B3GL1_HUMAN
ID B3GL1_HUMAN Reviewed; 331 AA.
AC O75752; D3DNM4; Q3Y531; Q6IAI5; Q8NFM8; Q8NFM9; Q9HA06;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE Short=Beta-1,3-GalNAc-T1;
DE EC=2.4.1.79 {ECO:0000269|PubMed:10993897};
DE AltName: Full=Beta-1,3-galactosyltransferase 3;
DE Short=Beta-1,3-GalTase 3;
DE Short=Beta3Gal-T3;
DE Short=Beta3GalT3;
DE Short=b3Gal-T3;
DE AltName: Full=Beta-3-Gx-T3;
DE AltName: Full=Galactosylgalactosylglucosylceramide beta-D-acetyl-galactosaminyltransferase;
DE AltName: Full=Globoside synthase;
DE AltName: Full=UDP-N-acetylgalactosamine:globotriaosylceramide beta-1,3-N-acetylgalactosaminyltransferase;
GN Name=B3GALNT1 {ECO:0000312|HGNC:HGNC:918}; Synonyms=B3GALT3;
GN ORFNames=UNQ531/PRO1074;
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], COFACTOR, 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE
RP SPECIFICITY, AND POLYMORPHISM.
RC TISSUE=Kidney;
RX PubMed=10993897; DOI=10.1074/jbc.m006902200;
RA Okajima T., Nakamura Y., Uchikawa M., Haslam D.B., Numata S., Furukawa K.,
RA Urano T., Furukawa K.;
RT "Expression cloning of human globoside synthase cDNAs. Identification of
RT beta3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta1,3-N-
RT acetylgalactosaminyltransferase.";
RL J. Biol. Chem. 275:40498-40503(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Luo W.Q., Chen J.H., Huang X.W., Zhou Y., Zhou H.J., Hu S.N., Yuan J.G.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-266 AND ARG-271, AND
RP POLYMORPHISM.
RX PubMed=12023287; DOI=10.1074/jbc.m203047200;
RA Hellberg A., Poole J., Olsson M.L.;
RT "Molecular basis of the globoside-deficient P(k) blood group phenotype.
RT Identification of four inactivating mutations in the UDP-N-
RT acetylgalactosamine: globotriaosylceramide 3-beta-N-
RT acetylgalactosaminyltransferase gene.";
RL J. Biol. Chem. 277:29455-29459(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-126.
RG SeattleSNPs variation discovery resource;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH47618.1};
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: Transfers N-acetylgalactosamine onto globotriaosylceramide
CC (PubMed:10993897). Plays a critical role in preimplantation stage
CC embryonic development (By similarity). {ECO:0000250|UniProtKB:Q920V1,
CC ECO:0000269|PubMed:10993897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = globoside Gb4Cer (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:22252, ChEBI:CHEBI:15378, ChEBI:CHEBI:18259,
CC ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.79;
CC Evidence={ECO:0000269|PubMed:10993897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22253;
CC Evidence={ECO:0000269|PubMed:10993897};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10993897, ECO:0000269|PubMed:9582303};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Higher expression in heart and brain, and to a
CC lesser extent in lung, placenta, kidney and testis. Lower expression in
CC liver, spleen and stomach. No expression in skeletal muscle.
CC {ECO:0000269|PubMed:10993897, ECO:0000269|PubMed:9582303}.
CC -!- POLYMORPHISM: Genetic variation in B3GALNT1 is responsible for the
CC blood group P1PK system [MIM:111400]. Different combinations or absence
CC of the P1PK antigens define 5 different phenotypes: P1, P2, P1(k),
CC P2(k), and P. The P1(k) and P2(k) phenotypes are rare and characterized
CC by lack of the P antigen. {ECO:0000269|PubMed:12023287}.
CC -!- POLYMORPHISM: B3GALNT1 activity is responsible for the globoside blood
CC group system (GLOB), which is defined by the P antigen [MIM:615021].
CC {ECO:0000269|PubMed:10993897}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=p";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/b3galt3/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,3-
CC galactosyltransferase 3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_451";
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DR EMBL; Y15062; CAA75346.1; -; mRNA.
DR EMBL; AB050855; BAB17690.1; -; mRNA.
DR EMBL; AB050856; BAB17691.1; -; mRNA.
