ST1A1_BOVIN
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 03-AUG-2022, entry version 134.
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}.
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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; P50227; -.
DR PeptideAtlas; P50227; -.
DR PRIDE; P50227; -.
DR Ensembl; ENSBTAT00000011388; ENSBTAP00000011388; ENSBTAG00000008635.
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; IIYLCRE; -.
DR OrthoDB; 780670at2759; -.
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 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:0008146; F: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; -; 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 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
