ID   ST1A1_CANLF             Reviewed;         295 AA.
AC   Q29476;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Sulfotransferase 1A1;
DE            Short=ST1A1;
DE            EC=2.8.2.1 {ECO:0000269|PubMed:12054462};
DE   AltName: Full=Aryl sulfotransferase;
DE   AltName: Full=Phenol sulfotransferase;
DE   AltName: Full=Phenol-sulfating phenol sulfotransferase;
DE            Short=P-PST;
GN   Name=SULT1A1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; TISSUE=Liver;
RA   Satsukawa M., Ogura K., Nakamura T., Watabe T.;
RT   "Molecular cloning and sequencing of a dog liver cDNA (dPST-1) encoding a
RT   phenol sulfotransferase.";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND
RP   FUNCTION.
RC   TISSUE=Liver;
RX   PubMed=12054462; DOI=10.1016/s0003-9861(02)00021-8;
RA   Tsoi C., Morgenstern R., Swedmark S.;
RT   "Canine sulfotransferase SULT1A1: molecular cloning, expression, and
RT   characterization.";
RL   Arch. Biochem. Biophys. 401:125-133(2002).
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       (PubMed:12054462). Sulfonation increases the water solubility of most
CC       compounds, and therefore their renal excretion, but it can also result
CC       in 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       ECO:0000269|PubMed:12054462}.
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:0000269|PubMed:12054462};
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:0000269|PubMed:12054462};
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: Ubiquitously expressed in canine tissues with
CC       highest expression in male and female liver.
CC       {ECO:0000269|PubMed:12054462}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; D29807; BAA06190.1; -; mRNA.
DR   EMBL; AY069922; AAL57717.1; -; mRNA.
DR   RefSeq; NP_001003223.1; NM_001003223.1.
DR   RefSeq; XP_013969862.1; XM_014114387.1.
DR   AlphaFoldDB; Q29476; -.
DR   SMR; Q29476; -.
DR   STRING; 9615.ENSCAFP00000036703; -.
DR   PaxDb; 9612-ENSCAFP00000025221; -.
DR   Ensembl; ENSCAFT00000027121.3; ENSCAFP00000025221.1; ENSCAFG00000017122.5.
DR   Ensembl; ENSCAFT00030001324.1; ENSCAFP00030001165.1; ENSCAFG00030000768.1.
DR   Ensembl; ENSCAFT00040000610.1; ENSCAFP00040000504.1; ENSCAFG00040000352.1.
DR   Ensembl; ENSCAFT00805054942; ENSCAFP00805043160; ENSCAFG00805030218.
DR   Ensembl; ENSCAFT00845003885.1; ENSCAFP00845003096.1; ENSCAFG00845002193.1.
DR   GeneID; 403892; -.
DR   KEGG; cfa:403892; -.
DR   CTD; 6817; -.
DR   VEuPathDB; HostDB:ENSCAFG00845002193; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   GeneTree; ENSGT00940000162765; -.
DR   HOGENOM; CLU_027239_1_2_1; -.
DR   InParanoid; Q29476; -.
DR   OMA; CQRAPVF; -.
DR   OrthoDB; 3083090at2759; -.
DR   TreeFam; TF321745; -.
DR   BRENDA; 2.8.2.1; 1153.
DR   Reactome; R-CFA-156584; Cytosolic sulfonation of small molecules.
DR   Reactome; R-CFA-9753281; Paracetamol ADME.
DR   Proteomes; UP000002254; Chromosome 6.
DR   Proteomes; UP000694429; Chromosome 6.
DR   Proteomes; UP000694542; Chromosome 6.
DR   Proteomes; UP000805418; Chromosome 6.
DR   Bgee; ENSCAFG00000017122; Expressed in jejunum and 47 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; Lipid metabolism; Phosphoprotein;
KW   Reference proteome; Steroid metabolism; Transferase.
FT   CHAIN           1..295
FT                   /note="Sulfotransferase 1A1"
FT                   /id="PRO_0000085126"
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;  34115 MW;  C297A9211A5609B6 CRC64;
     MEDIPDTSRP PLKYVKGIPL IKYFAEALES LQDFQAQPDD LLISTYPKSG TTWVSEILDM
     IYQDGDVEKC RRAPVFIRVP FLEFKAPGIP TGLEVLKDTP APRLIKTHLP LALLPQTLLD
     QKVKVVYVAR NAKDVAVSYY HFYRMAKVHP DPDTWDSFLE KFMAGEVSYG SWYQHVQEWW
     ELSHTHPVLY LFYEDMKENP KREIQKILKF VGRSLPEETV DLIVQHTSFK EMKNNSMANY
     TTLSPDIMDH SISAFMRKGI SGDWKTTFTV AQNERFDADY AKKMEGCGLS FRTQL
//