B3GT4_RAT
ID B3GT4_RAT Reviewed; 371 AA.
AC O88178;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Beta-1,3-galactosyltransferase 4;
DE Short=Beta-1,3-GalTase 4;
DE Short=Beta3Gal-T4;
DE Short=Beta3GalT4;
DE Short=b3Gal-T4;
DE EC=2.4.1.62 {ECO:0000269|PubMed:9312075};
DE AltName: Full=Gal-T2;
DE AltName: Full=Ganglioside galactosyltransferase;
DE AltName: Full=UDP-galactose:beta-N-acetyl-galactosamine-beta-1,3-galactosyltransferase;
GN Name=B3galt4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9312075; DOI=10.1074/jbc.272.40.24794;
RA Miyazaki H., Fukumoto S., Okada M., Hasegawa T., Furukawa K., Furukawa K.;
RT "Expression cloning of rat cDNA encoding UDP-galactose:GD2 beta1,3-
RT galactosyltransferase that determines the expression of GD1b/GM1/GA1.";
RL J. Biol. Chem. 272:24794-24799(1997).
CC -!- FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
CC {ECO:0000269|PubMed:9312075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 (d18:1(4E)) + UDP-alpha-D-galactose =
CC ganglioside GM1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16773,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:71502, ChEBI:CHEBI:77709; EC=2.4.1.62;
CC Evidence={ECO:0000269|PubMed:9312075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16774;
CC Evidence={ECO:0000305|PubMed:9312075};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 + UDP-alpha-D-galactose = ganglioside GM1 +
CC H(+) + UDP; Xref=Rhea:RHEA:48280, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:79218,
CC ChEBI:CHEBI:82639; Evidence={ECO:0000250|UniProtKB:Q9Z0F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48281;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD2 (d18:1(4E)) + UDP-alpha-D-galactose =
CC ganglioside GD1b (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:47568,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:78542, ChEBI:CHEBI:87785;
CC Evidence={ECO:0000269|PubMed:9312075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47569;
CC Evidence={ECO:0000305|PubMed:9312075};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA2 (d18:1(4E)) + UDP-alpha-D-galactose =
CC ganglioside GA1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41960,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27731, ChEBI:CHEBI:27938,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914;
CC Evidence={ECO:0000269|PubMed:9312075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41961;
CC Evidence={ECO:0000305|PubMed:9312075};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9Z0F0}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in thymus, spleen, kidney and
CC testis and, to a lesser extent, in brain and liver.
CC {ECO:0000269|PubMed:9312075}.
CC -!- DEVELOPMENTAL STAGE: In the embryonic brain, expression begins at day
CC 12 and continues until birth. Expression is maintained at low levels in
CC adult brain. {ECO:0000269|PubMed:9312075}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AB003478; BAA32045.1; -; mRNA.
DR AlphaFoldDB; O88178; -.
DR SMR; O88178; -.
DR STRING; 10116.ENSRNOP00000000550; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; O88178; 1 site.
DR PaxDb; O88178; -.
DR UCSC; RGD:620328; rat.
DR RGD; 620328; B3galt4.
DR eggNOG; KOG2287; Eukaryota.
DR InParanoid; O88178; -.
DR PhylomeDB; O88178; -.
DR Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:O88178; -.
DR Proteomes; UP000002494; Unplaced.
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:0047915; F:ganglioside 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; ISO:RGD.
DR GO; GO:0001574; P:ganglioside biosynthetic process; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..371
FT /note="Beta-1,3-galactosyltransferase 4"
FT /id="PRO_0000219162"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..371
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 371 AA; 41254 MW; 327FB76EFDACF131 CRC64;
MPLSLFRRLL LAVLLLVIIW TLFGPSGLGE ELLSLSLASL LPAPASPGPP LALPRLLIPN
PQACGGSGPP PFLLILVCTA PEHLNQRNAI RGSWGAIREA RGFRVQTLFL LGEPMGQQFA
DLASESAAQG DVLQASFQDS YRNLTLKTLT GLNWVNKYCP MARYILKTDD DVYVNVPELV
SELIQRGGPS EQWQKGKEPQ EETTAVHKEH KGQAVPLLYL GRVHWRVRPT RTPESRHHVS
EELWPENWGP FPPYASGTGY VLSISAVQLI LKVASRAPYL PLEDVFVGVS ARRVGLAPTH
CVKLAGATHY PLDRCCYGKF LLTSHKVDPW KMQEAWKLVR GLNGRRTEPF CSWLQGFLGT
LRCRFIAWLN S
