B3GT2_PONAB
ID B3GT2_PONAB Reviewed; 422 AA.
AC Q5R5Y3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Beta-1,3-galactosyltransferase 2;
DE Short=Beta-1,3-GalTase 2;
DE Short=Beta3Gal-T2;
DE Short=Beta3GalT2;
DE EC=2.4.1.86 {ECO:0000250|UniProtKB:O43825};
DE AltName: Full=UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase 2;
GN Name=B3GALT2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Can also utilize substrates with a terminal
CC galactose residue, albeit with lower efficiency. Involved in the
CC biosynthesis of the carbohydrate moieties of glycolipids and
CC glycoproteins. Inactive towards substrates with terminal alpha-N-
CC acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-
CC GalNAc) residues. {ECO:0000250|UniProtKB:O43825}.
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:O43825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433;
CC Evidence={ECO:0000250|UniProtKB:O43825};
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:O43825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046;
CC Evidence={ECO:0000250|UniProtKB:O43825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) + UDP-
CC alpha-D-galactose = a neolactoside IV(3)-beta-[Gal-beta-(1->3)-
CC GlcNAc]-nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41936,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:78565, ChEBI:CHEBI:142448;
CC Evidence={ECO:0000250|UniProtKB:O43825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41937;
CC Evidence={ECO:0000250|UniProtKB:O43825};
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}.
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; CR860718; CAH92833.1; -; mRNA.
DR RefSeq; NP_001126654.1; NM_001133182.1.
DR AlphaFoldDB; Q5R5Y3; -.
DR SMR; Q5R5Y3; -.
DR STRING; 9601.ENSPPYP00000000448; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GeneID; 100173654; -.
DR KEGG; pon:100173654; -.
DR CTD; 8707; -.
DR eggNOG; KOG2287; Eukaryota.
DR InParanoid; Q5R5Y3; -.
DR OrthoDB; 1037602at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR045821; B3GT2_N.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF19341; B3GALT2_N; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..422
FT /note="Beta-1,3-galactosyltransferase 2"
FT /id="PRO_0000219152"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..422
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 90..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 422 AA; 49239 MW; F28CEDC31C4A9717 CRC64;
MLQWRRRHCC FAKMTWNAKR SLFRTHLIGV LSLVFLFAMF LFFNHHDWLP GRAGFKENPV
TYTFRGFRST KSETNHSSLR NIWKETVPQT LRPQTATNSN NTDLSPQGVT GLENTLSANG
SIYNEKGTGY PNSYHFKYII NEPEKCQEKS PFLILLIAAE PGQIEARRAI RQTWGNESLA
PGIQITRIFL LGLSIKLNGY LQRAILEESR QYHDIIQQEY LDTYYNLTIK TLMGMNWVAT
YCPHIPYVMK TDSDMFVNTE YLINKLLKPD LPPRHNYFTG YLMRGYAPNR NKDSKWYMPP
DLYPSERYPV FCSGTGYVFS GDLAEKIFKV SLGIRRLHLE DVYVGICLAK LRIDPVPPPN
EFVFNHWRVS YSSCKYSHLI TSHQFQPSEL IKYWNHLQQN KHNACANAAK EKAGRYRHRK
LH