ID   B4GT2_CRIGR             Reviewed;         369 AA.
AC   Q80WN9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Beta-1,4-galactosyltransferase 2;
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;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=14567696; DOI=10.1021/bi0353068;
RA   Lee J., Park S.-H., Sundaram S., Raju T.S., Shaper N.L., Stanley P.;
RT   "A mutation causing a reduced level of expression of six beta4-
RT   galactosyltransferase genes is the basis of the Lec19 CHO glycosylation
RT   mutant.";
RL   Biochemistry 42:12349-12357(2003).
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 = lactose + UDP + H(+);
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 + UDP + H(+); 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 + UDP + H(+);
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY117536; AAM77195.1; -; mRNA.
DR   RefSeq; NP_001233623.1; NM_001246694.2.
DR   RefSeq; XP_007641467.1; XM_007643277.4.
DR   AlphaFoldDB; Q80WN9; -.
DR   SMR; Q80WN9; -.
DR   GlyCosmos; Q80WN9; 3 sites, No reported glycans.
DR   GlyGen; Q80WN9; 3 sites.
DR   Ensembl; ENSCGRT00000010269; ENSCGRP00000010100; ENSCGRG00000007365.
DR   Ensembl; ENSCGRT00001017640; ENSCGRP00001013403; ENSCGRG00001014544.
DR   GeneID; 100689434; -.
DR   KEGG; cge:100689434; -.
DR   CTD; 8704; -.
DR   eggNOG; KOG3916; Eukaryota.
DR   OMA; GEQPRHF; -.
DR   OrthoDB; 10016069at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP001108280; Chromosome 2.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004461; F:lactose synthase activity; ISS:UniProtKB.
DR   GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00899; b4GalT; 1.
DR   FunFam; 3.90.550.10:FF:000028; beta-1,4-galactosyltransferase 1; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 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.
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_0000080532"
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          59..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..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;  42005 MW;  7577A87D31BFDB04 CRC64;
     MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSIRSP AHALYPAASS
     STNCSRPNAT ASSSGLPEVP SARPGPTAPV IPPCPDVPPG LVGRVVIEFT SPMPLERVQR
     ENPGVLLGGR YTPPDCTPAQ TVAVIIPFRH REHHLRYWLH YLHPMLRRQR LRYGIYVINQ
     HGEETFNRAK LLNVGFLEAL KEDATYDCFI FSDVDLVPMD DRNLYRCGDQ PRHFAIAMDK
     FGFRLPYASY FGGVSGLSKA QFLRINGFPN EYWGWGGEDD DIFNRISLTG MKISRPDVRI
     GRYRMIKHDR DKHNEPNPQR FSKIQNTKLS MKWDGIGSLR YRVLEVSRQP LFTNITVDIG
     RPMSWLNQG
//