ST1A1_CANLF
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 03-AUG-2022, entry version 119.
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}.
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; 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; 9612.ENSCAFP00000025221; -.
DR PaxDb; Q29476; -.
DR PRIDE; Q29476; -.
DR Ensembl; ENSCAFT00030001324; ENSCAFP00030001165; ENSCAFG00030000768.
DR Ensembl; ENSCAFT00040000610; ENSCAFP00040000504; ENSCAFG00040000352.
DR Ensembl; ENSCAFT00845003885; ENSCAFP00845003096; ENSCAFG00845002193.
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; IIYLCRE; -.
DR OrthoDB; 780670at2759; -.
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 Bgee; ENSCAFG00000017122; Expressed in jejunum and 47 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; 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
