CHSTB_DANRE
ID CHSTB_DANRE Reviewed; 352 AA.
AC Q7T3S3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Carbohydrate sulfotransferase 11;
DE EC=2.8.2.5;
DE AltName: Full=Chondroitin 4-O-sulfotransferase 1;
DE AltName: Full=Chondroitin 4-sulfotransferase 1;
DE Short=C4ST-1;
DE Short=C4ST1;
DE Short=zC4ST-1;
GN Name=chst11;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kobayashi N., Mizumoto S., Mikami T., Kitagawa H., Sugahara K.;
RT "Molecular cloning and expression of zebrafish chondroitin 4-
RT sulfotransferase.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the N-
CC acetylgalactosamine (GalNAc) residue of chondroitin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+);
CC Xref=Rhea:RHEA:16101, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9829,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:58422; EC=2.8.2.5;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AB097217; BAC76973.1; -; mRNA.
DR AlphaFoldDB; Q7T3S3; -.
DR STRING; 7955.ENSDARP00000042962; -.
DR PaxDb; Q7T3S3; -.
DR ZFIN; ZDB-GENE-040315-1; chst11.
DR eggNOG; KOG4651; Eukaryota.
DR InParanoid; Q7T3S3; -.
DR PhylomeDB; Q7T3S3; -.
DR BRENDA; 2.8.2.5; 928.
DR Reactome; R-DRE-2022870; Chondroitin sulfate biosynthesis.
DR PRO; PR:Q7T3S3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0047756; F:chondroitin 4-sulfotransferase activity; IDA:ZFIN.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR GO; GO:0007517; P:muscle organ development; IMP:ZFIN.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
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..352
FT /note="Carbohydrate sulfotransferase 11"
FT /id="PRO_0000189667"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..352
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 124..130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 186..194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 40998 MW; 2FD1C9CA6F27088D CRC64;
MKQTILDLMR MSRICRMVLA TCLGSFILVI FYFQSMFQPV MRRNPFAAEG CCRKGSRNAL
QELYNPTQAE FSAAAVLHQA RRDQVAETCR AHSASSRKRR VLTPSDLKHL VVDEDHELIY
CYVPKVACTN WKRVMMVLSG RGKYSNPMEI PSNEAHVPSN LKTLNQYSIP DINHRLKNYL
KFLFVREPFE RLVSAYRNKF TLRYNTSFHK RYGTKIVRRY RKNATTEALQ SGADVKFQEF
AEYLVDPGTQ REAPLNEHWQ TVYSLCHPCH IHYDLVGKYE TLEDDANYVL KLVGEGDSLR
FPSFAKSTRT TDQMAAMFFG NISSQQQSQL YQLYKLDYLM FNYSIPSYLK LQ
