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   27-MAR-2024, entry version 161.
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;
CC       Note=Beta-1,3-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   GlyCosmos; Q9Y5Z6; 2 sites, No reported glycans.
DR   GlyGen; Q9Y5Z6; 2 sites.
DR   iPTMnet; Q9Y5Z6; -.
DR   PhosphoSitePlus; Q9Y5Z6; -.
DR   SwissPalm; Q9Y5Z6; -.
DR   BioMuta; B3GALT1; -.
DR   DMDM; 61212254; -.
DR   EPD; Q9Y5Z6; -.
DR   MassIVE; Q9Y5Z6; -.
DR   PaxDb; 9606-ENSP00000376456; -.
DR   PeptideAtlas; Q9Y5Z6; -.
DR   ProteomicsDB; 86553; -.
DR   Antibodypedia; 33791; 107 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   AGR; HGNC:916; -.
DR   CTD; 8708; -.
DR   DisGeNET; 8708; -.
DR   GeneCards; B3GALT1; -.
DR   HGNC; HGNC:916; B3GALT1.
DR   HPA; ENSG00000172318; Tissue enhanced (brain, skeletal muscle, 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; 532757at2759; -.
DR   PhylomeDB; Q9Y5Z6; -.
DR   TreeFam; TF318639; -.
DR   BioCyc; MetaCyc:ENSG00000172318-MONOMER; -.
DR   BRENDA; 2.4.1.134; 2681.
DR   PathwayCommons; Q9Y5Z6; -.
DR   Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR   SABIO-RK; Q9Y5Z6; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 8708; 15 hits in 1153 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 89 other cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:UniProtKB.
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:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11214:SF20; BETA-1,3-GALACTOSYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; Q9Y5Z6; HS.
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
//