ID   CHST3_TETCF             Reviewed;         441 AA.
AC   O93403;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   22-FEB-2023, entry version 67.
DE   RecName: Full=Carbohydrate sulfotransferase 3 {ECO:0000305|PubMed:9736640};
DE            EC=2.8.2.17 {ECO:0000305|PubMed:9736640};
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=Nervous system involved sulfotransferase {ECO:0000303|PubMed:9736640};
GN   Name=CHST3; Synonyms=NSIST {ECO:0000303|PubMed:9736640};
OS   Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX   NCBI_TaxID=7787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9736640; DOI=10.1523/jneurosci.18-18-07167.1998;
RA   Nastuk M.A., Davis S., Yancopoulos G.D., Fallon J.R.;
RT   "Expression cloning and characterization of NSIST, a novel sulfotransferase
RT   expressed by a subset of neurons and postsynaptic targets.";
RL   J. Neurosci. 18:7167-7177(1998).
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 chondroitin
CC       (Probable). Chondroitin sulfate constitutes the predominant
CC       proteoglycan present in cartilage and is distributed on the surfaces of
CC       many cells and extracellular matrices (PubMed:9736640). Catalyzes with
CC       a lower efficiency the sulfation of Gal residues of keratan sulfate,
CC       another glycosaminoglycan (By similarity). Can also catalyze the
CC       sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl
CC       LacNAc) oligosaccharides (By similarity).
CC       {ECO:0000250|UniProtKB:Q7LGC8, ECO:0000250|UniProtKB:Q92179,
CC       ECO:0000303|PubMed:9736640, ECO:0000305|PubMed:9736640}.
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:0000305|PubMed:9736640};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11109;
CC         Evidence={ECO:0000305|PubMed:9736640};
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   -!- TISSUE SPECIFICITY: In electric organ, it is moderately expressed in
CC       spinal cord and electric lobe and undetectable in non-neural tissues.
CC       Expressed in a punctate distribution in the innervated portion of
CC       electrocytes. In the CNS, it is localized within the somas of motor
CC       neurons and neurons of the electromotor nucleus.
CC       {ECO:0000269|PubMed:9736640}.
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; AF079875; AAC28491.1; -; mRNA.
DR   AlphaFoldDB; O93403; -.
DR   GlyCosmos; O93403; 4 sites, No reported glycans.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008459; F:chondroitin 6-sulfotransferase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISS:UniProtKB.
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:SF60; CARBOHYDRATE SULFOTRANSFERASE 3; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Membrane;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..441
FT                   /note="Carbohydrate sulfotransferase 3"
FT                   /id="PRO_0000085192"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..21
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..441
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   BINDING         106..112
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..274
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   441 AA;  50393 MW;  993B8B858743BA53 CRC64;
     MKMRSKYAII LFFVVALVII EKERNIISRV SDKFTLKFPH AESVAPNNTI SARSLTKNNS
     LLANSVAAVW KLLKARRSYS SLQSAASSDV RKVLKGRKHL LLMATTRTGS SFVGEFFNQN
     NDIFYLFEPL WHVEKTVTFE PGGMNAVASS IIYRDVVQQL MLCDLYTLEN FLFPMADRHL
     TGILFRRGSS KSLCEGEVCT PPKKGGTEKF PCRLRDCGLL NLTLATQACL QKQHVAIKTV
     PLRQLEFLRP LVEDFRINLK IIQLVRDPRA VLASRMVAFP SKYNAWKKWA NEGRVPDDDE
     VGKIRGNCEN LRATAQLGIS QPPWLKDRFL LMRYEDIALE PVKRAQEMYR FSGIPMTPEV
     KKWIYENTQV SKASNNIYST HKISSEQFEK WRLGLPFKIA RVVQQVCEPA MKLFGYKLVK
     DAATLANRSA SLLENRNFWI T
//