ST2A1_MACFA
ID ST2A1_MACFA Reviewed; 285 AA.
AC P52842;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sulfotransferase 2A1;
DE Short=ST2A1;
DE EC=2.8.2.2 {ECO:0000269|PubMed:31100221};
DE AltName: Full=Bile salt sulfotransferase;
DE EC=2.8.2.14 {ECO:0000250|UniProtKB:Q06520};
DE AltName: Full=Hydroxysteroid sulfotransferase;
DE Short=HST;
GN Name=SULT2A1; Synonyms=STD;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Ogura K., Satsukawa M., Kato K., Okuda H., Watabe T.;
RT "Molecular cloning of monkey liver hydroxysteroid sulfotransferase.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=31100221; DOI=10.1016/j.bcp.2019.05.018;
RA Uno Y., Murayama N., Yamazaki H.;
RT "Molecular and functional characterization of cytosolic sulfotransferases
RT in cynomolgus macaque.";
RL Biochem. Pharmacol. 166:153-162(2019).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and
CC bile acids in the liver and adrenal glands (PubMed:31100221). Mediates
CC the sulfation of a wide range of steroids and sterols, including
CC pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well
CC many xenobiotics that contain alcohol and phenol functional groups.
CC Sulfonation increases the water solubility of most compounds, and
CC therefore their renal excretion, but it can also result in
CC bioactivation to form active metabolites. Plays an important role in
CC maintening steroid and lipid homeostasis. Plays a key role in bile acid
CC metabolism (By similarity). In addition, catalyzes the metabolic
CC activation of potent carcinogenic polycyclic arylmethanols (By
CC similarity). {ECO:0000250|UniProtKB:P15709,
CC ECO:0000250|UniProtKB:Q06520, ECO:0000269|PubMed:31100221}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-
CC bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2;
CC Evidence={ECO:0000269|PubMed:31100221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC Evidence={ECO:0000269|PubMed:31100221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217;
CC Evidence={ECO:0000305|PubMed:31100221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + taurolithocholate = adenosine
CC 3',5'-bisphosphate + H(+) + taurolithocholate 3-sulfate;
CC Xref=Rhea:RHEA:14013, ChEBI:CHEBI:15378, ChEBI:CHEBI:17179,
CC ChEBI:CHEBI:58301, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=2.8.2.14;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14014;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + lithocholate = adenosine 3',5'-
CC bisphosphate + H(+) + lithocholate sulfate; Xref=Rhea:RHEA:51064,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29744, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133940;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51065;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 24-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52344, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52345;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol 24-sulfate + 3'-phosphoadenylyl
CC sulfate = (24S)-hydroxycholesterol 3,24-disulfate + adenosine 3',5'-
CC bisphosphate + H(+); Xref=Rhea:RHEA:52352, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566,
CC ChEBI:CHEBI:136568; Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52353;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-
CC bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133000;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3alpha-hydroxy-5alpha-androstan-
CC 17-one = adenosine 3',5'-bisphosphate + androsterone 3alpha-sulfate +
CC H(+); Xref=Rhea:RHEA:60644, ChEBI:CHEBI:15378, ChEBI:CHEBI:16032,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133003;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60645;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:31100221}.
CC -!- TISSUE SPECIFICITY: Predominanly expressed in liver. Detected also in
CC adrenal gland and in jejunum. {ECO:0000269|PubMed:31100221}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; D85521; BAA12823.1; -; mRNA.
DR RefSeq; NP_001306532.1; NM_001319603.1.
DR AlphaFoldDB; P52842; -.
DR SMR; P52842; -.
DR STRING; 9541.XP_005589775.1; -.
DR GeneID; 102130325; -.
DR KEGG; mcf:102130325; -.
DR CTD; 6822; -.
DR eggNOG; KOG1584; Eukaryota.
DR BRENDA; 2.8.2.2; 1793.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISS:UniProtKB.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0047704; F:bile-salt sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0050294; F:steroid sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Bile acid catabolism; Cytoplasm; Lipid degradation; Lipid metabolism;
KW Phosphoprotein; Reference proteome; Steroid metabolism; Transferase.
FT CHAIN 1..285
FT /note="Sulfotransferase 2A1"
FT /id="PRO_0000085142"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 44..49
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 121
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 129
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 184
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 218..223
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 247..249
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
SQ SEQUENCE 285 AA; 33920 MW; B0DBF032D3AC0824 CRC64;
MSDDFLWFEG IAFPNMGFRS ETLRKVRDEF VIKDEDVIIL TYPKSGTNWL IEILCLIHSN
GDPKWIQSVP IWERSPWVET EMGYKLLSEE EGPRLFSSHL PIQLFPKSFF SSKAKVIYLM
RNPRDVFVSG YFFWNSVKFV KKPKSWQQYF EWFCQGNVIY GSWFDHIHGW MPMREKKNFL
LLSYEELKQD TRRTVEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN FSLLSVDFVE
EKAQLLRKGI SGDWKNHLTV AQAEAFDKLF QEKMTDLPRE LFPWE
