CHSTB_MOUSE
ID CHSTB_MOUSE Reviewed; 352 AA.
AC Q9JME2; Q9JJS2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Carbohydrate sulfotransferase 11;
DE EC=2.8.2.5;
DE AltName: Full=Chondroitin 4-O-sulfotransferase 1;
DE AltName: Full=Chondroitin 4-sulfotransferase 1;
DE Short=C4S-1;
DE Short=C4ST-1;
DE Short=C4ST1;
GN Name=Chst11;
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], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10722746; DOI=10.1074/jbc.275.12.8975;
RA Yamauchi S., Mita S., Matsubara T., Fukuta M., Habuchi H., Kimata K.,
RA Habuchi O.;
RT "Molecular cloning and expression of chondroitin 4-sulfotransferase.";
RL J. Biol. Chem. 275:8975-8981(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xia G., Evers M.R., Schachner M.;
RT "Cloning and expression of molecules homologous to HNK-1
RT sulfotransferase.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12351172; DOI=10.1016/s0925-4773(02)00198-3;
RA Klueppel M., Vallis K.A., Wrana J.L.;
RT "A high-throughput induction gene trap approach defines C4ST as a target of
RT BMP signaling.";
RL Mech. Dev. 118:77-89(2002).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-
CC acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin
CC sulfate constitutes the predominant proteoglycan present in cartilage
CC and is distributed on the surfaces of many cells and extracellular
CC matrices. Can also sulfate Gal residues in desulfated dermatan sulfate.
CC Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit.
CC Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is
CC used as an acceptor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+);
CC Xref=Rhea:RHEA:16101, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9829,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:58422; EC=2.8.2.5;
CC Evidence={ECO:0000269|PubMed:10722746};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain and kidney. Also
CC expressed at weaker level in heart, spleen and lung. Expressed in
CC developing chondrocytes. {ECO:0000269|PubMed:10722746}.
CC -!- DEVELOPMENTAL STAGE: First expressed at day 9.75 of embryogenesis in
CC the apical ectodermal ridge (AER) of the developing limb buds and at
CC the edges of branchial arches 1 and 2. Also expressed in the ventral
CC neural tube, notochord and sympathetic ganglia and the mesonephric
CC tubules of the developing kidneys. In the heart, it is expressed in the
CC myocardium of the atrium and in the endocardial cushions of both the
CC developing inflow tract and the atrioventricular valves. At day 15, it
CC is expressed in the cartilage of developing bones, in vertebrae and
CC cartilage of the trachea as well as in the thymus. In the forelimb, it
CC is expressed in all developing bones, but absent from developing joint
CC regions and was down-regulated in chondrocytes beginning to undergo
CC mineralization, such as in the center of the ulna. At day 15, no
CC expression in the neural tube is observed. In the heart at day 15, it
CC is still expressed in the atrial valve, the atrioventricular valves and
CC in the myocardium of the atrium, while in the kidney, it is expressed
CC in the collecting tubules as well as in Bowman capsule. Interestingly,
CC the liver displays a punctate expression at day 15. Also expressed in
CC tooth primordia, hair follicles and mammary glands.
CC {ECO:0000269|PubMed:12351172}.
CC -!- INDUCTION: By BMP2, suggesting it is a target of BMP signaling.
CC {ECO:0000269|PubMed:12351172}.
CC -!- PTM: N-glycosylated; required for activity and stability.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AB030378; BAA92942.1; -; mRNA.
DR EMBL; AJ289133; CAB92141.1; -; mRNA.
DR CCDS; CCDS24074.1; -.
DR RefSeq; NP_067414.2; NM_021439.2.
DR AlphaFoldDB; Q9JME2; -.
DR STRING; 10090.ENSMUSP00000045349; -.
DR GlyGen; Q9JME2; 4 sites.
DR iPTMnet; Q9JME2; -.
DR PhosphoSitePlus; Q9JME2; -.
DR MaxQB; Q9JME2; -.
DR PaxDb; Q9JME2; -.
DR PRIDE; Q9JME2; -.
DR ProteomicsDB; 281679; -.
DR Antibodypedia; 30604; 185 antibodies from 26 providers.
DR DNASU; 58250; -.
DR Ensembl; ENSMUST00000040110; ENSMUSP00000045349; ENSMUSG00000034612.
DR GeneID; 58250; -.
DR KEGG; mmu:58250; -.
DR UCSC; uc007gke.1; mouse.
DR CTD; 50515; -.
DR MGI; MGI:1927166; Chst11.
DR VEuPathDB; HostDB:ENSMUSG00000034612; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000159167; -.
DR HOGENOM; CLU_043398_1_1_1; -.
DR InParanoid; Q9JME2; -.
DR OMA; KMDFLMF; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q9JME2; -.
DR TreeFam; TF325581; -.
DR BRENDA; 2.8.2.5; 3474.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR SABIO-RK; Q9JME2; -.
DR BioGRID-ORCS; 58250; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Chst11; mouse.
DR PRO; PR:Q9JME2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JME2; protein.
DR Bgee; ENSMUSG00000034612; Expressed in humerus cartilage element and 229 other tissues.
DR ExpressionAtlas; Q9JME2; baseline and differential.
DR Genevisible; Q9JME2; 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:0047756; F:chondroitin 4-sulfotransferase activity; ISO:MGI.
DR GO; GO:0001537; F:N-acetylgalactosamine 4-O-sulfotransferase activity; ISO:MGI.
DR GO; GO:0050659; F:N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase activity; IDA:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:MGI.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0033037; P:polysaccharide localization; IMP:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR InterPro; IPR018011; Carb_sulfotrans_8-10.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12137; PTHR12137; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..352
FT /note="Carbohydrate sulfotransferase 11"
FT /id="PRO_0000189665"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..352
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 124..130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 186..194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CONFLICT 255
FT /note="F -> L (in Ref. 2; CAB92141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 41632 MW; 6573EA72EB0C4FA1 CRC64;
MKPALLEVMR MNRICRMVLA TCFGSFILVI FYFQSMLHPV MRRNPFGVDI CCRKGSRSPL
QELYNPIQLE LSNTAILHQM RRDQVTDTCR ANSAMSRKRR VLTPNDLKHL VVDEDHELIY
CYVPKVACTN WKRLMMVLSG RGKYSDPMEI PANEAHVSAN LKTLNQYSIP EINHRLKSYM
KFLFVREPFE RLVSAYRNKF TQKYNTSFHK RYGTKIIRRQ RKNATQEALR KGDDVKFEEF
VAYLIDPHTQ REEPFNEHWQ TVYSLCHPCH IHYDLVGKYE TLEEDSNYVL QLAGVSGYLK
FPTYAKSTRT TDEMTTEFFQ NISAEHQTQL YEVYKLDFLM FNYSVPNYLK LD
