G3ST1_BOVIN
ID G3ST1_BOVIN Reviewed; 423 AA.
AC A6QNK1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Galactosylceramide sulfotransferase;
DE Short=GalCer sulfotransferase {ECO:0000250|UniProtKB:Q99999};
DE EC=2.8.2.11 {ECO:0000250|UniProtKB:Q99999};
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase {ECO:0000250|UniProtKB:Q99999};
DE AltName: Full=3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase {ECO:0000250|UniProtKB:Q99999};
DE AltName: Full=Cerebroside sulfotransferase {ECO:0000250|UniProtKB:Q9JHE4};
GN Name=GAL3ST1 {ECO:0000250|UniProtKB:Q99999};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a sulfate group to position 3 of
CC non-reducing beta-galactosyl residues in glycerolipids and
CC sphingolipids, therefore participates in the biosynthesis of
CC sulfoglycolipids. Catalyzes the synthesis of galactosylceramide sulfate
CC (sulfatide), a major lipid component of the myelin sheath and of
CC monogalactosylalkylacylglycerol sulfate (seminolipid), present in
CC spermatocytes. Seems to prefer beta-glycosides at the non-reducing
CC termini of sugar chains attached to a lipid moiety. Also acts on
CC lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl
CC diacylglycerol (in vitro). {ECO:0000250|UniProtKB:Q99999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a beta-D-galactosyl-(1<->1')-N-
CC acylsphing-4-enine = adenosine 3',5'-bisphosphate + H(+) + N-acyl-1-
CC beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine; Xref=Rhea:RHEA:20613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18390, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:75956; EC=2.8.2.11;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20614;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a 1-O-alkyl-2-acyl-3-O-(beta-D-
CC galactosyl)-sn-glycerol = a 1-O-alkyl-2-acyl-3-(beta-D-3-
CC sulfogalactosyl)-sn-glycerol + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:41744, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:78428, ChEBI:CHEBI:78429; EC=2.8.2.11;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41745;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + beta-D-Gal-(1<->1')-Cer = 1-(3-O-
CC sulfo-beta-D-galactosyl)-ceramide + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:43304, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:82953, ChEBI:CHEBI:143593;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43305;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a 1,2-diacyl-3-O-(beta-D-
CC galactosyl)-sn-glycerol = 1,2-diacyl-3-(3-O-sulfo-beta-D-galactosyl)-
CC sn-glycerol + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:41748, ChEBI:CHEBI:15378, ChEBI:CHEBI:17615,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:157618;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41749;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a beta-D-Gal-(1->4)-beta-D-Glc-
CC (1<->1)-Cer(d18:1(4E)) = adenosine 3',5'-bisphosphate + beta-D-3-
CC sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine
CC + H(+); Xref=Rhea:RHEA:41736, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:78426;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41737;
CC Evidence={ECO:0000250|UniProtKB:Q99999};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q99999}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; BC148870; AAI48871.1; -; mRNA.
DR RefSeq; NP_001095442.1; NM_001101972.1.
DR AlphaFoldDB; A6QNK1; -.
DR STRING; 9913.ENSBTAP00000048547; -.
DR PaxDb; A6QNK1; -.
DR GeneID; 513295; -.
DR KEGG; bta:513295; -.
DR CTD; 9514; -.
DR eggNOG; ENOG502QTXT; Eukaryota.
DR InParanoid; A6QNK1; -.
DR OrthoDB; 1385827at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000009136; 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:0050694; F:galactose 3-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0001733; F:galactosylceramide sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006681; P:galactosylceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR009729; Gal-3-0_sulfotransfrase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR14647; PTHR14647; 1.
DR Pfam; PF06990; Gal-3-0_sulfotr; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Lipid metabolism; Membrane;
KW Reference proteome; Signal-anchor; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..423
FT /note="Galactosylceramide sulfotransferase"
FT /id="PRO_0000315388"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..423
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 48..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 423 AA; 48754 MW; C987BABD661282A7 CRC64;
MPLPQKKRWE SMAKGLVLGA LFTSFLLLLY SYAVPPLYTG LASTTPEGAA PCSPAPREPE
APTSANGSAG GCQPRRDIVF MKTHKTASST LLNILFRFGQ KHGLKFAFPN GRNDFDYPAF
FARSLVQDYR PGACFNIICN HMRFHYDEVR GLVAPNATFI TVLRDPARLF ESSFHYFGSV
VPFTWKLSGR DKLAEFLQDP DRYYDARGYN AHYLRNLLFF DLGYDSDLDP SSPQVQEHIL
EVERHFHLVL LQEYFDESLV LLKDLLCWEL EDVLYFKLNA RRASAVPRLS GELYRRATAW
NVLDARLYRH FNASFWRKVE AFGRERMARE VAALRRANER MRRICIDGGR AVDAAAIEDS
AMQPWQPLGA KSILGYNLKK SIGQRHAQLC RRMLTPEIQY LMDLGANLWI TKLWKFIRDF
LRW
