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   24-JAN-2024, entry version 142.
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   GlyCosmos; Q80WV3; 3 sites, No reported glycans.
DR   GlyGen; Q80WV3; 3 sites.
DR   PhosphoSitePlus; Q80WV3; -.
DR   EPD; Q80WV3; -.
DR   MaxQB; Q80WV3; -.
DR   PaxDb; 10090-ENSMUSP00000040775; -.
DR   PeptideAtlas; Q80WV3; -.
DR   ProteomicsDB; 281674; -.
DR   Antibodypedia; 2653; 256 antibodies from 27 providers.
DR   DNASU; 54371; -.
DR   Ensembl; ENSMUST00000036267.8; ENSMUSP00000040775.7; ENSMUSG00000033350.8.
DR   GeneID; 54371; -.
DR   KEGG; mmu:54371; -.
DR   UCSC; uc009raz.2; mouse.
DR   AGR; MGI:1891160; -.
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; KWRREPR; -.
DR   OrthoDB; 3031241at2759; -.
DR   PhylomeDB; Q80WV3; -.
DR   TreeFam; TF342871; -.
DR   Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR   UniPathway; UPA00353; -.
DR   BioGRID-ORCS; 54371; 1 hit in 79 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 233 other cell types or tissues.
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: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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR10704; CARBOHYDRATE SULFOTRANSFERASE; 1.
DR   PANTHER; PTHR10704:SF3; CARBOHYDRATE SULFOTRANSFERASE 2; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; Q80WV3; MM.
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
//