B3GT4_CANLF
ID B3GT4_CANLF Reviewed; 383 AA.
AC Q5TJE8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Beta-1,3-galactosyltransferase 4;
DE Short=Beta-1,3-GalTase 4;
DE Short=Beta3Gal-T4;
DE Short=Beta3GalT4;
DE Short=GalT4;
DE Short=b3Gal-T4;
DE EC=2.4.1.62 {ECO:0000250|UniProtKB:O96024};
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Doberman pinscher;
RX PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA Ollier W.E.R., Binns M.M.;
RT "Genomic sequence of the class II region of the canine MHC: comparison with
RT the MHC of other mammalian species.";
RL Genomics 85:48-59(2005).
CC -!- FUNCTION: Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
CC {ECO:0000250|UniProtKB:O96024}.
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:0000250|UniProtKB:Q9Z0F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16774;
CC Evidence={ECO:0000250|UniProtKB:Q9Z0F0};
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:0000250|UniProtKB:O88178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47569;
CC Evidence={ECO:0000250|UniProtKB:O88178};
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:0000250|UniProtKB:O88178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41961;
CC Evidence={ECO:0000250|UniProtKB:O88178};
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 -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AJ630366; CAI11440.1; -; Genomic_DNA.
DR RefSeq; NP_001074191.1; NM_001080722.1.
DR RefSeq; XP_005627127.1; XM_005627070.2.
DR RefSeq; XP_013973519.1; XM_014118044.1.
DR AlphaFoldDB; Q5TJE8; -.
DR SMR; Q5TJE8; -.
DR STRING; 9612.ENSCAFP00000037824; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q5TJE8; -.
DR Ensembl; ENSCAFT00845036965; ENSCAFP00845028946; ENSCAFG00845020962.
DR GeneID; 481737; -.
DR KEGG; cfa:481737; -.
DR CTD; 8705; -.
DR VEuPathDB; HostDB:ENSCAFG00845020962; -.
DR VGNC; VGNC:38335; B3GALT4.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000161798; -.
DR HOGENOM; CLU_036849_1_0_1; -.
DR InParanoid; Q5TJE8; -.
DR OMA; RCRVIAW; -.
DR OrthoDB; 1037602at2759; -.
DR TreeFam; TF318639; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Chromosome 12.
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; IBA:GO_Central.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IEA:Ensembl.
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 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..383
FT /note="Beta-1,3-galactosyltransferase 4"
FT /id="PRO_0000219159"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..383
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 383 AA; 42465 MW; 8CEBC3C3E3D3DAC1 CRC64;
MPLSLFRRLL LAALLLVIIW TLFGPSGIGE ELLSLSLASL SPAPASPGPP LALPRLLIPN
EKACGGPGSP PFLLILVCTA PENLNQRNAI RASWGGLREA QGFRVQILFL LGEPSLWHPT
KEPHDIDLVR EAAAQGDILQ AAFRDSYRNL TLKTLSGLNW ADKHCSMARY ILKTDDDVFV
NVPELVSELI RRGGHWEQWE KGKEPPRAVK AGDKEWEERP ILKSQPMPLL YLGRVHWRVH
PSRTPGSKHQ ISEEQWPPTW GPFPPYASGT GYVLSASAVQ LILKVASRAP PLPLEDVFVG
VSARRGGLTP THCVKLAGAT HYPLDRCCYG KFLLTSHKLD PWKMQEAWKL VGGSDGERTA
PFCSWLQEVL GILRCRVIAW LHS
