CHST2_MOUSE
ID CHST2_MOUSE Reviewed; 530 AA.
AC Q80WV3; E9QNG2; O88276; Q794G9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Carbohydrate sulfotransferase 2;
DE EC=2.8.2.- {ECO:0000269|PubMed:16227985};
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2;
DE Short=GST-2;
DE AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 1;
DE Short=GlcNAc6ST-1;
DE Short=Gn6st-1;
GN Name=Chst2; Synonyms=Gst2;
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, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=9712885; DOI=10.1074/jbc.273.35.22577;
RA Uchimura K., Muramatsu H., Kadomatsu K., Fan Q.-W., Kurosawa N.,
RA Mitsuoka C., Kannagi R., Habuchi O., Muramatsu T.;
RT "Molecular cloning and characterization of an N-acetylglucosamine-6-O-
RT sulfotransferase.";
RL J. Biol. Chem. 273:22577-22583(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15175329; DOI=10.1074/jbc.m404456200;
RA Uchimura K., Kadomatsu K., El-Fasakhany F.M., Singer M.S., Izawa M.,
RA Kannagi R., Takeda N., Rosen S.D., Muramatsu T.;
RT "N-acetylglucosamine 6-O-sulfotransferase-1 regulates expression of L-
RT selectin ligands and lymphocyte homing.";
RL J. Biol. Chem. 279:35001-35008(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 TISSUE SPECIFICITY.
RX PubMed=9722682; DOI=10.1093/oxfordjournals.jbchem.a022164;
RA Uchimura K., Muramatsu H., Kaname T., Ogawa H., Yamakawa T., Fan Q.-W.,
RA Mitsuoka C., Kannagi R., Habuchi O., Yokoyama I., Yamamura K., Ozaki T.,
RA Nakagawara A., Kadomatsu K., Muramatsu T.;
RT "Human N-acetylglucosamine-6-O-sulfotransferase involved in the
RT biosynthesis of 6-sulfo sialyl Lewis X: molecular cloning, chromosomal
RT mapping, and expression in various organs and tumor cells.";
RL J. Biochem. 124:670-678(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16227985; DOI=10.1038/ni1259;
RA Kawashima H., Petryniak B., Hiraoka N., Mitoma J., Huckaby V., Nakayama J.,
RA Uchimura K., Kadomatsu K., Muramatsu T., Lowe J.B., Fukuda M.;
RT "N-acetylglucosamine-6-O-sulfotransferases 1 and 2 cooperatively control
RT lymphocyte homing through L-selectin ligand biosynthesis in high
RT endothelial venules.";
RL Nat. Immunol. 6:1096-1104(2005).
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 non-reducing N-acetylglucosamine (GlcNAc) residues within
CC keratan-like structures on N-linked glycans and within mucin-associated
CC glycans that can ultimately serve as SELL ligands. SELL ligands are
CC present in high endothelial cells (HEVs) and play a central role in
CC lymphocyte homing at sites of inflammation. Participates in
CC biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in
CC lymphocyte homing to Peyer patches. Has no activity toward O-linked
CC sugars. Its substrate specificity may be influenced by its subcellular
CC location. Sulfates GlcNAc residues at terminal, non-reducing ends of
CC oligosaccharide chains. {ECO:0000269|PubMed:15175329,
CC ECO:0000269|PubMed:16227985, ECO:0000269|PubMed:9712885}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-threonyl-[protein] = 3-O-{6-O-sulfo-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-threonyl-[protein] + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67856, Rhea:RHEA-COMP:17368, Rhea:RHEA-
CC COMP:17369, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:176489, ChEBI:CHEBI:176492;
CC Evidence={ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67857;
CC Evidence={ECO:0000305|PubMed:16227985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-seryl-[protein] = 3-O-{6-O-sulfo-N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-seryl-[protein] + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67860, Rhea:RHEA-COMP:17365, Rhea:RHEA-
CC COMP:17366, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:176490, ChEBI:CHEBI:176491;
CC Evidence={ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67861;
CC Evidence={ECO:0000305|PubMed:16227985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-galactosyl-(1->3)-[N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-threonyl-[protein] = 3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-threonyl-[protein] + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67864, Rhea:RHEA-COMP:14420, Rhea:RHEA-COMP:17370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:139607, ChEBI:CHEBI:176493;
CC Evidence={ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67865;
CC Evidence={ECO:0000305|PubMed:16227985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-galactosyl-(1->3)-[N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-seryl-[protein] = 3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-seryl-[protein] + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67868, Rhea:RHEA-COMP:14419, Rhea:RHEA-COMP:17367,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:139605, ChEBI:CHEBI:176494;
CC Evidence={ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67869;
CC Evidence={ECO:0000305|PubMed:16227985};
CC -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC {ECO:0000269|PubMed:16227985}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homodimerization is not essential
CC for enzyme activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In brain, it is expressed in pyramidal cells in the
CC CA3 subregion of the hippocampus, cerebellar nucleus and Purkinje
CC cells. Expressed in peripheral lymph nodes.
