CHST3_TETCF
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 03-AUG-2022, entry version 65.
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 GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 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
