ST1A1_MACFA
ID ST1A1_MACFA Reviewed; 295 AA.
AC P52846;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Sulfotransferase 1A1;
DE Short=ST1A1;
DE EC=2.8.2.1 {ECO:0000250|UniProtKB:P50225};
DE AltName: Full=Aryl sulfotransferase;
DE AltName: Full=Phenol sulfotransferase {ECO:0000303|Ref.1};
DE AltName: Full=Phenol-sulfating phenol sulfotransferase;
DE Short=P-PST;
GN Name=SULT1A1; Synonyms=STP;
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., Okuda H., Watabe T.;
RT "cDNA cloning and bacterial expression of monkey liver phenol
RT sulfotransferase.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide
CC variety of acceptor molecules bearing a hydroxyl or an amine groupe.
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. Displays broad substrate
CC specificity for small phenolic compounds. Plays an important role in
CC the sulfonation of endogenous molecules such as steroid hormones and
CC 3,3'-diiodothyronin (By similarity). Mediates the sulfate conjugation
CC of a variety of xenobiotics, including the drugs acetaminophen and
CC minoxidil (By similarity). Mediates also the metabolic activation of
CC carcinogenic N-hydroxyarylamines leading to highly reactive
CC intermediates capable of forming DNA adducts, potentially resulting in
CC mutagenesis (By similarity). May play a role in gut microbiota-host
CC metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary
CC tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS
CC crosses the blood-brain barrier and may negatively regulate
CC oligodendrocyte maturation and myelination, affecting the functional
CC connectivity of different brain regions associated with the limbic
CC system. {ECO:0000250|UniProtKB:P17988, ECO:0000250|UniProtKB:P50225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC Evidence={ECO:0000250|UniProtKB:P50225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000250|UniProtKB:P50225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-
CC estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582;
CC Evidence={ECO:0000250|UniProtKB:P50225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000250|UniProtKB:P50225};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl
CC sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133681;
CC Evidence={ECO:0000250|UniProtKB:P50225};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC Evidence={ECO:0000250|UniProtKB:P50225};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50225}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17988}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; D85514; BAA12822.1; -; mRNA.
DR PIR; G02924; G02924.
DR AlphaFoldDB; P52846; -.
DR SMR; P52846; -.
DR STRING; 9541.XP_005591694.1; -.
DR eggNOG; KOG1584; Eukaryota.
DR BRENDA; 2.8.2.1; 1793.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISS:UniProtKB.
DR GO; GO:0004062; F:aryl sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS: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 2: Evidence at transcript level;
KW Catecholamine metabolism; Cytoplasm; Lipid metabolism; Phosphoprotein;
KW Reference proteome; Steroid metabolism; Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1A1"
FT /id="PRO_0000085129"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 227..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 255..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17988"
SQ SEQUENCE 295 AA; 34239 MW; BD51639D1570A841 CRC64;
MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFRARPDD LLISTYPKSG TTWVSQILDM
IYQGGDLEKC RRAPIFMRVP FLEFKVPGIP SGMETLKDTP APRLLKTHLP LALLPQTLLD
QKVKVVYVAR NAKDVAVSYY HFYHMAKVHP EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW
ELSHTHPVLY LFYEDMKENP KREIWKILEF VGRSLPEETV DLMVQHTSFK EMKKNPMANY
TTIPQELMDH SISPFMRKGM TGDWKTTFTV AQNEHFDVDY AEKMAGCSLS FRSEL
