G3ST1_HUMAN
ID G3ST1_HUMAN Reviewed; 423 AA.
AC Q99999; Q96C63;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Galactosylceramide sulfotransferase {ECO:0000305};
DE Short=GalCer sulfotransferase {ECO:0000303|PubMed:10785389};
DE EC=2.8.2.11 {ECO:0000269|PubMed:8830034};
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase {ECO:0000303|PubMed:8830034};
DE AltName: Full=3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase {ECO:0000303|PubMed:9030544};
DE AltName: Full=Cerebroside sulfotransferase {ECO:0000250|UniProtKB:Q9JHE4};
GN Name=GAL3ST1 {ECO:0000312|HGNC:HGNC:24240};
GN Synonyms=CST {ECO:0000250|UniProtKB:Q9JHE4};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-14; 86-101; 102-105;
RP 187-192; 278-286; 372-379 AND 416-423, CATALYTIC ACTIVITY, FUNCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Renal cell carcinoma;
RX PubMed=9030544; DOI=10.1074/jbc.272.8.4864;
RA Honke K., Tsuda M., Hirahara Y., Ishii A., Makita A., Wada Y.;
RT "Molecular cloning and expression of cDNA encoding human 3'-
RT phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase.";
RL J. Biol. Chem. 272:4864-4868(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney proximal tubule;
RX PubMed=10785389; DOI=10.1046/j.1432-1327.2000.01281.x;
RA Tsuda M., Egashira M., Niikawa N., Wada Y., Honke K.;
RT "Cancer-associated alternative usage of multiple promoters of human GalCer
RT sulfotransferase gene.";
RL Eur. J. Biochem. 267:2672-2679(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-29.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-29.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=8830034; DOI=10.1093/oxfordjournals.jbchem.a021258;
RA Honke K., Yamane M., Ishii A., Kobayashi T., Makita A.;
RT "Purification and characterization of 3'-phosphoadenosine-5'-
RT phosphosulfate:GalCer sulfotransferase from human renal cancer cells.";
RL J. Biochem. 119:421-427(1996).
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 (PubMed:9030544, PubMed:8830034). Catalyzes the
CC synthesis of galactosylceramide sulfate (sulfatide), a major lipid
CC component of the myelin sheath and of monogalactosylalkylacylglycerol
CC sulfate (seminolipid), present in spermatocytes (PubMed:8830034). Seems
CC to prefer beta-glycosides at the non-reducing termini of sugar chains
CC attached to a lipid moiety (PubMed:8830034). Also acts on
CC lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl
CC diacylglycerol (in vitro) (PubMed:8830034).
CC {ECO:0000269|PubMed:8830034, ECO:0000269|PubMed:9030544}.
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:0000269|PubMed:8830034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20614;
CC Evidence={ECO:0000305|PubMed:8830034};
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:0000269|PubMed:8830034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41745;
CC Evidence={ECO:0000305|PubMed:8830034};
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:0000269|PubMed:9030544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43305;
CC Evidence={ECO:0000269|PubMed:9030544};
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:0000269|PubMed:8830034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41749;
CC Evidence={ECO:0000305|PubMed:8830034};
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:0000269|PubMed:8830034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41737;
CC Evidence={ECO:0000305|PubMed:8830034};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:8830034}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney proximal tubule, gastric mucosa
CC and adenocarcinoma (PubMed:9030544, PubMed:10785389). Highly expressed
CC in renal cell carcinoma cell lines (PubMed:9030544, PubMed:8830034).
CC {ECO:0000269|PubMed:10785389, ECO:0000269|PubMed:8830034,
CC ECO:0000269|PubMed:9030544}.
CC -!- SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; D88667; BAA13673.1; -; mRNA.
DR EMBL; AB029901; BAA89503.1; -; Genomic_DNA.
DR EMBL; CR456350; CAG30236.1; -; mRNA.
DR EMBL; BC014649; AAH14649.1; -; mRNA.
DR EMBL; BC019077; AAH19077.1; -; mRNA.
DR CCDS; CCDS13879.1; -.
DR RefSeq; NP_001305032.1; NM_001318103.1.
DR RefSeq; NP_001305033.1; NM_001318104.1.
DR RefSeq; NP_001305034.1; NM_001318105.1.
DR RefSeq; NP_001305035.1; NM_001318106.1.
DR RefSeq; NP_001305036.1; NM_001318107.1.
DR RefSeq; NP_001305037.1; NM_001318108.1.
DR RefSeq; NP_001305038.1; NM_001318109.1.
DR RefSeq; NP_001305039.1; NM_001318110.1.
DR RefSeq; NP_001305040.1; NM_001318111.1.
DR RefSeq; NP_001305041.1; NM_001318112.1.
DR RefSeq; NP_001305042.1; NM_001318113.1.
DR RefSeq; NP_001305043.1; NM_001318114.1.
DR RefSeq; NP_001305044.1; NM_001318115.1.
