ID B4GT4_MOUSE Reviewed; 344 AA.
AC Q9JJ04; Q8BR54; Q9QY12;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 161.
DE RecName: Full=Beta-1,4-galactosyltransferase 4 {ECO:0000305};
DE Short=Beta-1,4-GalTase 4;
DE Short=Beta4Gal-T4;
DE Short=b4Gal-T4;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:O60513};
DE AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE AltName: Full=Lactotriaosylceramide beta-1,4-galactosyltransferase;
DE EC=2.4.1.275 {ECO:0000250|UniProtKB:O60513};
DE AltName: Full=N-acetyllactosamine synthase;
DE EC=2.4.1.90 {ECO:0000250|UniProtKB:O60513};
DE AltName: Full=Nal synthase;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 4;
GN Name=B4galt4 {ECO:0000312|MGI:MGI:1928387};
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=Embryo;
RA Schwientek T., Clausen H.;
RT "Molecular cloning of mouse beta-1,4-galactosyltransferase 4.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Hippocampus, Kidney, 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=FVB/N; TISSUE=Colon, and Mammary tumor;
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).
CC -!- FUNCTION: Galactose (Gal) transferase involved in the synthesis of
CC terminal N-acetyllactosamine (LacNac) unit present on glycan chains of
CC glycoproteins and glycosphingolipids. Catalyzes the transfer of Gal
CC residue via a beta1->4 linkage from UDP-Gal to the non-reducing
CC terminal N-acetyl glucosamine 6-O-sulfate (6-O-sulfoGlcNAc) in the
CC linearly growing chain of both N- and O-linked keratan sulfate
CC proteoglycans. Cooperates with B3GNT7 N-acetyl glucosamine transferase
CC and CHST6 and CHST1 sulfotransferases to construct and elongate
CC mono- and disulfated disaccharide units [->3Galbeta1->4(6-
CC sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-
CC sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Transfers Gal
CC residue via a beta1->4 linkage to terminal 6-O-sulfoGlcNAc within the
CC LacNac unit of core 2 O-glycans forming 6-sulfo-sialyl-Lewis X (sLex).
CC May contribute to the generation of sLex epitope on mucin-type
CC glycoproteins that serve as ligands for SELL/L-selectin, a major
CC regulator of leukocyte migration. In the biosynthesis pathway of
CC neolacto-series glycosphingolipids, transfers Gal residue via a
CC beta1->4 linkage to terminal GlcNAc of a lactotriaosylceramide (Lc3Cer)
CC acceptor to form a neolactotetraosylceramide.
CC {ECO:0000250|UniProtKB:O60513}.
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:O60513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000250|UniProtKB:O60513};
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 neolactoside
CC nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275;
CC Evidence={ECO:0000250|UniProtKB:O60513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000250|UniProtKB:O60513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-
CC [protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-
CC [beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:67948, Rhea:RHEA-COMP:17367, Rhea:RHEA-
CC COMP:17398, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:176494, ChEBI:CHEBI:176635;
CC Evidence={ECO:0000250|UniProtKB:O60513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67949;
CC Evidence={ECO:0000250|UniProtKB:O60513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC [protein] + UDP-alpha-D-galactose = 3-O-{beta-D-galactosyl-(1->3)-
CC [beta-D-galactosyl-(1->4)-6-O-sulfo-N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + H(+)
CC + UDP; Xref=Rhea:RHEA:67872, Rhea:RHEA-COMP:17370, Rhea:RHEA-
CC COMP:17397, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:176493, ChEBI:CHEBI:176634;
CC Evidence={ECO:0000250|UniProtKB:O60513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67873;
CC Evidence={ECO:0000250|UniProtKB:O60513};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:O60513}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:O60513}.
CC -!- SUBUNIT: Interacts with SLC35A2/UGT1. {ECO:0000250|UniProtKB:O60513}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O60513}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:O60513}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32433.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b4GalT4;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_463";
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DR EMBL; AF142672; AAF22222.1; -; mRNA.
DR EMBL; AF158746; AAF80363.1; -; mRNA.
DR EMBL; AK041692; BAC31035.1; -; mRNA.
