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   24-JAN-2024, entry version 142.
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}, B3gt3
GN   {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=a globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC         galactosamine = a 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   GlyCosmos; Q920V1; 5 sites, 1 glycan.
DR   GlyGen; Q920V1; 5 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q920V1; -.
DR   PhosphoSitePlus; Q920V1; -.
DR   MaxQB; Q920V1; -.
DR   PaxDb; 10090-ENSMUSP00000058363; -.
DR   PeptideAtlas; Q920V1; -.
DR   ProteomicsDB; 277145; -.
DR   Pumba; Q920V1; -.
DR   Antibodypedia; 33673; 117 antibodies from 19 providers.
DR   DNASU; 26879; -.
DR   Ensembl; ENSMUST00000061826.3; ENSMUSP00000058363.2; ENSMUSG00000043300.3.
DR   GeneID; 26879; -.
DR   KEGG; mmu:26879; -.
DR   UCSC; uc008pmj.2; mouse.
DR   AGR; MGI:1349405; -.
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; DICKYRH; -.
DR   OrthoDB; 532757at2759; -.
DR   PhylomeDB; Q920V1; -.
DR   TreeFam; TF318639; -.
DR   Reactome; R-MMU-9840309; Glycosphingolipid biosynthesis.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 26879; 4 hits in 80 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 262 other cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0047273; F:galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:MGI.
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   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11214:SF153; UDP-GALNAC:BETA-1,3-N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   Genevisible; Q920V1; MM.
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
//