DR EMBL; AF132731; AAF66442.1; -; mRNA.
DR EMBL; AF154848; AAF72106.1; -; mRNA.
DR EMBL; AF494105; AAM96011.1; -; Genomic_DNA.
DR EMBL; AF494106; AAM96012.1; -; Genomic_DNA.
DR EMBL; AY359049; AAQ89408.1; -; mRNA.
DR EMBL; CR457170; CAG33451.1; -; mRNA.
DR EMBL; DQ158095; AAZ67917.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78621.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78623.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78624.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78625.1; -; Genomic_DNA.
DR EMBL; BC047618; AAH47618.1; -; mRNA.
DR CCDS; CCDS3193.1; -.
DR RefSeq; NP_001033717.1; NM_001038628.1.
DR RefSeq; NP_003772.1; NM_003781.3.
DR RefSeq; NP_149357.1; NM_033167.2.
DR RefSeq; NP_149358.1; NM_033168.2.
DR RefSeq; NP_149359.1; NM_033169.2.
DR RefSeq; XP_005247916.1; XM_005247859.4.
DR AlphaFoldDB; O75752; -.
DR SMR; O75752; -.
DR BioGRID; 114249; 30.
DR IntAct; O75752; 21.
DR STRING; 9606.ENSP00000376532; -.
DR SwissLipids; SLP:000000789; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; O75752; 7 sites.
DR iPTMnet; O75752; -.
DR PhosphoSitePlus; O75752; -.
DR BioMuta; B3GALNT1; -.
DR EPD; O75752; -.
DR MassIVE; O75752; -.
DR MaxQB; O75752; -.
DR PaxDb; O75752; -.
DR PeptideAtlas; O75752; -.
DR PRIDE; O75752; -.
DR ProteomicsDB; 50180; -.
DR Antibodypedia; 33673; 99 antibodies from 19 providers.
DR DNASU; 8706; -.
DR Ensembl; ENST00000320474.10; ENSP00000323479.4; ENSG00000169255.15.
DR Ensembl; ENST00000392779.6; ENSP00000376530.2; ENSG00000169255.15.
DR Ensembl; ENST00000392781.7; ENSP00000376532.2; ENSG00000169255.15.
DR Ensembl; ENST00000473285.5; ENSP00000418226.1; ENSG00000169255.15.
DR Ensembl; ENST00000488170.5; ENSP00000420163.1; ENSG00000169255.15.
DR Ensembl; ENST00000650695.1; ENSP00000498902.1; ENSG00000169255.15.
DR Ensembl; ENST00000650733.1; ENSP00000499186.1; ENSG00000169255.15.
DR Ensembl; ENST00000651117.1; ENSP00000498854.1; ENSG00000169255.15.
DR Ensembl; ENST00000651147.1; ENSP00000498478.1; ENSG00000169255.15.
DR Ensembl; ENST00000651178.1; ENSP00000498982.1; ENSG00000169255.15.
DR Ensembl; ENST00000651254.1; ENSP00000498553.1; ENSG00000169255.15.
DR Ensembl; ENST00000651292.1; ENSP00000498542.1; ENSG00000169255.15.
DR Ensembl; ENST00000651305.1; ENSP00000498427.1; ENSG00000169255.15.
DR Ensembl; ENST00000651379.1; ENSP00000498978.1; ENSG00000169255.15.
DR Ensembl; ENST00000651380.1; ENSP00000499072.1; ENSG00000169255.15.
DR Ensembl; ENST00000651460.1; ENSP00000498369.1; ENSG00000169255.15.
DR Ensembl; ENST00000651509.1; ENSP00000499003.1; ENSG00000169255.15.
DR Ensembl; ENST00000651686.1; ENSP00000498346.1; ENSG00000169255.15.
DR Ensembl; ENST00000651689.1; ENSP00000499010.1; ENSG00000169255.15.
DR Ensembl; ENST00000651791.1; ENSP00000499180.1; ENSG00000169255.15.
DR Ensembl; ENST00000651916.1; ENSP00000498487.1; ENSG00000169255.15.
DR Ensembl; ENST00000651953.1; ENSP00000498633.1; ENSG00000169255.15.
DR Ensembl; ENST00000651972.1; ENSP00000498907.1; ENSG00000169255.15.
