B4GT2_MOUSE
ID B4GT2_MOUSE Reviewed; 369 AA.
AC Q9Z2Y2; Q3TMP2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Beta-1,4-galactosyltransferase 2 {ECO:0000305};
DE Short=Beta-1,4-GalTase 2;
DE Short=Beta4Gal-T2;
DE Short=b4Gal-T2;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:O60909};
DE AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE AltName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
DE EC=2.4.1.38 {ECO:0000250|UniProtKB:O60909};
DE AltName: Full=Lactose synthase A protein;
DE EC=2.4.1.22 {ECO:0000250|UniProtKB:O60909};
DE AltName: Full=N-acetyllactosamine synthase;
DE EC=2.4.1.90 {ECO:0000250|UniProtKB:O60909};
DE AltName: Full=Nal synthase;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2;
GN Name=B4galt2 {ECO:0000312|MGI:MGI:1858493};
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 [MRNA].
RX PubMed=9597550; DOI=10.1093/glycob/8.5.517;
RA Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.;
RT "The expanding beta 4-galactosyltransferase gene family: messages from the
RT databanks.";
RL Glycobiology 8:517-526(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Sato T.;
RT "Mouse beta-1,4-galactosyltransferase II (beta-1,4-GalT II).";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
CC -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC oligosaccharides in many glycoproteins as well as the carbohydrate
CC moieties of glycolipids. Can produce lactose (By similarity).
CC {ECO:0000250|UniProtKB:O60909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP;
CC Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22;
CC Evidence={ECO:0000250|UniProtKB:O60909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405;
CC Evidence={ECO:0000250|UniProtKB:O60909};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133507; EC=2.4.1.38;
CC Evidence={ECO:0000250|UniProtKB:O60909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={ECO:0000250|UniProtKB:O60909};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-
CC galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP;
CC Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227;
CC EC=2.4.1.90; Evidence={ECO:0000250|UniProtKB:O60909};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000250|UniProtKB:O60909};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Trans cisternae of Golgi stack. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b4GalT2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_461";
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DR EMBL; AF142670; AAF22220.1; -; mRNA.
DR EMBL; AB019541; BAA34385.1; -; mRNA.
DR EMBL; AK165829; BAE38399.1; -; mRNA.
DR CCDS; CCDS18539.1; -.
DR RefSeq; NP_001240310.1; NM_001253381.1.
DR RefSeq; NP_059073.1; NM_017377.5.
DR RefSeq; XP_006503293.1; XM_006503230.3.
DR RefSeq; XP_017175805.1; XM_017320316.1.
DR AlphaFoldDB; Q9Z2Y2; -.
DR SMR; Q9Z2Y2; -.
DR STRING; 10090.ENSMUSP00000030266; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q9Z2Y2; 3 sites.
DR PhosphoSitePlus; Q9Z2Y2; -.
DR MaxQB; Q9Z2Y2; -.
DR PaxDb; Q9Z2Y2; -.
DR PRIDE; Q9Z2Y2; -.
DR ProteomicsDB; 273460; -.
DR Antibodypedia; 32429; 194 antibodies from 27 providers.
DR DNASU; 53418; -.
DR Ensembl; ENSMUST00000030266; ENSMUSP00000030266; ENSMUSG00000028541.
DR Ensembl; ENSMUST00000084325; ENSMUSP00000081352; ENSMUSG00000028541.
DR Ensembl; ENSMUST00000106421; ENSMUSP00000102029; ENSMUSG00000028541.
DR GeneID; 53418; -.
DR KEGG; mmu:53418; -.
DR UCSC; uc008ujb.2; mouse.
DR CTD; 8704; -.
DR MGI; MGI:1858493; B4galt2.
DR VEuPathDB; HostDB:ENSMUSG00000028541; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000159367; -.
DR HOGENOM; CLU_044391_0_0_1; -.
DR InParanoid; Q9Z2Y2; -.
DR OMA; RCGEQPR; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; Q9Z2Y2; -.
DR TreeFam; TF312834; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 53418; 2 hits in 76 CRISPR screens.
DR ChiTaRS; B4galt2; mouse.
DR PRO; PR:Q9Z2Y2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z2Y2; protein.
DR Bgee; ENSMUSG00000028541; Expressed in embryonic brain and 212 other tissues.
DR ExpressionAtlas; Q9Z2Y2; baseline and differential.
DR Genevisible; Q9Z2Y2; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004461; F:lactose synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..369
FT /note="Beta-1,4-galactosyltransferase 2"
FT /id="PRO_0000080534"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..369
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 58..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147..151
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 214..215
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 277..280
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT BINDING 308..310
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..136
FT /evidence="ECO:0000250"
FT DISULFID 208..227
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 41909 MW; EF4465AFE51C6C30 CRC64;
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSTRSP AHALYPAASS
STNCSRPNAT AASSGLPEVP SARPGPTAPV IPPCPDVPPG LVGRVVIEFT SPMPLERVQR
ENPGVLLGGR YSPPDCTPAQ TVAVIIPFRH REHHLRYWLH YLHPMLRRQR LRYGVYVINQ
HGEETFNRAK LLNVGFLEAL KEDAAYDCFI FSDVDLVPMD DRNLYRCGDQ PRHFAIAMDK
FGFRLPYASY FGGVSGLSKA QFLRINGFPN EYWGWGGEDD DIFNRISLTG MKISRPDVRI
GRYRMIKHDR DKHNEPNPQR FNKIQNTKMS MKWDGIGSVR YRVLEVSRQP LFTNITVDIG
QPMSWLTQG
