B4GT2_CRIGR
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 03-AUG-2022, entry version 97.
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 = 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}.
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DR EMBL; AY117536; AAM77195.1; -; mRNA.
DR RefSeq; NP_001233623.1; NM_001246694.2.
DR RefSeq; XP_007641467.1; XM_007643277.2.
DR AlphaFoldDB; Q80WN9; -.
DR SMR; Q80WN9; -.
DR STRING; 10029.NP_001233623.1; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR Ensembl; ENSCGRT00001017640; ENSCGRP00001013403; ENSCGRG00001014544.
DR GeneID; 100689434; -.
DR KEGG; cge:100689434; -.
DR CTD; 8704; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000159367; -.
DR OMA; RCGEQPR; -.
DR OrthoDB; 1201618at2759; -.
DR UniPathway; UPA00378; -.
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:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
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; Signal-anchor; Transferase;
KW 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..77
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
