Reviewed, UniProtKB/Swiss-Prot Q9JHE4 (G3ST1_MOUSE)

Names and origin

Protein names

Recommended name:
    Galactosylceramide sulfotransferase
      Short name=GalCer sulfotransferase
    EC=2.8.2.11
Alternative name(s):
    Cerebroside sulfotransferase
    3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase
    3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase

Gene names

Name:	Gal3st1
Synonyms:	Cst, Gcst

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the sulfation of membrane glycolipids. Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Catalyzes the synthesis of HSO3-3-galactosylceramide (sulfatide), a major lipid component of the myelin sheath and of HSO3-3-monogalactosylalkylacylglycerol (seminolipid), present in spermatocytes. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro). Ref.4
Catalytic activity	3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate. 3'-phosphoadenylyl sulfate + monogalactosylalkylacylglycerol = adenosine 3',5'-bisphosphate + monogalactosylalkylacylglycerol sulfate.
Pathway	Lipid metabolism; sphingolipid metabolism.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Expressed in brain, testis, kidney, stomach, small intestine, liver, and lung. Not detected in heart, skeletal muscle, and spleen. Ref.1
Miscellaneous	Mice homozygous for a null mutation of the CST gene display hindlimb weakness from week 6 of age and subsequently show a prenounced tremor and progressive ataxia. Myelin vacuolation is observed in the cerebellar white matter, diencephalon, brainstem and spinal anterior column. Male mice were infertile due to a blocked spermatogenesis.
Sequence similarities	Belongs to the galactose-3-O-sulfotransferase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	galactosylceramide biosynthetic process Ref.1 Inferred from direct assay. Source: MGI myelination Ref.4 Inferred from mutant phenotype. Source: MGI spermatogenesis Ref.4 Inferred from mutant phenotype. Source: MGI
Cellular component	Golgi membrane Ref.4 Traceable author statement. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	galactosylceramide sulfotransferase activity Ref.1 Ref.4 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 423	423	Galactosylceramide sulfotransferase		PRO_0000085202
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 35	23	Signal-anchor for type II membrane protein Potential
	Topological domain	36 – 423	388	Lumenal Potential
Amino acid modifications
	Glycosylation	66	1	N-linked (GlcNAc...) Potential
	Glycosylation	312	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	18	1	L → P in BAB25160. Ref.2
	Sequence conflict	263	1	R → Q in BAB25160. Ref.2
	Sequence conflict	271	1	E → K in BAB25160. Ref.2
	Sequence conflict	358	1	Q → R in BAA93009. Ref.1
	Sequence conflict	358	1	Q → R in BAA93008. Ref.1
	Sequence conflict	392	1	R → G in BAB25160. Ref.2
	Sequence conflict	398	1	I → T in BAA93009. Ref.1
	Sequence conflict	398	1	I → T in BAA93008. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9JHE4-1 [UniParc]. Last modified July 26, 2002. Version 2. Checksum: FD54A1A71F4AEE46	FASTA	423	48,968
	10 20 30 40 50 60 MTLLPKKPCK SKAKGLLLGA LFTSFLLLLY SYVVPPLYPN MAFTTSEAAA PCSPIPNEPV 70 80 90 100 110 120 AATPANGSAG GCQPRRDIVF MKTHKTASST LLNILFRFGQ KHELKFAFPN GRNDFHYPSY 130 140 150 160 170 180 FARSLVQDYR PGACFNIICN HMRFHYEEVR GLVRPGATFI TVIRDPARLF ESSFHYFGSV 190 200 210 220 230 240 VPLTWKLSSR DKLAEFLQDP DRYYDPSSYN AHYLRNLLFF DLGYDSSLDP ASPRVQEHIL 250 260 270 280 290 300 EVERRFHLVL LQEYFDESLV LLRELLCWDL EDVLYFKLNA RRDSPVPRLS GELYRRATAW 310 320 330 340 350 360 NLLDVRLYRH FNASFWRKVE AFGRERMARE VAELRQANEH MRHICIDGGQ AVGAEAIQDS 370 380 390 400 410 420 AMQPWQPLGI KSILGYNLKK SIGPQHEQLC RRMLTPEIQY LSDLGANLWV TKLWKFLRDF LRW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, genomic cloning, and tissue-specific regulation of mouse cerebroside sulfotransferase." Hirahara Y., Tsuda M., Wada Y., Honke K. Eur. J. Biochem. 267:1909-1917(2000) [PubMed: 10727929] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY. Tissue: Kidney.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Pancreas.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[4]	"Paranodal junction formation and spermatogenesis require sulfoglycolipids." Honke K., Hirahara Y., Dupree J., Suzuki K., Popko B., Fukushima K., Fukushima J., Nagasawa T., Yoshida N., Wada Y., Taniguchi N. Proc. Natl. Acad. Sci. U.S.A. 99:4227-4232(2002) [PubMed: 11917099] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB032940 Genomic DNA. Translation: BAA93009.1. AB032939 mRNA. Translation: BAA93008.1. AK007645 mRNA. Translation: BAB25160.1. BC026806 mRNA. Translation: AAH26806.1.
IPI	IPI00310026.
RefSeq	NP_058618.2.
UniGene	Mm.103414
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JHE4.
Proteomic databases
PRIDE	Q9JHE4.
Genome annotation databases
Ensembl	ENSMUST00000063004; ENSMUSP00000058348; ENSMUSG00000049721; Mus musculus. [Genome view] ENSMUST00000078757; ENSMUSP00000077815; ENSMUSG00000049721; Mus musculus. [Genome view] ENSMUST00000109981; ENSMUSP00000105608; ENSMUSG00000049721; Mus musculus. [Genome view]
GeneID	53897.
KEGG	mmu:53897.
UCSC	uc007hub.1. mouse.
Organism-specific databases
CTD	53897.
MGI	MGI:1858277. Gal3st1.
Phylogenomic databases
HOGENOM	Q9JHE4.
HOVERGEN	Q9JHE4.
OMA	IQDSAMQ.
Enzyme and pathway databases
BRENDA	2.8.2.11. 244.
Gene expression databases
ArrayExpress	Q9JHE4.
Bgee	Q9JHE4.
CleanEx	MM_GAL3ST1.
Genevestigator	Q9JHE4.
GermOnline	ENSMUSG00000049721. Mus musculus.
Family and domain databases
InterPro	IPR009729. Gal-3-0_sulfotransfrase. [Graphical view]
PANTHER	PTHR14647. Gal-3-0_sulfotr. 1 hit.
Pfam	PF06990. Gal-3-0_sulfotr. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	310799.
SOURCE	Search...

Entry information

Entry name

G3ST1_MOUSE

Accession

Primary (citable) accession number: Q9JHE4
Secondary accession number(s): Q9D8V6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	July 26, 2002
Last modified:	November 3, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)