B3GL1_MOUSE
ID B3GL1_MOUSE Reviewed; 331 AA.
AC Q920V1; O54906; Q91V72; Q920V0; Q9CTE5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1;
DE Short=Beta-1,3-GalNAc-T1;
DE EC=2.4.1.79 {ECO:0000250|UniProtKB:O75752};
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=Brainiac 1 {ECO:0000303|PubMed:11463849};
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|MGI:MGI:1349405};
GN Synonyms=B3galt3 {ECO:0000303|PubMed:9417047},
GN B3gt3 {ECO:0000312|EMBL:BAB68678.1}, Mbrn1 {ECO:0000303|PubMed:11463849};
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 [GENOMIC DNA], AND VARIANTS THR-4; HIS-87 AND MET-128.
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=9417047; DOI=10.1074/jbc.273.1.58;
RA Hennet T., Dinter A., Kuhnert P., Mattu T.S., Rudd P.M., Berger E.G.;
RT "Genomic cloning and expression of three murine UDP-galactose: beta-N-
RT acetylglucosamine beta1,3-galactosyltransferase genes.";
RL J. Biol. Chem. 273:58-65(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11463849; DOI=10.1128/mcb.21.16.5688-5697.2001;
RA Vollrath B., Fitzgerald K.J., Leder P.;
RT "A murine homologue of the Drosophila brainiac gene shows homology to
RT glycosyltransferases and is required for preimplantation development of the
RT mouse.";
RL Mol. Cell. Biol. 21:5688-5697(2001).
CC -!- FUNCTION: Transfers N-acetylgalactosamine onto globotriaosylceramide
CC (PubMed:9417047). Plays a critical role in preimplantation stage
CC embryonic development (PubMed:11463849). {ECO:0000269|PubMed:11463849,
CC ECO:0000269|PubMed:9417047}.
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:0000250|UniProtKB:O75752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22253;
CC Evidence={ECO:0000250|UniProtKB:O75752};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O75752}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O75752}.
CC -!- TISSUE SPECIFICITY: Detected in brain, ovary, kidney, uterus and
CC stomach (PubMed:9417047, PubMed:11463849). In ovary, specifically
CC expressed in follicular granulosa cells and shows particularly strong
CC expression at later stages of follicle development (PubMed:11463849).
CC {ECO:0000269|PubMed:11463849, ECO:0000269|PubMed:9417047}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos from 12.5 days post coitum
CC (dpc) onwards. Expressed in all four ventricles of the developing
CC brain, with highest expression in the outer ventricular layer. Also
CC found in the limb buds at 12.5 dpc. Detected in the brain (hippocampus)
CC and retina at postnatal day 1. Expression in the retina is localized to
CC the ganglion cell layer. At postnatal day 10, expression remains strong
CC in the hippocampus where it localizes to the four CA fields and the
CC dentate gyrus. {ECO:0000269|PubMed:11463849}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Lethality occurs at the
CC preimplantation stage, between 3.5 and 4.5 days post-coitum (dpc).
CC {ECO:0000269|PubMed:11463849}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b3GalT3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_456";
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DR EMBL; AB039154; BAB68678.1; -; Genomic_DNA.
DR EMBL; AB039155; BAB68679.1; -; Genomic_DNA.
DR EMBL; AB039156; BAB68680.1; -; Genomic_DNA.
DR EMBL; AB039157; BAB68681.1; -; Genomic_DNA.
DR EMBL; AB039158; BAB68682.1; -; Genomic_DNA.
DR EMBL; AB039159; BAB68683.1; -; Genomic_DNA.
DR EMBL; AB039160; BAB68684.1; -; Genomic_DNA.
DR EMBL; AB039161; BAB68685.1; -; Genomic_DNA.
DR EMBL; AB039162; BAB68686.1; -; Genomic_DNA.
DR EMBL; AF029792; AAC53525.1; -; Genomic_DNA.
DR EMBL; AK003837; BAB23028.1; -; mRNA.
DR EMBL; AK088407; BAC40336.1; -; mRNA.
DR EMBL; BC003835; AAH03835.3; -; mRNA.
DR CCDS; CCDS17406.1; -.
DR RefSeq; NP_064410.1; NM_020026.4.
DR RefSeq; XP_006501592.1; XM_006501529.3.
DR AlphaFoldDB; Q920V1; -.
DR SMR; Q920V1; -.
DR STRING; 10090.ENSMUSP00000058363; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyConnect; 2808; 1 N-Linked glycan (1 site).
DR GlyGen; Q920V1; 5 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q920V1; -.
DR MaxQB; Q920V1; -.
DR PaxDb; Q920V1; -.
DR PeptideAtlas; Q920V1; -.
DR PRIDE; Q920V1; -.
DR ProteomicsDB; 277145; -.
DR Antibodypedia; 33673; 99 antibodies from 19 providers.
DR DNASU; 26879; -.
DR Ensembl; ENSMUST00000061826; ENSMUSP00000058363; ENSMUSG00000043300.
DR GeneID; 26879; -.
DR KEGG; mmu:26879; -.
DR UCSC; uc008pmj.2; mouse.
DR CTD; 8706; -.
DR MGI; MGI:1349405; B3galnt1.
DR VEuPathDB; HostDB:ENSMUSG00000043300; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000162252; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q920V1; -.
DR OMA; PYCSGMG; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q920V1; -.
DR TreeFam; TF318639; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 26879; 4 hits in 75 CRISPR screens.
DR ChiTaRS; B3galnt1; mouse.
DR PRO; PR:Q920V1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q920V1; protein.
DR Bgee; ENSMUSG00000043300; Expressed in gastrula and 259 other tissues.
DR Genevisible; Q920V1; MM.
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; 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:MGI.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA: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 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Magnesium; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..331
FT /note="UDP-GalNAc:beta-1,3-N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000219154"
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 4
FT /note="A -> T (in strain: NJL/Msf, BLG2/Msf, MSM/Msf and
FT SWN/Msf)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 87
FT /note="R -> H (in strain: SWN/Msf)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 128
FT /note="T -> M (in strain: CAST/Ei)"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 331 AA; 39371 MW; 387E8B0C75FC282D CRC64;
MAPAVLTALP NRMSLRSLKW SLLLLSLLSF LVIWYLSLPH YNVIERVNWM YFYEYEPIYR
QDFRFTLREH SNCSHQNPFL VILVTSRPSD VKARQAIRVT WGEKKSWWGY EVLTFFLLGQ
QAEREDKTLA LSLEDEHVLY GDIIRQDFLD TYNNLTLKTI MAFRWVMEFC PNAKYIMKTD
TDVFINTGNL VKYLLNLNHS EKFFTGYPLI DNYSYRGFFH KNHISYQEYP FKVFPPYCSG
LGYIMSGDLV PRVYEMMSHV KPIKFEDVYV GICLNLLKVD IHIPEDTNLF FLYRIHLDVC
QLRRVIAAHG FSSKEIITFW QVMLRNTTCH Y