DR RefSeq; NP_001305045.1; NM_001318116.1.
DR RefSeq; NP_004852.1; NM_004861.2.
DR RefSeq; XP_016884587.1; XM_017029098.1.
DR AlphaFoldDB; Q99999; -.
DR BioGRID; 114891; 24.
DR IntAct; Q99999; 12.
DR MINT; Q99999; -.
DR STRING; 9606.ENSP00000385735; -.
DR SwissLipids; SLP:000000746; -.
DR GlyGen; Q99999; 5 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q99999; -.
DR PhosphoSitePlus; Q99999; -.
DR BioMuta; GAL3ST1; -.
DR MassIVE; Q99999; -.
DR MaxQB; Q99999; -.
DR PaxDb; Q99999; -.
DR PeptideAtlas; Q99999; -.
DR PRIDE; Q99999; -.
DR ProteomicsDB; 78572; -.
DR Antibodypedia; 243; 145 antibodies from 20 providers.
DR DNASU; 9514; -.
DR Ensembl; ENST00000338911.6; ENSP00000343234.5; ENSG00000128242.13.
DR Ensembl; ENST00000401975.5; ENSP00000384388.1; ENSG00000128242.13.
DR Ensembl; ENST00000402321.5; ENSP00000385735.1; ENSG00000128242.13.
DR Ensembl; ENST00000402369.5; ENSP00000384122.1; ENSG00000128242.13.
DR Ensembl; ENST00000406361.6; ENSP00000385207.1; ENSG00000128242.13.
DR Ensembl; ENST00000406955.5; ENSP00000385825.1; ENSG00000128242.13.
DR GeneID; 9514; -.
DR KEGG; hsa:9514; -.
DR MANE-Select; ENST00000406361.6; ENSP00000385207.1; NM_001318104.2; NP_001305033.1.
DR UCSC; uc003aih.2; human.
DR CTD; 9514; -.
DR DisGeNET; 9514; -.
DR GeneCards; GAL3ST1; -.
DR HGNC; HGNC:24240; GAL3ST1.
DR HPA; ENSG00000128242; Tissue enhanced (brain, intestine).
DR MIM; 602300; gene.
DR neXtProt; NX_Q99999; -.
DR OpenTargets; ENSG00000128242; -.
DR PharmGKB; PA134889661; -.
DR VEuPathDB; HostDB:ENSG00000128242; -.
DR eggNOG; ENOG502QTXT; Eukaryota.
DR GeneTree; ENSGT00950000182923; -.
DR HOGENOM; CLU_040616_1_1_1; -.
DR InParanoid; Q99999; -.
DR OMA; FHYFGRV; -.
DR OrthoDB; 1385827at2759; -.
DR PhylomeDB; Q99999; -.
DR TreeFam; TF314802; -.
DR BioCyc; MetaCyc:HS05164-MON; -.
DR BRENDA; 2.8.2.11; 2681.
DR PathwayCommons; Q99999; -.
DR SignaLink; Q99999; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 9514; 12 hits in 1061 CRISPR screens.
DR GeneWiki; GAL3ST1; -.
DR GenomeRNAi; 9514; -.
DR Pharos; Q99999; Tbio.
DR PRO; PR:Q99999; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q99999; protein.
DR Bgee; ENSG00000128242; Expressed in C1 segment of cervical spinal cord and 130 other tissues.
DR ExpressionAtlas; Q99999; baseline and differential.
DR Genevisible; Q99999; HS.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0050694; F:galactose 3-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0001733; F:galactosylceramide sulfotransferase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0042552; P:myelination; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006665; P:sphingolipid metabolic process; IDA: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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..423
FT /note="Galactosylceramide sulfotransferase"
FT /id="PRO_0000085201"
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 CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 29
FT /note="V -> M (in dbSNP:rs2267161)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_013684"
FT CONFLICT 281..282
FT /note="RR -> LN (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="R -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="R -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48764 MW; 0FD4F2E374447C56 CRC64;
MLPPQKKPWE SMAKGLVLGA LFTSFLLLVY SYAVPPLHAG LASTTPEAAA SCSPPALEPE
AVIRANGSAG ECQPRRNIVF LKTHKTASST LLNILFRFGQ KHRLKFAFPN GRNDFDYPTF
FARSLVQDYR PGACFNIICN HMRFHYDEVR GLVPTNAIFI TVLRDPARLF ESSFHYFGPV
VPLTWKLSAG DKLTEFLQDP DRYYDPNGFN AHYLRNLLFF DLGYDNSLDP SSPQVQEHIL
EVERRFHLVL LQEYFDESLV LLKDLLCWEL EDVLYFKLNA RRDSPVPRLS GELYGRATAW
NMLDSHLYRH FNASFWRKVE AFGRERMARE VAALRHANER MRTICIDGGH AVDAAAIQDE
AMQPWQPLGT KSILGYNLKK SIGQRHAQLC RRMLTPEIQY LMDLGANLWV TKLWKFIRDF
LRW