CC {ECO:0000269|PubMed:16227985, ECO:0000269|PubMed:9712885,
CC ECO:0000269|PubMed:9722682}.
CC -!- DISRUPTION PHENOTYPE: Mice are impaired in the elaboration of sialyl 6-
CC sulfo Lewis X in HEV. Lymphocyte homing to peripheral lymph nodes,
CC mesenteric lymph nodes, and Peyer patches are significantly reduced.
CC Simultaneous knockdown of CHST4 and CHST2 results in lower contact
CC hypersensitivity response when compared to wild-type littermates.
CC {ECO:0000269|PubMed:15175329, ECO:0000269|PubMed:16227985}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-48 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51963.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA32137.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA32139.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD16775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB011451; BAA32137.1; ALT_INIT; mRNA.
DR EMBL; AB011452; BAA32138.1; -; mRNA.
DR EMBL; AB011452; BAA32139.1; ALT_INIT; mRNA.
DR EMBL; AB125058; BAD16775.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC144813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051963; AAH51963.2; ALT_INIT; mRNA.
DR CCDS; CCDS52888.1; -.
DR RefSeq; NP_061233.2; NM_018763.2.
DR AlphaFoldDB; Q80WV3; -.
DR STRING; 10090.ENSMUSP00000040775; -.
DR GlyGen; Q80WV3; 3 sites.
DR PhosphoSitePlus; Q80WV3; -.
DR EPD; Q80WV3; -.
DR MaxQB; Q80WV3; -.
DR PaxDb; Q80WV3; -.
DR PeptideAtlas; Q80WV3; -.
DR PRIDE; Q80WV3; -.
DR ProteomicsDB; 281674; -.
DR Antibodypedia; 2653; 228 antibodies from 26 providers.
DR DNASU; 54371; -.
DR Ensembl; ENSMUST00000036267; ENSMUSP00000040775; ENSMUSG00000033350.
DR GeneID; 54371; -.
DR KEGG; mmu:54371; -.
DR UCSC; uc009raz.2; mouse.
DR CTD; 9435; -.
DR MGI; MGI:1891160; Chst2.
DR VEuPathDB; HostDB:ENSMUSG00000033350; -.
DR eggNOG; ENOG502QTSD; Eukaryota.
DR GeneTree; ENSGT00940000161292; -.
DR HOGENOM; CLU_028381_1_0_1; -.
DR InParanoid; Q80WV3; -.
DR OMA; YCHQPMA; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q80WV3; -.
DR TreeFam; TF342871; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR UniPathway; UPA00353; -.
DR BioGRID-ORCS; 54371; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Chst2; mouse.
DR PRO; PR:Q80WV3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80WV3; protein.
DR Bgee; ENSMUSG00000033350; Expressed in supraoptic nucleus and 232 other tissues.
DR Genevisible; Q80WV3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:MGI.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO: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; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Inflammatory response; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..530
FT /note="Carbohydrate sulfotransferase 2"
FT /id="PRO_0000085187"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..530
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173..179
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 332..340
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 301
FT /note="L -> V (in Ref. 1; BAA32137/BAA32139/BAA32138 and 2;
FT BAD16775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 57828 MW; 275363BF15440730 CRC64;
MSRSSPRALP PGALPRPLPA APAAVQRALL PPWPRRAGRR WPASPLGMKV FRRKALVLCA
GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAVGAAG AGWGRPGSPP AAPPRAHSRM
DPRTPYRPPA AGVGAVPAAA AGSAGAAASL GNATRGTRGG GDKRQLVYVF TTWRSGSSFF
GELFNQNPEV FFLYEPVWHV WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG
GRNLTTLGIF GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT
LVIKGVRVFD VAVLAPLLKD PALDLKVIHL VRDPRAVASS RIRSRHGLIR ESLQVVRSRD
PRAHRMPFLE AAGHKLGAKK EGMGGPADYH ALGAMEVICN SMAKTLQTAL QPPDWLQGHY
LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE MEQFALNMTS GSGSSSKPFV VSARNATQAA
NAWRTALTFQ QIKQVEEFCY QPMAVLGYER VNSPEEVKDL SKTLLRKPRL
