ID   ST1A1_BOVIN             Reviewed;         295 AA.
AC   P50227; Q3T0S9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 142.
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|PubMed:8890738};
DE   AltName: Full=Phenol-sulfating phenol sulfotransferase;
DE            Short=P-PST;
GN   Name=SULT1A1; Synonyms=STP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Tracheobronchial;
RX   PubMed=7575456; DOI=10.1042/bj3110209;
RA   Schauss S.J., Henry T., Palmatier R., Halvorson L., Dannenbring R.,
RA   Beckmann J.D.;
RT   "Characterization of bovine tracheobronchial phenol sulphotransferase cDNA
RT   and detection of mRNA regulation by cortisol.";
RL   Biochem. J. 311:209-217(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8890738; DOI=10.1016/0378-1119(96)00083-2;
RA   Henry T., Kliewer B., Palmatier R., Ulphani J.S., Beckmann J.D.;
RT   "Isolation and characterization of a bovine gene encoding phenol
RT   sulfotransferase.";
RL   Gene 174:221-224(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-57.
RA   Nonneman D.J., Shibuya H., Johnson G.S.;
RL   Submitted (DEC-1994) 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. Mediates also the metabolic activation of carcinogenic N-
CC       hydroxyarylamines leading to highly reactive intermediates capable of
CC       forming DNA adducts, potentially resulting in mutagenesis (By
CC       similarity). May play a role in gut microbiota-host metabolic
CC       interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-
CC       derived metabolite produced by gut bacteria. The product 4-EPS crosses
CC       the blood-brain barrier and may negatively regulate oligodendrocyte
CC       maturation and myelination, affecting the functional connectivity of
CC       different brain regions associated with the limbic system.
CC       {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   -!- TISSUE SPECIFICITY: Distal lung parenchyma.
CC       {ECO:0000269|PubMed:7575456}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U35253; AAA85510.1; -; mRNA.
DR   EMBL; U34753; AAC48677.1; -; Genomic_DNA.
DR   EMBL; BC102274; AAI02275.1; -; mRNA.
DR   EMBL; L33828; AAA56789.1; -; Genomic_DNA.
DR   PIR; JC5000; JC5000.
DR   RefSeq; NP_803487.1; NM_177521.2.
DR   RefSeq; XP_005224892.1; XM_005224835.3.
DR   RefSeq; XP_005224893.1; XM_005224836.3.
DR   RefSeq; XP_005224894.1; XM_005224837.3.
DR   RefSeq; XP_005224895.1; XM_005224838.3.
DR   RefSeq; XP_010817689.1; XM_010819387.2.
DR   RefSeq; XP_010817690.1; XM_010819388.2.
DR   RefSeq; XP_010817691.1; XM_010819389.2.
DR   AlphaFoldDB; P50227; -.
DR   SMR; P50227; -.
DR   STRING; 9913.ENSBTAP00000011388; -.
DR   PaxDb; 9913-ENSBTAP00000011388; -.
DR   PeptideAtlas; P50227; -.
DR   Ensembl; ENSBTAT00000011388.3; ENSBTAP00000011388.2; ENSBTAG00000008635.4.
DR   GeneID; 282485; -.
DR   KEGG; bta:282485; -.
DR   CTD; 6817; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008635; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   GeneTree; ENSGT00940000162765; -.
DR   HOGENOM; CLU_027239_1_2_1; -.
DR   InParanoid; P50227; -.
DR   OMA; CQRAPVF; -.
DR   OrthoDB; 3083090at2759; -.
DR   TreeFam; TF321745; -.
DR   BRENDA; 2.8.2.1; 908.
DR   Reactome; R-BTA-156584; Cytosolic sulfonation of small molecules.
DR   Reactome; R-BTA-9753281; Paracetamol ADME.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000008635; Expressed in omental fat pad and 103 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR11783:SF324; SULFOTRANSFERASE 1A3-RELATED; 1.
DR   PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   1: Evidence at protein level;
KW   Catecholamine metabolism; Cytoplasm; Direct protein sequencing;
KW   Lipid metabolism; Phosphoprotein; Reference proteome; Steroid metabolism;
KW   Transferase.
FT   CHAIN           1..295
FT                   /note="Sulfotransferase 1A1"
FT                   /id="PRO_0000085125"
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"
FT   CONFLICT        200
FT                   /note="P -> S (in Ref. 3; AAI02275)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285..291
FT                   /note="AGCKLRF -> RAATPL (in Ref. 1; AAA85510 and 2;
FT                   AAC48677)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   295 AA;  34184 MW;  8F5B7F1E1094D6C5 CRC64;
     MELIQDTSRP PAKYVKGIPL IKYFAEALGP LESFEAWPDD LLISTYPKSG TTWVSEILDL
     IYQEGDLEKC QRAPVFLRVP FLEFSAPGVP TGVELLKDTP APRLLKTHLP LALLPKTLLD
     QKVKVIYIAR NAKDVAVSYY HFYRMAKVHP DPGTWDSFLE KFMAGEVCYG SWYQHVQEWW
     ELSHTHPVLY LFYEDIKEDP KREIQKILEF IGRSLPEETV DHIVQRTSFK EMKKNPMTNY
     STIPTAVMDH SISAFMRKGI TGDWKSTFTV AQNELFEAHY AKKMAGCKLR FRWEL
//