G3ST1_MOUSE
ID G3ST1_MOUSE Reviewed; 423 AA.
AC Q9JHE4; Q9D8V6;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Galactosylceramide sulfotransferase {ECO:0000305};
DE Short=GalCer sulfotransferase {ECO:0000250|UniProtKB:Q99999};
DE EC=2.8.2.11 {ECO:0000269|PubMed:11917099};
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:0000303|PubMed:10727929};
GN Name=Gal3st1 {ECO:0000312|MGI:MGI:1858277};
GN Synonyms=Cst {ECO:0000303|PubMed:10727929}, Gcst;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10727929; DOI=10.1046/j.1432-1327.2000.01139.x;
RA Hirahara Y., Tsuda M., Wada Y., Honke K.;
RT "cDNA cloning, genomic cloning, and tissue-specific regulation of mouse
RT cerebroside sulfotransferase.";
RL Eur. J. Biochem. 267:1909-1917(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=11917099; DOI=10.1073/pnas.032068299;
RA Honke K., Hirahara Y., Dupree J., Suzuki K., Popko B., Fukushima K.,
RA Fukushima J., Nagasawa T., Yoshida N., Wada Y., Taniguchi N.;
RT "Paranodal junction formation and spermatogenesis require
RT sulfoglycolipids.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4227-4232(2002).
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:11917099). Catalyzes the synthesis of
CC galactosylceramide sulfate (sulfatide), a major lipid component of the
CC myelin sheath and of monogalactosylalkylacylglycerol sulfate
CC (seminolipid), present in spermatocytes (PubMed:11917099). Seems to
CC prefer beta-glycosides at the non-reducing termini of sugar chains
CC attached to a lipid moiety. Also acts on lactosylceramide, galactosyl
CC 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro) (By
CC similarity). {ECO:0000250|UniProtKB:Q99999,
CC ECO:0000269|PubMed:11917099}.
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:11917099};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20614;
CC Evidence={ECO:0000269|PubMed:11917099};
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:11917099};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41745;
CC Evidence={ECO:0000269|PubMed:11917099};
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:0000269|PubMed:11917099}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis, kidney, stomach, small
CC intestine, liver, and lung. Not detected in heart, skeletal muscle, and
CC spleen. {ECO:0000269|PubMed:10727929}.
CC -!- DISRUPTION PHENOTYPE: Mice homozygous for a null mutation of the CST
CC gene born healthy and display hindlimb weakness from week 6 of age and
CC subsequently show a prenounced tremor and progressive ataxia. Myelin
CC vacuolation is observed in the cerebellar white matter, diencephalon,
CC brainstem and spinal anterior column. Male mice were infertile due to a
CC blocked spermatogenesis. {ECO:0000269|PubMed:11917099}.
CC -!- SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; AB032940; BAA93009.1; -; Genomic_DNA.
DR EMBL; AB032939; BAA93008.1; -; mRNA.
DR EMBL; AK007645; BAB25160.1; -; mRNA.
DR EMBL; BC026806; AAH26806.1; -; mRNA.
DR CCDS; CCDS24373.1; -.
DR RefSeq; NP_001171162.1; NM_001177691.1.
DR RefSeq; NP_001171174.1; NM_001177703.1.
DR RefSeq; NP_058618.2; NM_016922.3.
DR RefSeq; XP_006514819.2; XM_006514756.3.
DR RefSeq; XP_006514820.1; XM_006514757.3.
DR AlphaFoldDB; Q9JHE4; -.
DR STRING; 10090.ENSMUSP00000058348; -.
DR GlyGen; Q9JHE4; 2 sites.
DR iPTMnet; Q9JHE4; -.
DR PhosphoSitePlus; Q9JHE4; -.
DR PaxDb; Q9JHE4; -.
DR PRIDE; Q9JHE4; -.
DR ProteomicsDB; 273404; -.
DR Antibodypedia; 243; 145 antibodies from 20 providers.
DR DNASU; 53897; -.
DR Ensembl; ENSMUST00000063004; ENSMUSP00000058348; ENSMUSG00000049721.
DR Ensembl; ENSMUST00000078757; ENSMUSP00000077815; ENSMUSG00000049721.
DR Ensembl; ENSMUST00000109981; ENSMUSP00000105608; ENSMUSG00000049721.
DR GeneID; 53897; -.
DR KEGG; mmu:53897; -.
DR UCSC; uc007hub.2; mouse.
DR CTD; 9514; -.
DR MGI; MGI:1858277; Gal3st1.
DR VEuPathDB; HostDB:ENSMUSG00000049721; -.
DR eggNOG; ENOG502QTXT; Eukaryota.
DR GeneTree; ENSGT00950000182923; -.
DR HOGENOM; CLU_040616_1_1_1; -.
DR InParanoid; Q9JHE4; -.
DR OMA; FHYFGRV; -.
DR OrthoDB; 1385827at2759; -.
DR PhylomeDB; Q9JHE4; -.
DR TreeFam; TF314802; -.
DR BRENDA; 2.8.2.11; 3474.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 53897; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Casz1; mouse.
DR PRO; PR:Q9JHE4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JHE4; protein.
DR Bgee; ENSMUSG00000049721; Expressed in pyloric antrum and 171 other tissues.
DR Genevisible; Q9JHE4; MM.
DR GO; GO:0000139; C:Golgi membrane; TAS:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0050694; F:galactose 3-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0001733; F:galactosylceramide sulfotransferase activity; IDA:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IDA:MGI.
DR GO; GO:0006681; P:galactosylceramide metabolic process; IMP:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; TAS:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISO:MGI.
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 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_0000085202"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..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 CONFLICT 18
FT /note="L -> P (in Ref. 2; BAB25160)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="R -> Q (in Ref. 2; BAB25160)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="E -> K (in Ref. 2; BAB25160)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Q -> R (in Ref. 1; BAA93009/BAA93008)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="R -> G (in Ref. 2; BAB25160)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="I -> T (in Ref. 1; BAA93009/BAA93008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48968 MW; FD54A1A71F4AEE46 CRC64;
MTLLPKKPCK SKAKGLLLGA LFTSFLLLLY SYVVPPLYPN MAFTTSEAAA PCSPIPNEPV
AATPANGSAG GCQPRRDIVF MKTHKTASST LLNILFRFGQ KHELKFAFPN GRNDFHYPSY
FARSLVQDYR PGACFNIICN HMRFHYEEVR GLVRPGATFI TVIRDPARLF ESSFHYFGSV
VPLTWKLSSR DKLAEFLQDP DRYYDPSSYN AHYLRNLLFF DLGYDSSLDP ASPRVQEHIL
EVERRFHLVL LQEYFDESLV LLRELLCWDL EDVLYFKLNA RRDSPVPRLS GELYRRATAW
NLLDVRLYRH FNASFWRKVE AFGRERMARE VAELRQANEH MRHICIDGGQ AVGAEAIQDS
AMQPWQPLGI KSILGYNLKK SIGPQHEQLC RRMLTPEIQY LSDLGANLWV TKLWKFLRDF
LRW
