CHST9_MOUSE
ID CHST9_MOUSE Reviewed; 413 AA.
AC Q76EC5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Carbohydrate sulfotransferase 9;
DE EC=2.8.2.-;
DE AltName: Full=GalNAc-4-O-sulfotransferase 2;
DE Short=GalNAc-4-ST2;
DE Short=GalNAc4ST-2;
DE AltName: Full=N-acetylgalactosamine-4-O-sulfotransferase 2;
GN Name=Chst9;
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=12944377; DOI=10.1093/jb/mvg118;
RA Okuda T., Sawada T., Nakano H., Matsubara K., Matsuda Y., Fukuta M.,
RA Habuchi O.;
RT "Mouse N-acetylgalactosamine 4-sulfotransferases-1 and -2. Molecular
RT cloning, expression, chromosomal mapping and detection of their activity
RT with GalNAcbeta1-4GlcNAcbeta1-octyl.";
RL J. Biochem. 134:111-120(2003).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of non-
CC reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and
CC O-glycans. Participates in biosynthesis of glycoprotein hormones
CC lutropin and thyrotropin, by mediating sulfation of their carbohydrate
CC structures. Has a higher activity toward carbonic anhydrase VI than
CC toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and pituitary gland.
CC {ECO:0000269|PubMed:12944377}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AB106879; BAC87754.1; -; mRNA.
DR CCDS; CCDS29074.1; -.
DR RefSeq; NP_951010.1; NM_199055.2.
DR AlphaFoldDB; Q76EC5; -.
DR STRING; 10090.ENSMUSP00000049975; -.
DR GlyGen; Q76EC5; 5 sites.
DR PhosphoSitePlus; Q76EC5; -.
DR PaxDb; Q76EC5; -.
DR PRIDE; Q76EC5; -.
DR ProteomicsDB; 283839; -.
DR Antibodypedia; 2549; 144 antibodies from 23 providers.
DR DNASU; 71367; -.
DR Ensembl; ENSMUST00000053017; ENSMUSP00000049975; ENSMUSG00000047161.
DR GeneID; 71367; -.
DR KEGG; mmu:71367; -.
DR UCSC; uc008edv.1; mouse.
DR CTD; 83539; -.
DR MGI; MGI:1918617; Chst9.
DR VEuPathDB; HostDB:ENSMUSG00000047161; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000160563; -.
DR HOGENOM; CLU_043398_5_1_1; -.
DR InParanoid; Q76EC5; -.
DR OMA; NWPLDIR; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q76EC5; -.
DR TreeFam; TF325581; -.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 71367; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Chst9; mouse.
DR PRO; PR:Q76EC5; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q76EC5; protein.
DR Bgee; ENSMUSG00000047161; Expressed in conjunctival fornix and 49 other tissues.
DR ExpressionAtlas; Q76EC5; baseline and differential.
DR Genevisible; Q76EC5; 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:0001537; F:N-acetylgalactosamine 4-O-sulfotransferase activity; IDA:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO: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..413
FT /note="Carbohydrate sulfotransferase 9"
FT /id="PRO_0000189656"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..413
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 190..196
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 250..258
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 413 AA; 48004 MW; E05D123E430DD7F4 CRC64;
MKAKQVFFSV LLFGTAGLLL FMYLQAWIEE HHTGKIEKKR DQKGVSVTTG KIQKQITNQN
SEVHMPEDLK KKGGDLLNLG SPTRVLRKIS HSQRENGAYR STEAHQGAKI EVFQKPIQMD
WPLVTQPLNK SLVQGNKWKK ADATQEKRRS FLHEFCKKYG RVNDPKFNLF HIVSRIYVED
KHKILYCEVP KAGCSNWKRI LMVLNGLASS AYNISHDTVH YGKHLKTLDS FDLKGVHMRL
NTYTKAVFVR DPMERLVSAF RDKFEHPNSY YHPVFGKAII KKYRPNASAE ALNNGSGVKF
KEFAYYLLDA HRPVGMDIHW ERVSKLCYPC LINYDFVGKF ETLGEDANYF LQLIGAPKEL
TFPNFKDRHS SDERTNAHVV RQYLKDLSTA ERQLIYDFYH LDYLMFNYTT PHL
