CHST3_MOUSE
ID CHST3_MOUSE Reviewed; 472 AA.
AC O88199; Q794I5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Carbohydrate sulfotransferase 3 {ECO:0000305|PubMed:9597547};
DE EC=2.8.2.17 {ECO:0000269|PubMed:11696535, ECO:0000269|PubMed:9597547};
DE EC=2.8.2.21 {ECO:0000269|PubMed:11696535};
DE AltName: Full=Chondroitin 6-O-sulfotransferase 1;
DE Short=C6ST-1;
DE AltName: Full=Chondroitin 6-sulfotransferase {ECO:0000303|PubMed:9597547};
DE Short=C6ST {ECO:0000303|PubMed:9597547};
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0;
DE Short=GST-0;
GN Name=Chst3; Synonyms=C6st, Gst0;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9597547; DOI=10.1093/glycob/8.5.489;
RA Uchimura K., Kadomatsu K., Fan Q.-W., Muramatsu H., Kurosawa N., Kaname T.,
RA Yamamura K., Fukuta M., Habuchi O., Muramatsu T.;
RT "Mouse chondroitin 6-sulfotransferase: molecular cloning, characterization
RT and chromosomal mapping.";
RL Glycobiology 8:489-496(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=11696535; DOI=10.1074/jbc.m104719200;
RA Uchimura K., Kadomatsu K., Nishimura H., Muramatsu H., Nakamura E.,
RA Kurosawa N., Habuchi O., El-Fasakhany F.M., Yoshikai Y., Muramatsu T.;
RT "Functional analysis of the chondroitin 6-sulfotransferase gene in relation
RT to lymphocyte subpopulations, brain development, and oversulfated
RT chondroitin sulfates.";
RL J. Biol. Chem. 277:1443-1450(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the transfer of sulfate to
CC position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin
CC (PubMed:9597547, PubMed:11696535). Chondroitin sulfate constitutes the
CC predominant proteoglycan present in cartilage and is distributed on the
CC surfaces of many cells and extracellular matrices (PubMed:9597547).
CC Catalyzes with a lower efficiency the sulfation of Gal residues of
CC keratan sulfate, another glycosaminoglycan (PubMed:11696535). Can also
CC catalyze the sulfation of the Gal residues in sialyl N-
CC acetyllactosamine (sialyl LacNAc) oligosaccharides (By similarity). May
CC play a role in the maintenance of naive T-lymphocytes in the spleen
CC (PubMed:11696535). {ECO:0000250|UniProtKB:Q92179,
CC ECO:0000269|PubMed:11696535, ECO:0000269|PubMed:9597547,
CC ECO:0000303|PubMed:9597547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+);
CC Xref=Rhea:RHEA:11108, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9828,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:62065; EC=2.8.2.17;
CC Evidence={ECO:0000269|PubMed:11696535, ECO:0000269|PubMed:9597547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11109;
CC Evidence={ECO:0000269|PubMed:11696535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-
CC bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21;
CC Evidence={ECO:0000269|PubMed:11696535};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen, lung,
CC eye and stomach. Constitutively expressed at low level during the
CC mid- to late-gestation period. Expressed in the brain in a temporally
CC controlled manner: peaks at 2 weeks after birth in the cerebellum, but
CC at 3 weeks in the cerebrum. Localizes to stromal cells in the bone
CC marrow, and stromal cells in the marginal zone and red pulp of the
CC spleen, but the sense probe did not. {ECO:0000269|PubMed:9597547}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92179}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable through adulthood. In their
CC spleen the level of chondroitin 6'-sulfate is almost undetectable. In
CC the spleen of 5-6 week-old mice, the number of CD62L(+)CD44(low) T-
CC lymphocytes corresponding to naive T-lymphocytes is significantly
CC decreased, whereas those in other secondary lymphoid organs are
CC unchanged. {ECO:0000269|PubMed:11696535}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; AB008937; BAA29054.1; -; mRNA.
DR EMBL; AB008938; BAA29055.1; -; mRNA.
DR EMBL; AB062109; BAB72166.1; -; Genomic_DNA.
DR EMBL; BC055055; AAH55055.1; -; mRNA.
DR RefSeq; NP_058083.2; NM_016803.3.
DR AlphaFoldDB; O88199; -.
DR STRING; 10090.ENSMUSP00000126281; -.
DR GlyGen; O88199; 6 sites.
DR PhosphoSitePlus; O88199; -.
DR MaxQB; O88199; -.
DR PaxDb; O88199; -.
DR PRIDE; O88199; -.
DR ProteomicsDB; 283837; -.
DR Antibodypedia; 29214; 183 antibodies from 30 providers.
DR DNASU; 53374; -.
DR Ensembl; ENSMUST00000068690; ENSMUSP00000065010; ENSMUSG00000057337.
DR Ensembl; ENSMUST00000167915; ENSMUSP00000131532; ENSMUSG00000057337.
DR GeneID; 53374; -.
DR KEGG; mmu:53374; -.
DR CTD; 9469; -.
DR MGI; MGI:1858224; Chst3.
DR VEuPathDB; HostDB:ENSMUSG00000057337; -.
DR eggNOG; ENOG502QWEX; Eukaryota.
DR GeneTree; ENSGT00940000161045; -.
DR HOGENOM; CLU_028381_3_2_1; -.
DR InParanoid; O88199; -.
DR OMA; QFDKWRF; -.
DR PhylomeDB; O88199; -.
DR BRENDA; 2.8.2.17; 3474.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 53374; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Chst3; mouse.
DR PRO; PR:O88199; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O88199; protein.
DR Bgee; ENSMUSG00000057337; Expressed in retinal neural layer and 54 other tissues.
DR ExpressionAtlas; O88199; baseline and differential.
DR Genevisible; O88199; MM.
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:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0008459; F:chondroitin 6-sulfotransferase activity; IDA:MGI.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050698; F:proteoglycan sulfotransferase activity; IMP:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:MGI.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="Carbohydrate sulfotransferase 3"
FT /id="PRO_0000085189"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..472
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 135..141
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 295..303
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 53997 MW; F021147196D9D339 CRC64;
MEKGLALPQD FRDLVHSLKI RGRYVLFLAF VVIVFIFIEK ENKIISRVSD KLKQIPHFVA
DANSTDPALL LSENASLLSL SELDSTFSHL RSRLHNLSLQ LGVEPAMESQ EAGAEKPSQQ
AGAGTRRHVL LMATTRTGSS FVGEFFNQQG NIFYLFEPLW HIERTVFFQQ RGASAAGSAL
VYRDVLKQLL LCDLYVLEPF ISPPPEDHLT QFLFRRGSSR SLCEDPVCTP FVKKVFEKYH
CRNRRCGPLN VTLAGEACRR KDHVALKAVR IRQLEFLQPL VEDPRLDLRV IQLVRDPRAV
LASRIVAFAG KYENWKKWLS EGQDQLSEDE VQRLRGNCES IRLSAELGLR QPAWLRGRYM
LVRYEDVARR PLQKAREMYS FAGIPLTPQV EDWIQKNTQA TRDSSDVYST QKNSSEQFEK
WRFSMPFKLA QVVQAACGPT MHLFGYKLAR DAASLTNRSI SLLEERGTFW VT
