ST1A1_MOUSE
ID ST1A1_MOUSE Reviewed; 291 AA.
AC P52840;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
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;
DE AltName: Full=Phenol/aryl sulfotransferase {ECO:0000303|PubMed:8424956};
DE Short=mSTp1 {ECO:0000303|PubMed:8424956};
DE AltName: Full=ST1A4;
DE AltName: Full=Sulfokinase;
GN Name=Sult1a1; Synonyms=St1a1, Stp, Stp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=8424956; DOI=10.1016/0167-4781(93)90073-m;
RA Kong A.-N.T., Ma M., Tao D., Yang L.;
RT "Molecular cloning of cDNA encoding the phenol/aryl form of
RT sulfotransferase (mSTp1) from mouse liver.";
RL Biochim. Biophys. Acta 1171:315-318(1993).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=35165440; DOI=10.1038/s41586-022-04396-8;
RA Needham B.D., Funabashi M., Adame M.D., Wang Z., Boktor J.C., Haney J.,
RA Wu W.L., Rabut C., Ladinsky M.S., Hwang S.J., Guo Y., Zhu Q.,
RA Griffiths J.A., Knight R., Bjorkman P.J., Shapiro M.G., Geschwind D.H.,
RA Holschneider D.P., Fischbach M.A., Mazmanian S.K.;
RT "A gut-derived metabolite alters brain activity and anxiety behaviour in
RT mice.";
RL Nature 602:647-653(2022).
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 -!- TISSUE SPECIFICITY: Expressed in brain, colon, liver, and small
CC intestine of mice colonized with B. ovatus and L. plantarum.
CC {ECO:0000269|PubMed:35165440}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; L02331; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P52840; -.
DR SMR; P52840; -.
DR STRING; 10090.ENSMUSP00000101981; -.
DR iPTMnet; P52840; -.
DR PhosphoSitePlus; P52840; -.
DR SwissPalm; P52840; -.
DR REPRODUCTION-2DPAGE; P52840; -.
DR jPOST; P52840; -.
DR MaxQB; P52840; -.
DR PaxDb; P52840; -.
DR PeptideAtlas; P52840; -.
DR PRIDE; P52840; -.
DR ProteomicsDB; 257081; -.
DR MGI; MGI:102896; Sult1a1.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; P52840; -.
DR PhylomeDB; P52840; -.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR ChiTaRS; Sult1a1; mouse.
DR PRO; PR:P52840; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P52840; protein.
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:0047685; F:amine sulfotransferase activity; ISO:MGI.
DR GO; GO:0004062; F:aryl sulfotransferase activity; ISO:MGI.
DR GO; GO:0047894; F:flavonol 3-sulfotransferase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IDA:MGI.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISO:MGI.
DR GO; GO:0043199; F:sulfate binding; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0018960; P:4-nitrophenol metabolic process; ISO:MGI.
DR GO; GO:0006584; P:catecholamine metabolic process; ISO:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
DR GO; GO:0051923; P:sulfation; IDA:MGI.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:MGI.
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 Cytoplasm; Lipid metabolism; Phosphoprotein; Reference proteome;
KW Steroid metabolism; Transferase.
FT CHAIN 1..291
FT /note="Sulfotransferase 1A1"
FT /id="PRO_0000085130"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 44..49
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 126
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 134
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 189
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 223..228
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT BINDING 251..255
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P50225"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17988"
SQ SEQUENCE 291 AA; 33974 MW; ADC07187DFA51D96 CRC64;
MEPLRKPLVP VKGIPLIKYF AETMEQLQNF TAWPDDVLIS TYPKSGTNWM SEIMDMIYQG
GKLDKCGRAP VYARIPFLEF SCPGVPPGLE TLKETPAPRI IKTHLPLSLL PQSLLDQKIK
VIYVARNAKD VVVSYYNFYK MAKLHPDPGT WESFLENFMD GKVSYGSWYQ HVKEWWELRR
THPVLYLFYE DMKENPKREI KKILEFLGRS LPEETVDLIV HHTSFKKMKE NPMANYTTIP
TEVMDHTIYP FMRKGTIGDW KNTFTVAQSE HFDAHYAKLM TGCDFTFRCQ I
