CHSTA_DANRE
ID CHSTA_DANRE Reviewed; 365 AA.
AC Q6AXM1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Carbohydrate sulfotransferase 10;
DE EC=2.8.2.-;
DE AltName: Full=HNK-1 sulfotransferase;
DE Short=HNK-1ST;
DE Short=HNK1ST;
GN Name=chst10; ORFNames=zgc:100964;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 3 of terminal
CC glucuronic acid of both protein- and lipid-linked oligosaccharides.
CC Participates in biosynthesis of HNK-1 carbohydrate structure, a
CC sulfated glucuronyl-lactosaminyl residue carried by many neural
CC recognition molecules.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079482; AAH79482.1; -; mRNA.
DR RefSeq; NP_001003779.1; NM_001003779.1.
DR AlphaFoldDB; Q6AXM1; -.
DR STRING; 7955.ENSDARP00000047210; -.
DR PaxDb; Q6AXM1; -.
DR Ensembl; ENSDART00000047211; ENSDARP00000047210; ENSDARG00000031632.
DR GeneID; 445322; -.
DR KEGG; dre:445322; -.
DR CTD; 9486; -.
DR ZFIN; ZDB-GENE-040808-40; chst10.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000157128; -.
DR HOGENOM; CLU_043398_2_0_1; -.
DR InParanoid; Q6AXM1; -.
DR OMA; NVCREDT; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q6AXM1; -.
DR TreeFam; TF325581; -.
DR Reactome; R-DRE-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR PRO; PR:Q6AXM1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000031632; Expressed in pharyngeal gill and 35 other tissues.
DR ExpressionAtlas; Q6AXM1; baseline and differential.
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:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
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..365
FT /note="Carbohydrate sulfotransferase 10"
FT /id="PRO_0000189662"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 132..138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 194..202
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 365 AA; 42512 MW; B0AB8AEE181D8CA1 CRC64;
MRRHWLLVGA CGWVLLILMF VSKFINFSFR IPGDYAGRSE IFVWTLSSVT TKLPSVVWPE
KGASQPYILS SVSPSVVEPI DWHLVNEKRL EQLSTVCSNS SIWNLTHTTV RKFVLDRIFV
CDKHKILFCQ TPKVGNTQWK KVLIVLNGKF SKVEAIPENL VHDHERNGLP RLSSMTDTEI
HQRLNSYFKF FIVRDPFERL ISAFKDKFVK NPRFEPWYKH DIAPAIVRKY RRSHHDDSES
VGLRFEDFVR YLGDKTGRQH LDRQFGDHII HWLTYAELCA PCDISYNVVG HHETLELDAP
YILKSAGIAG LVSYPSIPPG ITRYNRTKVE RYFSGISQRD IRRLYARYQG DFSLFDYPKP
AFLLN