B3GT1_GORGO
ID B3GT1_GORGO Reviewed; 326 AA.
AC Q7JK24;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Beta-1,3-galactosyltransferase 1;
DE Short=Beta-1,3-GalTase 1;
DE Short=Beta3Gal-T1;
DE Short=Beta3GalT1;
DE EC=2.4.1.86 {ECO:0000250|UniProtKB:Q9Y5Z6};
DE AltName: Full=UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1;
GN Name=B3GALT1;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
CC -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC UDP-galactose to substrates with a terminal beta-N-acetylglucosamine
CC (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate
CC moieties of glycolipids and glycoproteins.
CC {ECO:0000250|UniProtKB:Q9Y5Z6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133506; EC=2.4.1.86;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Z6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Z6};
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 beta-D-Gal-(1->3)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) +
CC H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914; EC=2.4.1.86;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Z6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Z6};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AB041410; BAA94495.1; -; Genomic_DNA.
DR RefSeq; XP_004032783.1; XM_004032735.2.
DR AlphaFoldDB; Q7JK24; -.
DR SMR; Q7JK24; -.
DR STRING; 9593.ENSGGOP00000007931; -.
DR Ensembl; ENSGGOT00000008148; ENSGGOP00000007931; ENSGGOG00000008115.
DR GeneID; 101153312; -.
DR KEGG; ggo:101153312; -.
DR CTD; 8708; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000156219; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q7JK24; -.
DR OMA; CEKNAPF; -.
DR OrthoDB; 1037602at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001519; Chromosome 2B.
DR Bgee; ENSGGOG00000008115; Expressed in prefrontal cortex and 2 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002659; Glyco_trans_31.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Beta-1,3-galactosyltransferase 1"
FT /id="PRO_0000219144"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..326
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 326 AA; 37993 MW; 83271E99B2EE74F5 CRC64;
MASKVSCLYV LTVVCWASAL WYLSITRPTS SYTGSKPFSH LTVARKNFTF GNIRTRPINP
HSFEFLINEP NKCEKNIPFL VILISTTHKE FDARQAIRET WGDENNFKGI KIATLFLLGK
NADPVLNQMV EQESQIFHDI IVEDFIDSYH NLTLKTLMGM RWVATFCSKA KYVMKTDSDI
FVNMDNLIYK LLKPSTKPRR RYFTGYVING GPIRDVRSKW YMPRDLYPDS NYPPFCSGTG
YIFSADVAEL IYKTSLHTRL LHLEDVYVGL CLRKLGIHPF QNSGFNHWKM AYSLCRYRRV
ITVHQISPEE MHRIWNDMSS KKHLRC