DR EMBL; AK045602; BAC32433.1; ALT_FRAME; mRNA.
DR EMBL; AK050005; BAC34028.1; -; mRNA.
DR EMBL; AK052013; BAC34832.1; -; mRNA.
DR EMBL; AK053603; BAC35443.1; -; mRNA.
DR EMBL; AK085368; BAC39433.1; -; mRNA.
DR EMBL; BC013492; AAH13492.1; -; mRNA.
DR EMBL; BC031115; AAH31115.1; -; mRNA.
DR CCDS; CCDS28173.1; -.
DR RefSeq; NP_001272722.1; NM_001285793.1.
DR RefSeq; NP_062778.2; NM_019804.4.
DR RefSeq; XP_006522462.1; XM_006522399.3.
DR AlphaFoldDB; Q9JJ04; -.
DR SMR; Q9JJ04; -.
DR STRING; 10090.ENSMUSP00000023482; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyCosmos; Q9JJ04; 2 sites, No reported glycans.
DR GlyGen; Q9JJ04; 2 sites.
DR iPTMnet; Q9JJ04; -.
DR PhosphoSitePlus; Q9JJ04; -.
DR MaxQB; Q9JJ04; -.
DR PaxDb; 10090-ENSMUSP00000023482; -.
DR ProteomicsDB; 273526; -.
DR Antibodypedia; 32692; 228 antibodies from 27 providers.
DR DNASU; 56375; -.
DR Ensembl; ENSMUST00000023482.13; ENSMUSP00000023482.7; ENSMUSG00000022793.18.
DR Ensembl; ENSMUST00000114712.8; ENSMUSP00000110360.2; ENSMUSG00000022793.18.
DR GeneID; 56375; -.
DR KEGG; mmu:56375; -.
DR UCSC; uc007zfi.3; mouse.
DR AGR; MGI:1928387; -.
DR CTD; 8702; -.
DR MGI; MGI:1928387; B4galt4.
DR VEuPathDB; HostDB:ENSMUSG00000022793; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158378; -.
DR HOGENOM; CLU_044391_1_0_1; -.
DR InParanoid; Q9JJ04; -.
DR OMA; QVWRKDG; -.
DR PhylomeDB; Q9JJ04; -.
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; 56375; 4 hits in 79 CRISPR screens.
DR ChiTaRS; B4galt4; mouse.
DR PRO; PR:Q9JJ04; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JJ04; Protein.
DR Bgee; ENSMUSG00000022793; Expressed in animal zygote and 212 other cell types or tissues.
DR ExpressionAtlas; Q9JJ04; baseline and differential.
DR Genevisible; Q9JJ04; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISS:UniProtKB.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001572; P:lactosylceramide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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:SF9; BETA-1,4-GALACTOSYLTRANSFERASE 4; 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Manganese; Membrane; Metal-binding; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Beta-1,4-galactosyltransferase 4"
FT /id="PRO_0000080543"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..344
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 129..133
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 168..170
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 195..196
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 258..261
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT BINDING 289..291
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..118
FT /evidence="ECO:0000250"
FT DISULFID 189..208
FT /evidence="ECO:0000250"
FT CONFLICT 238
FT /note="L -> F (in Ref. 1; AAF22222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 39700 MW; 74FA110191A4BCC8 CRC64;
MGCNPPYHLS YRLRLLLLFT LCLTVVGWAT SNYFVGAIQV IPKAKDFMAS FHKVIHLGNE
ETLGHDGATK KPELANCPSV SPNLRGQSKL VFKPDLTLEE IEAENPKVSR GRYHPEECKA
LQRVAILIPH RNREKHLIYL LEHLHPFLQR QQLDYGIYII HQTGSKKFNR AKLLNVGYLE
ALKEENWDCF VFHDVDLVPE NDFNLYTCGD QPKHLVVGRN STGYRLRYSK YFGGVTALSR
EQFLKVNGFS NNYWGWGGED DDLRLRVELH KMKISRPKPD VGKYTMIFHT RDKGNEVNMG
RMKLLQQMSR VWKTDGLSSC SYRLLSVEHN PLYANITVDF WTAA
//
