ID   CHSTA_XENLA             Reviewed;         355 AA.
AC   Q6GNS1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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 (By similarity). {ECO:0000250}.
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; BC073432; AAH73432.1; -; mRNA.
DR   RefSeq; NP_001085854.1; NM_001092385.1.
DR   AlphaFoldDB; Q6GNS1; -.
DR   DNASU; 444281; -.
DR   GeneID; 444281; -.
DR   KEGG; xla:444281; -.
DR   CTD; 444281; -.
DR   Xenbase; XB-GENE-5856012; chst10.L.
DR   OMA; NVCREDT; -.
DR   OrthoDB; 1330889at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 444281; Expressed in blastula and 19 other tissues.
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; IEA:InterPro.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR018011; Carb_sulfotrans_8-10.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12137; PTHR12137; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..355
FT                   /note="Carbohydrate sulfotransferase 10"
FT                   /id="PRO_0000189663"
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..355
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   BINDING         126..132
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..196
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   355 AA;  41667 MW;  484D4E36E66DB4B6 CRC64;
     MHHRWLLLVA CFWVLFMLMV ASKLITLTMK DPEGYGNKQG PLTVLPETEK IAVAETTKLQ
     IESQPTTNSL KDESYTVLLH KERTELLRSV CSNGSLRNLS HTAISKFVLD RIFVSDKHRI
     LFCQTPKVGN TQWKKVLIVL NGAFSSIEEI PENVVHDHEK NGLPRLSSFS AQDVHERLNS
     YFKFFIVRDP FERLISAFKD KFVHNPRFEP WYKHDIAPAI IRKYRKDRRE SRGGLQFQDF
     VRYLGDPNHR FLDLQFGDHI IHWVTYVELC APCEIDYNVI GHHETLEDDA PYILREAGIE
     HLVSYPTIPP GITKYNKSKV ENYFSKVSKR DIRRLYTRFE RDFKLFGYKE PTFLF