CHST3_CHICK
ID CHST3_CHICK Reviewed; 458 AA.
AC Q92179;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Carbohydrate sulfotransferase 3 {ECO:0000305|PubMed:7629189};
DE EC=2.8.2.17 {ECO:0000269|PubMed:7629189};
DE EC=2.8.2.21 {ECO:0000269|PubMed:7629189};
DE AltName: Full=Chondroitin 6-O-sulfotransferase 1;
DE Short=C6ST-1;
DE AltName: Full=Chondroitin 6-sulfotransferase {ECO:0000303|PubMed:7629189};
DE Short=C6ST {ECO:0000303|PubMed:7629189};
GN Name=CHST3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-44; 46-52 AND 186-192,
RP FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION.
RC STRAIN=White leghorn; TISSUE=Embryonic chondrocyte;
RX PubMed=7629189; DOI=10.1074/jbc.270.31.18575;
RA Fukuta M., Uchimura K., Nakashima K., Kato M., Kimata K., Shinomura T.,
RA Habuchi O.;
RT "Molecular cloning and expression of chick chondrocyte chondroitin 6-
RT sulfotransferase.";
RL J. Biol. Chem. 270:18575-18580(1995).
RN [2]
RP FUNCTION.
RX PubMed=9147050; DOI=10.1093/glycob/7.3.405;
RA Habuchi O., Suzuki Y., Fukuta M.;
RT "Sulfation of sialyl lactosamine oligosaccharides by chondroitin 6-
RT sulfotransferase.";
RL Glycobiology 7:405-412(1997).
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 (PubMed:7629189). Chondroitin sulfate constitutes the predominant
CC proteoglycan present in cartilage and is distributed on the surfaces of
CC many cells and extracellular matrices (PubMed:7629189). Catalyzes with
CC a lower efficiency the sulfation of Gal residues of keratan sulfate,
CC another glycosaminoglycan (PubMed:7629189). Can also catalyze the
CC sulfation of the Gal residues in sialyl N-acetyllactosamine (sialyl
CC LacNAc) oligosaccharides (PubMed:9147050). {ECO:0000269|PubMed:7629189,
CC ECO:0000269|PubMed:9147050, ECO:0000303|PubMed:7629189}.
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:0000269|PubMed:7629189};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11109;
CC Evidence={ECO:0000305|PubMed:7629189};
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:0000269|PubMed:7629189};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7629189}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; D49915; BAA08655.1; -; mRNA.
DR PIR; A57397; A57397.
DR RefSeq; NP_990452.1; NM_205121.1.
DR AlphaFoldDB; Q92179; -.
DR STRING; 9031.ENSGALP00000039792; -.
DR PaxDb; Q92179; -.
DR GeneID; 396018; -.
DR KEGG; gga:396018; -.
DR CTD; 9469; -.
DR VEuPathDB; HostDB:geneid_396018; -.
DR eggNOG; ENOG502QWEX; Eukaryota.
DR InParanoid; Q92179; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q92179; -.
DR BRENDA; 2.8.2.17; 1306.
DR PRO; PR:Q92179; -.
DR Proteomes; UP000000539; 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: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:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
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; Direct protein sequencing; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..458
FT /note="Carbohydrate sulfotransferase 3"
FT /id="PRO_0000085191"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..458
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 121..127
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 281..289
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 458 AA; 52253 MW; C9A3B7D0A5086F0C CRC64;
MERRSALPQD FREVLHCLKM RSKYAVLLVF VVGLVIIEKE NNFISRVSDK LKQSPQVLPE
ANETEASPVQ AENGSLASLR QLDTAFSQLR TRLRNVTLQL AGELGIAAPE PRRHVLLMAT
TRTGSSFVGE FFNQQGNIFY LFEPLWHIER TVTFEPGGAN AVGSALVYRD VLQQLLLCDL
YILESFISPA PEEHLTAALF RRGSSHSLCE EPVCTPSLKK VFEKYHCKNR RCGPLNITLA
AEACRRKQHM ALKTVRIRQL EFLQPLAEDP RLDLRIIQLV RDPRAVLVSR MVAFSGKYES
WKKWAAEGEA PLQEDEVQRL RGNCESIRLS AELGLRQPRW LRGRYMLVRY EDVARAPLRK
ALEMYRFAGI HPTPQVEEWI RANTQAPQDS NGIYSTQKNS SEQFEKWRFS IPFKLAQVVQ
DACEPAMRLF GYKLASSAQE LTNRSLSLLE EGPPTRIT
