ID   B3GT2_MOUSE             Reviewed;         422 AA.
AC   O54905; Q8BH19; Q8CBX4; Q91V19; Q91V58; Q91VE9; Q920V3; Q920V4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Beta-1,3-galactosyltransferase 2 {ECO:0000305};
DE            Short=Beta-1,3-GalTase 2;
DE            Short=Beta3Gal-T2;
DE            Short=Beta3GalT2;
DE            EC=2.4.1.86 {ECO:0000269|PubMed:9417047};
DE   AltName: Full=UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase-II;
GN   Name=B3galt2 {ECO:0000312|MGI:MGI:1349461};
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], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Diencephalon, and Hippocampus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-415, AND VARIANTS SER-44; ALA-86;
RP   SER-88; THR-100 AND ASP-124.
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.
CC   -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC       UDP-galactose to substrates with a terminal beta-N-acetylglucosamine
CC       (beta-GlcNAc) residue. Can also utilize substrates with a terminal
CC       galactose residue, albeit with lower efficiency. Involved in the
CC       biosynthesis of the carbohydrate moieties of glycolipids and
CC       glycoproteins. {ECO:0000269|PubMed:9417047}.
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:9417047};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433;
CC         Evidence={ECO:0000269|PubMed:9417047};
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:0000250|UniProtKB:O43825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) + UDP-
CC         alpha-D-galactose = a neolactoside IV(3)-beta-[Gal-beta-(1->3)-
CC         GlcNAc]-nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41936,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:78565, ChEBI:CHEBI:142448;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41937;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:9417047};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.6 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9417047};
CC         KM=38.3 mM for GlcNAc-beta-pNP {ECO:0000269|PubMed:9417047};
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 heart.
CC       {ECO:0000269|PubMed:9417047}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b3GalT2;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_455";
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DR   EMBL; AF029791; AAC53524.1; -; Genomic_DNA.
DR   EMBL; AK034371; BAC28688.1; -; mRNA.
DR   EMBL; AK036141; BAC29317.1; -; mRNA.
DR   EMBL; AK083168; BAC38793.1; -; mRNA.
DR   EMBL; BC046322; AAH46322.1; -; mRNA.
DR   EMBL; AB039144; BAB68668.1; -; Genomic_DNA.
DR   EMBL; AB039145; BAB68669.1; -; Genomic_DNA.
DR   EMBL; AB039146; BAB68670.1; -; Genomic_DNA.
DR   EMBL; AB039147; BAB68671.1; -; Genomic_DNA.
DR   EMBL; AB039148; BAB68672.1; -; Genomic_DNA.
DR   EMBL; AB039149; BAB68673.1; -; Genomic_DNA.
DR   EMBL; AB039150; BAB68674.1; -; Genomic_DNA.
DR   EMBL; AB039151; BAB68675.1; -; Genomic_DNA.
DR   EMBL; AB039152; BAB68676.1; -; Genomic_DNA.
DR   CCDS; CCDS15342.1; -.
DR   RefSeq; NP_064409.3; NM_020025.4.
DR   AlphaFoldDB; O54905; -.
DR   SMR; O54905; -.
DR   BioGRID; 205036; 2.
DR   IntAct; O54905; 1.
DR   STRING; 10090.ENSMUSP00000046118; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   GlyCosmos; O54905; 5 sites, No reported glycans.
DR   GlyGen; O54905; 5 sites.
DR   iPTMnet; O54905; -.
DR   PhosphoSitePlus; O54905; -.
DR   PaxDb; 10090-ENSMUSP00000046118; -.
DR   ProteomicsDB; 265193; -.
DR   Antibodypedia; 34468; 174 antibodies from 26 providers.
DR   DNASU; 26878; -.
DR   Ensembl; ENSMUST00000038252.4; ENSMUSP00000046118.3; ENSMUSG00000033849.4.
DR   GeneID; 26878; -.
DR   KEGG; mmu:26878; -.
DR   UCSC; uc007cwy.2; mouse.
DR   AGR; MGI:1349461; -.
DR   CTD; 8707; -.
DR   MGI; MGI:1349461; B3galt2.
DR   VEuPathDB; HostDB:ENSMUSG00000033849; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   GeneTree; ENSGT00940000155117; -.
DR   HOGENOM; CLU_036849_2_1_1; -.
DR   InParanoid; O54905; -.
DR   OMA; TSYHFKY; -.
DR   OrthoDB; 532757at2759; -.
DR   PhylomeDB; O54905; -.
DR   TreeFam; TF318639; -.
DR   Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 26878; 1 hit in 78 CRISPR screens.
DR   PRO; PR:O54905; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; O54905; Protein.
DR   Bgee; ENSMUSG00000033849; Expressed in epididymal fat pad and 162 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: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:MGI.
DR   GO; GO:0006682; P:galactosylceramide biosynthetic process; ISO:MGI.
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; IPR045821; B3GT2_N.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214:SF19; BETA-1,3-GALACTOSYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   Pfam; PF19341; B3GALT2_N; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   Genevisible; O54905; MM.
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..422
FT                   /note="Beta-1,3-galactosyltransferase 2"
FT                   /id="PRO_0000219151"
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..422
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          91..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         44
FT                   /note="N -> S (in strain: HMI/Msf)"
FT                   /evidence="ECO:0000269|Ref.4"
FT   VARIANT         86
FT                   /note="V -> A (in strain: BLG2/Msf, MSM/Msf, SWN/Msf and
FT                   NJL/Msf)"
FT                   /evidence="ECO:0000269|Ref.4"
FT   VARIANT         88
FT                   /note="P -> S (in strain: BLG2/Msf and NJL/Msf)"
FT                   /evidence="ECO:0000269|Ref.4"
FT   VARIANT         100
FT                   /note="S -> T (in strain: CAST/Ei and HMI/Msf)"
FT                   /evidence="ECO:0000269|Ref.4"
FT   VARIANT         124
FT                   /note="N -> D (in strain: BLG2/Msf, NJL/Msf, MSM/Msf and
FT                   SWN/Msf)"
FT                   /evidence="ECO:0000269|Ref.4"
FT   CONFLICT        95
FT                   /note="T -> I (in Ref. 1; AAC53524)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366
FT                   /note="H -> R (in Ref. 2; BAC28688)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  49095 MW;  58F5D3568143F4FB CRC64;
     MLQWRRRHCC FAKMTWSPKR SLLRTPLTGV LSLVFLFAMF LFFNHHDWLP GRPGFKENPV
     TYTFRGFRST KSETNHSSLR TIWKEVAPQT LRPHTASNSS NTELSPQGVT GLQNTLSANG
     SIYNEKGTGH PNSYHFKYII NEPEKCQEKS PFLILLIAAE PGQIEARRAI RQTWGNETLA
     PGIQIIRVFL LGISIKLNGY LQHAIQEESR QYHDIIQQEY LDTYYNLTIK TLMGMNWVAT
     YCPHTPYVMK TDSDMFVNTE YLIHKLLKPD LPPRHNYFTG YLMRGYAPNR NKDSKWYMPP
     DLYPSERYPV FCSGTGYVFS GDLAEKIFKV SLGIRRLHLE DVYVGICLAK LRVDPVPPPN
     EFVFNHWRVS YSSCKYSHLI TSHQFQPSEL IKYWNHLQQN KHNACANAAK EKAGRYRHRK
     LH
//