; Q9Y5Z6; -.
DR ChEMBL; CHEMBL2321634; -.
DR SwissLipids; SLP:000000774; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9Y5Z6; 2 sites.
DR iPTMnet; Q9Y5Z6; -.
DR PhosphoSitePlus; Q9Y5Z6; -.
DR BioMuta; B3GALT1; -.
DR DMDM; 61212254; -.
DR EPD; Q9Y5Z6; -.
DR MassIVE; Q9Y5Z6; -.
DR PaxDb; Q9Y5Z6; -.
DR PeptideAtlas; Q9Y5Z6; -.
DR PRIDE; Q9Y5Z6; -.
DR Antibodypedia; 33791; 92 antibodies from 20 providers.
DR DNASU; 8708; -.
DR Ensembl; ENST00000392690.4; ENSP00000376456.2; ENSG00000172318.6.
DR GeneID; 8708; -.
DR KEGG; hsa:8708; -.
DR MANE-Select; ENST00000392690.4; ENSP00000376456.2; NM_020981.4; NP_066191.1.
DR UCSC; uc061pgb.1; human.
DR CTD; 8708; -.
DR DisGeNET; 8708; -.
DR GeneCards; B3GALT1; -.
DR HGNC; HGNC:916; B3GALT1.
DR HPA; ENSG00000172318; Tissue enhanced (brain, tongue).
DR MIM; 603093; gene.
DR neXtProt; NX_Q9Y5Z6; -.
DR OpenTargets; ENSG00000172318; -.
DR PharmGKB; PA25209; -.
DR VEuPathDB; HostDB:ENSG00000172318; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000156219; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q9Y5Z6; -.
DR OMA; CEKNAPF; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q9Y5Z6; -.
DR TreeFam; TF318639; -.
DR BioCyc; MetaCyc:ENSG00000172318-MON; -.
DR BRENDA; 2.4.1.134; 2681.
DR PathwayCommons; Q9Y5Z6; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8708; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; B3GALT1; human.
DR GenomeRNAi; 8708; -.
DR Pharos; Q9Y5Z6; Tbio.
DR PRO; PR:Q9Y5Z6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y5Z6; protein.
DR Bgee; ENSG00000172318; Expressed in cortical plate and 88 other tissues.
DR Genevisible; Q9Y5Z6; HS.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0030259; P:lipid glycosylation; IDA:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002659; Glyco_trans_31.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Beta-1,3-galactosyltransferase 1"
FT /id="PRO_0000219145"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..326
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 326 AA; 37993 MW; 83271E99B2EE74F5 CRC64;
MASKVSCLYV LTVVCWASAL WYLSITRPTS SYTGSKPFSH LTVARKNFTF GNIRTRPINP
HSFEFLINEP NKCEKNIPFL VILISTTHKE FDARQAIRET WGDENNFKGI KIATLFLLGK
NADPVLNQMV EQESQIFHDI IVEDFIDSYH NLTLKTLMGM RWVATFCSKA KYVMKTDSDI
FVNMDNLIYK LLKPSTKPRR RYFTGYVING GPIRDVRSKW YMPRDLYPDS NYPPFCSGTG
YIFSADVAEL IYKTSLHTRL LHLEDVYVGL CLRKLGIHPF QNSGFNHWKM AYSLCRYRRV
ITVHQISPEE MHRIWNDMSS KKHLRC
