CHST3_RAT
ID CHST3_RAT Reviewed; 474 AA.
AC Q9QZL2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Carbohydrate sulfotransferase 3 {ECO:0000305};
DE EC=2.8.2.17 {ECO:0000250|UniProtKB:Q7LGC8};
DE EC=2.8.2.21 {ECO:0000250|UniProtKB:Q7LGC8};
DE AltName: Full=Chondroitin 6-O-sulfotransferase 1;
DE Short=C6ST-1;
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0;
DE Short=GST-0;
GN Name=Chst3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Li X., Kwok C.-F., Shum K.-Y.;
RT "Chondroitin 6-sulfotransferase of rat sciatic nerve.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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
CC chondroitin. Chondroitin sulfate constitutes the predominant
CC proteoglycan present in cartilage and is distributed on the surfaces of
CC many cells and extracellular matrices. Catalyzes with a lower
CC efficiency the sulfation of Gal residues of keratan sulfate, another
CC glycosaminoglycan (By similarity). Can also catalyze the sulfation of
CC the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc)
CC oligosaccharides (By similarity). May play a role in the maintenance of
CC naive T-lymphocytes in the spleen (By similarity).
CC {ECO:0000250|UniProtKB:O88199, ECO:0000250|UniProtKB:Q7LGC8,
CC ECO:0000250|UniProtKB:Q92179}.
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:0000250|UniProtKB:Q7LGC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11109;
CC Evidence={ECO:0000250|UniProtKB:Q7LGC8};
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:0000250|UniProtKB:Q7LGC8};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92179}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; AF178689; AAD54386.2; -; mRNA.
DR RefSeq; NP_445860.1; NM_053408.1.
DR AlphaFoldDB; Q9QZL2; -.
DR STRING; 10116.ENSRNOP00000000697; -.
DR GlyGen; Q9QZL2; 6 sites.
DR iPTMnet; Q9QZL2; -.
DR PhosphoSitePlus; Q9QZL2; -.
DR PaxDb; Q9QZL2; -.
DR PRIDE; Q9QZL2; -.
DR GeneID; 84468; -.
DR KEGG; rno:84468; -.
DR UCSC; RGD:620355; rat.
DR CTD; 9469; -.
DR RGD; 620355; Chst3.
DR eggNOG; ENOG502QWEX; Eukaryota.
DR InParanoid; Q9QZL2; -.
DR PhylomeDB; Q9QZL2; -.
DR BRENDA; 2.8.2.17; 5301.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR PRO; PR:Q9QZL2; -.
DR Proteomes; UP000002494; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050698; F:proteoglycan sulfotransferase activity; IDA:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:RGD.
DR GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
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 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..474
FT /note="Carbohydrate sulfotransferase 3"
FT /id="PRO_0000085190"
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..474
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 137..143
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 297..305
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 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 54018 MW; 83EC94C3894CE77E CRC64;
MEKGLALPQD CRDLVHNLKI RGRYVLFLAF VVIVFIFIEK ENKIISRVSD KLKQIPQFVA
DANSTDPALL LSENASLLSL SELDSTFSHL RSRLHNLSLQ LGIAPAMEAQ GQEAVAEKPS
QQAGAGTRRH VLLMATTRTG SSFVGEFFNQ QGNIFYLFEP LWHIERTVFF QQGGASAAGS
ALVYRDVLKQ LLLCDLYVLE PFISPPPEDH LTQFLFRRGS SRSLCEDPVC TPFVKKVFEK
YHCRNRHCGP LNVTLAAEAC RRKDHMALKV VRIRQLEFLQ PLAEDPRLDL RVIQLVRDPR
AVLASRMVAF AGKYESWKKW LSEGQDQLSE NEVQRLRGNC ENIRLSAELG LRQPAWLRGR
YMLVRYEDVA RRPLQKAREM YRSAGIPLTP QVEDWIQKNT QAARDSSDVY STQKNSSEQF
EKWRFSIPFK LAQVVQAVCG PAMHLFGHKL AKDTASLTNR SISLLEERGT FWVT
