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   24-JAN-2024, entry version 152.
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   GlyCosmos; Q9Z2Y2; 3 sites, No reported glycans.
DR   GlyGen; Q9Z2Y2; 3 sites.
DR   PhosphoSitePlus; Q9Z2Y2; -.
DR   MaxQB; Q9Z2Y2; -.
DR   PaxDb; 10090-ENSMUSP00000030266; -.
DR   ProteomicsDB; 273460; -.
DR   Antibodypedia; 32429; 219 antibodies from 27 providers.
DR   DNASU; 53418; -.
DR   Ensembl; ENSMUST00000030266.12; ENSMUSP00000030266.6; ENSMUSG00000028541.15.
DR   Ensembl; ENSMUST00000084325.10; ENSMUSP00000081352.4; ENSMUSG00000028541.15.
DR   Ensembl; ENSMUST00000106421.9; ENSMUSP00000102029.3; ENSMUSG00000028541.15.
DR   GeneID; 53418; -.
DR   KEGG; mmu:53418; -.
DR   UCSC; uc008ujb.2; mouse.
DR   AGR; MGI:1858493; -.
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; RPMYTNV; -.
DR   OrthoDB; 306273at2759; -.
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 81 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 215 other cell types or tissues.
DR   ExpressionAtlas; Q9Z2Y2; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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   CDD; cd00899; b4GalT; 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; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF32; BETA-1,4-GALACTOSYLTRANSFERASE 2; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; Q9Z2Y2; MM.
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
//