CHSTA_PONAB
ID CHSTA_PONAB Reviewed; 356 AA.
AC Q5RBZ6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Carbohydrate sulfotransferase 10;
DE EC=2.8.2.- {ECO:0000250|UniProtKB:O43529};
DE AltName: Full=HNK-1 sulfotransferase;
DE Short=HNK-1ST;
DE Short=HNK1ST;
GN Name=CHST10;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl
CC sulfate (PAPS) to position 3 of terminal glucuronic acid of both
CC protein- and lipid-linked oligosaccharides. Participates in
CC biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-
CC (1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl
CC residue carried by many neural recognition molecules, which is involved
CC in cell interactions during ontogenetic development and in synaptic
CC plasticity in the adult. May be indirectly involved in synapse
CC plasticity of the hippocampus, via its role in HNK-1 biosynthesis.
CC Sulfates terminal glucuronyl residue of the laminin globular (LG)-
CC domain binding epitope on DAG1/alpha-dystroglycan and prevents further
CC polymerization by LARGE1 glycosyltransferase. Likely defines the chain
CC length of LG epitope, confering binding specificity to extracellular
CC matrix components. Plays a role in down-regulating the steroid
CC hormones. Sulfates glucuronidated estrogens and androgens with an
CC impact in hormone cycle and fertility. Has a preference for glucuronyl
CC moiety at the 3-hydroxyl group of a sterol ring rather than the 17-
CC hydroxyl group, showing high catalytic efficiency for 17beta-estradiol
CC 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-
CC glucuronate) hormones. {ECO:0000250|UniProtKB:O43529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D-
CC Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-
CC P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-
CC Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-
CC beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-
CC GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein]
CC + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68304,
CC Rhea:RHEA-COMP:17486, Rhea:RHEA-COMP:17487, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:177355,
CC ChEBI:CHEBI:177363; Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68305;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) + 3'-phosphoadenylyl
CC sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D-glucuronate) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:136641, ChEBI:CHEBI:178093;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68697;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) 17-sulfate + 3'-
CC phosphoadenylyl sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D-
CC glucuronate) 17-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:68660, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178094, ChEBI:CHEBI:178095;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68661;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate) + 3'-
CC phosphoadenylyl sulfate = 17beta-estradiol 17-O-(3-sulfo-beta-D-
CC glucuronate) + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:68664, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:82961, ChEBI:CHEBI:178096;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68665;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha,17beta-estriol 3-O-(beta-D-glucuronate) + 3'-
CC phosphoadenylyl sulfate = 16alpha,17beta-estriol 3-O-(3-sulfo-beta-D-
CC glucuronate) + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:68668, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136649, ChEBI:CHEBI:178097;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68669;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha,17beta-estriol 16-O-(beta-D-glucuronate) + 3'-
CC phosphoadenylyl sulfate = 16alpha,17beta-estriol 16-O-(3-sulfo-beta-
CC D-glucuronate) + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:68672, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136650, ChEBI:CHEBI:178098;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68673;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha,17beta-estriol 17-O-(beta-D-glucuronate) + 3'-
CC phosphoadenylyl sulfate = 16alpha,17beta-estriol 17-O-(3-sulfo-beta-
CC D-glucuronate) + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:68700, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178099, ChEBI:CHEBI:178100;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68701;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + estrone 3-O-(beta-D-glucuronate)
CC = adenosine 3',5'-bisphosphate + estrone 3-O-(3-sulfo-beta-D-
CC glucuronate) + H(+); Xref=Rhea:RHEA:68676, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136634,
CC ChEBI:CHEBI:178101; Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68677;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3alpha,20alpha-dihydroxy-5beta-
CC pregnane 3-O-(beta-D-glucuronate) = 3alpha,20alpha-dihydroxy-5beta-
CC pregnane 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-
CC bisphosphate + H(+); Xref=Rhea:RHEA:68680, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178102,
CC ChEBI:CHEBI:178103; Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68681;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + testosterone 17-O-(beta-D-
CC glucuronate) = adenosine 3',5'-bisphosphate + H(+) + testosterone 17-
CC O-(3-sulfo-beta-D-glucuronate); Xref=Rhea:RHEA:68684,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:136639, ChEBI:CHEBI:178104;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68685;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3beta-androst-5-en-17-one 3-O-
CC (beta-D-glucuronate) = 3beta-androst-5-en-17-one 3-O-(3-sulfo-beta-D-
CC glucuronate) + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:68688, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178105, ChEBI:CHEBI:178106;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68689;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3alpha,17alpha-dihydroxy-5beta-
CC androstane-11-one-17beta-carboxylate 3-O-(beta-D-glucuronate) =
CC 3alpha,17alpha-dihydroxy-5beta-androstane-11-one-17beta-carboxylate
CC 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:68692, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178107, ChEBI:CHEBI:178108;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68693;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3alpha-hydroxyetiocholan-17-one
CC 3-O-(beta-D-glucuronate) = 3alpha-hydroxyetiocholan-17-one 3-O-(3-
CC sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:68704, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:178197, ChEBI:CHEBI:178198;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68705;
CC Evidence={ECO:0000250|UniProtKB:O43529};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:O43529}.
CC -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC {ECO:0000250|UniProtKB:O43529}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O54702}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; CR858486; CAH90714.1; -; mRNA.
DR RefSeq; NP_001125396.1; NM_001131924.1.
DR AlphaFoldDB; Q5RBZ6; -.
DR STRING; 9601.ENSPPYP00000013489; -.
DR Ensembl; ENSPPYT00000014038; ENSPPYP00000013489; ENSPPYG00000012098.
DR GeneID; 100172301; -.
DR KEGG; pon:100172301; -.
DR CTD; 9486; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000157128; -.
DR HOGENOM; CLU_043398_2_0_1; -.
DR InParanoid; Q5RBZ6; -.
DR OMA; NVCREDT; -.
DR OrthoDB; 1330889at2759; -.
DR TreeFam; TF325581; -.
DR UniPathway; UPA00353; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:Ensembl.
DR GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
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; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Steroid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..356
FT /note="Carbohydrate sulfotransferase 10"
FT /id="PRO_0000189659"
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 127..133
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 189..197
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 228
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 356 AA; 42231 MW; A6E71D3CFC39BDBB CRC64;
MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDVYSAKQE FLFLTTMPEV RKLPEEKHIP
EELKPTGKEL PDSRLVQPLV YMERLELIRN VCRDDALKNL SHTPVSKFVL DRIFVCDKHK
ILFCQTPKVG NTQWKKVLIV LNGAFPSIEE IPENVVHDHE KNGLPRLSSF SDAEIQKRLK
TYFKFFIVRD PFERLISAFK DKFVHNPRFE PWYRHEIAPG IIRKYRRNRT ESRGIQFEDF
VRYLGDPNHR WLDLQFGDHI IHWVTYVELC APCEIMYSVI GHHETLEDDA PYILKEAGID
HLVSYPTIPP GITVYNRTKV EHYFLGISKR DIRRLYARFE GDFKLFGYQK PDFLLN