DR Ensembl; ENST00000652032.1; ENSP00000498901.1; ENSG00000169255.15.
DR Ensembl; ENST00000652059.1; ENSP00000498743.1; ENSG00000169255.15.
DR Ensembl; ENST00000652111.1; ENSP00000498689.1; ENSG00000169255.15.
DR Ensembl; ENST00000652143.1; ENSP00000498655.1; ENSG00000169255.15.
DR Ensembl; ENST00000652377.1; ENSP00000498481.1; ENSG00000169255.15.
DR Ensembl; ENST00000652596.1; ENSP00000498810.1; ENSG00000169255.15.
DR Ensembl; ENST00000652669.1; ENSP00000498696.1; ENSG00000169255.15.
DR Ensembl; ENST00000652730.1; ENSP00000498660.1; ENSG00000169255.15.
DR GeneID; 8706; -.
DR KEGG; hsa:8706; -.
DR MANE-Select; ENST00000320474.10; ENSP00000323479.4; NM_003781.4; NP_003772.1.
DR UCSC; uc003fdv.4; human.
DR CTD; 8706; -.
DR DisGeNET; 8706; -.
DR GeneCards; B3GALNT1; -.
DR HGNC; HGNC:918; B3GALNT1.
DR HPA; ENSG00000169255; Tissue enhanced (heart).
DR MalaCards; B3GALNT1; -.
DR MIM; 111400; phenotype.
DR MIM; 603094; gene.
DR MIM; 615021; phenotype.
DR neXtProt; NX_O75752; -.
DR OpenTargets; ENSG00000169255; -.
DR PharmGKB; PA25211; -.
DR VEuPathDB; HostDB:ENSG00000169255; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000162252; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; O75752; -.
DR OMA; PYCSGMG; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; O75752; -.
DR TreeFam; TF318639; -.
DR BioCyc; MetaCyc:HS09918-MON; -.
DR BRENDA; 2.4.1.122; 2681.
DR BRENDA; 2.4.1.62; 2681.
DR BRENDA; 2.4.1.79; 2681.
DR BRENDA; 2.4.1.88; 2681.
DR PathwayCommons; O75752; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR SignaLink; O75752; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8706; 20 hits in 1061 CRISPR screens.
DR ChiTaRS; B3GALNT1; human.
DR GeneWiki; B3GALNT1; -.
DR GenomeRNAi; 8706; -.
DR Pharos; O75752; Tbio.
DR PRO; PR:O75752; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75752; protein.
DR Bgee; ENSG00000169255; Expressed in cortical plate and 183 other tissues.
DR ExpressionAtlas; O75752; baseline and differential.
DR Genevisible; O75752; HS.
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:0047273; F:galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase activity; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:Ensembl.
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 Blood group antigen; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Magnesium; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..331
FT /note="UDP-GalNAc:beta-1,3-N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000219153"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..331
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 126
FT /note="D -> N (in dbSNP:rs2231257)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_025091"
FT VARIANT 266
FT /note="E -> A (associated with P2(k) phenotype;
FT dbSNP:rs28937582)"
FT /evidence="ECO:0000269|PubMed:12023287"
FT /id="VAR_019646"
FT VARIANT 271
FT /note="G -> R (associated with P1(k) phenotype;
FT dbSNP:rs104893683)"
FT /evidence="ECO:0000269|PubMed:12023287"
FT /id="VAR_019647"
SQ SEQUENCE 331 AA; 39512 MW; 3556BCAF1646F702 CRC64;
MASALWTVLP SRMSLRSLKW SLLLLSLLSF FVMWYLSLPH YNVIERVNWM YFYEYEPIYR
QDFHFTLREH SNCSHQNPFL VILVTSHPSD VKARQAIRVT WGEKKSWWGY EVLTFFLLGQ
EAEKEDKMLA LSLEDEHLLY GDIIRQDFLD TYNNLTLKTI MAFRWVTEFC PNAKYVMKTD
TDVFINTGNL VKYLLNLNHS EKFFTGYPLI DNYSYRGFYQ KTHISYQEYP FKVFPPYCSG
LGYIMSRDLV PRIYEMMGHV KPIKFEDVYV GICLNLLKVN IHIPEDTNLF FLYRIHLDVC
QLRRVIAAHG FSSKEIITFW QVMLRNTTCH Y
