CHSTA_RAT
ID CHSTA_RAT Reviewed; 356 AA.
AC O54702;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Carbohydrate sulfotransferase 10;
DE EC=2.8.2.- {ECO:0000269|PubMed:23723439};
DE AltName: Full=HNK-1 sulfotransferase {ECO:0000303|PubMed:23723439};
DE Short=HNK-1ST;
DE Short=HNK1ST;
DE Short=RaHNK-1ST;
DE Short=Sul-T;
GN Name=Chst10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX PubMed=9368071; DOI=10.1074/jbc.272.47.29942;
RA Bakker H., Friedmann I., Oka S., Kawasaki T., Nifant'ev N., Schachner M.,
RA Mantei N.;
RT "Expression cloning of a cDNA encoding a sulfotransferase involved in the
RT biosynthesis of the HNK-1 carbohydrate epitope.";
RL J. Biol. Chem. 272:29942-29946(1997).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11044619; DOI=10.1016/s0925-4773(00)00449-4;
RA Nagase T., Shimoda Y., Sanai Y., Nakamura S., Harii K., Osumi N.;
RT "Differential expression of two glucuronyltransferases synthesizing HNK-1
RT carbohydrate epitope in the sublineages of the rat myogenic progenitors.";
RL Mech. Dev. 98:145-149(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23723439; DOI=10.1093/glycob/cwt043;
RA Nakagawa N., Takematsu H., Oka S.;
RT "HNK-1 sulfotransferase-dependent sulfation regulating laminin-binding
RT glycans occurs in the post-phosphoryl moiety on alpha-dystroglycan.";
RL Glycobiology 23:1066-1074(2013).
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 (PubMed:9368071). Sulfates terminal glucuronyl residue of the laminin
CC globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and
CC prevents further polymerization by LARGE1 glycosyltransferase. Likely
CC defines the chain length of LG epitope, confering binding specificity
CC to extracellular matrix components (PubMed:23723439). Plays a role in
CC down-regulating the steroid hormones. Sulfates glucuronidated estrogens
CC and androgens with an impact in hormone cycle and fertility. Has a
CC preference for glucuronyl moiety at the 3-hydroxyl group of a sterol
CC ring rather than the 17-hydroxyl group, showing high catalytic
CC efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and
CC dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones (By
CC similarity). {ECO:0000250|UniProtKB:O43529,
CC ECO:0000269|PubMed:23723439, ECO:0000269|PubMed:9368071}.
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:0000269|PubMed:23723439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68305;
CC Evidence={ECO:0000305|PubMed:23723439};
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:0000269|PubMed:23723439}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In myogenic progenitors, it is ubiquitously
CC expressed. {ECO:0000269|PubMed:11044619}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; AF022729; AAB88123.1; -; mRNA.
DR RefSeq; NP_536322.1; NM_080397.1.
DR RefSeq; XP_006244794.1; XM_006244732.3.
DR RefSeq; XP_017451739.1; XM_017596250.1.
DR RefSeq; XP_017451740.1; XM_017596251.1.
DR AlphaFoldDB; O54702; -.
DR STRING; 10116.ENSRNOP00000017714; -.
DR GlyGen; O54702; 3 sites.
DR PaxDb; O54702; -.
DR GeneID; 140568; -.
DR KEGG; rno:140568; -.
DR UCSC; RGD:621216; rat.
DR CTD; 9486; -.
DR RGD; 621216; Chst10.
DR VEuPathDB; HostDB:ENSRNOG00000012815; -.
DR eggNOG; KOG4651; Eukaryota.
DR HOGENOM; CLU_043398_2_0_1; -.
DR InParanoid; O54702; -.
DR PhylomeDB; O54702; -.
DR Reactome; R-RNO-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00353; -.
DR PRO; PR:O54702; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000012815; Expressed in frontal cortex and 16 other tissues.
DR ExpressionAtlas; O54702; baseline and differential.
DR Genevisible; O54702; RN.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016232; F:HNK-1 sulfotransferase activity; IDA:RGD.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008209; P:androgen metabolic process; ISO:RGD.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007616; P:long-term memory; ISO:RGD.
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 1: Evidence at protein 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_0000189660"
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; 42027 MW; 48DDC990973B5B28 CRC64;
MHHQWLLLAA CFWVIFMFMV ASKFITLTFK DPDGYSAKQE FVFLTAMPEA EKLRGEKHFS
EVMKPTGKML SESHPDQPPV YLERLELIRN ACKEEALRNL SHTEVSKFVL DRIFVCDKHK
ILFCQTPKVG NTQWKKVLIV LNGAFSSIEE IPENVVHDHE KNGLPRLSSF SKIGIQKRLK
TYFKFFIVRD PFERLISAFK DKFVHNPRFE PWYRHEIAPG IIRKYRKNRT ETRGIQFEDF
VRYLGDPNRR WLDLQFGDHI IHWVTYVKLC APCEIKYSVI GHHETLEADA PYILKEAGID
HLVSYPTIPP GITMYNRTKV EQYFLGISKR DIRRLYARFE GDFKLFGYQK PDFLLN
