B3GT2_MOUSE
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 03-AUG-2022, entry version 134.
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 GlyGen; O54905; 5 sites.
DR iPTMnet; O54905; -.
DR PhosphoSitePlus; O54905; -.
DR PaxDb; O54905; -.
DR PRIDE; O54905; -.
DR ProteomicsDB; 265193; -.
DR Antibodypedia; 34468; 165 antibodies from 26 providers.
DR DNASU; 26878; -.
DR Ensembl; ENSMUST00000038252; ENSMUSP00000046118; ENSMUSG00000033849.
DR GeneID; 26878; -.
DR KEGG; mmu:26878; -.
DR UCSC; uc007cwy.2; mouse.
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; 1037602at2759; -.
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 73 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 tissues.
DR Genevisible; O54905; 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:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase 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:0006682; P:galactosylceramide biosynthetic process; ISO:MGI.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR045821; B3GT2_N.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF19341; B3GALT2_N; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
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
