ID   ST2A1_MOUSE             Reviewed;         285 AA.
AC   P52843;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Sulfotransferase 2A1;
DE            Short=ST2A1;
DE            EC=2.8.2.2 {ECO:0000269|PubMed:12639899};
DE   AltName: Full=Bile salt sulfotransferase 1;
DE            EC=2.8.2.14 {ECO:0000250|UniProtKB:Q06520};
DE   AltName: Full=Hydroxysteroid sulfotransferase;
DE            Short=ST;
GN   Name=Sult2a1; Synonyms=Sta1;
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=BALB/cJ; TISSUE=Liver;
RX   PubMed=8483851; DOI=10.1023/a:1018926825475;
RA   Kong A.-N.T., Tao D., Ma M., Yang L.;
RT   "Molecular cloning of the alcohol/hydroxysteroid form (mSTa1) of
RT   sulfotransferase from mouse liver.";
RL   Pharm. Res. 10:627-630(1993).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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   CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=12639899; DOI=10.1210/en.2002-221011;
RA   Shimizu C., Fuda H., Yanai H., Strott C.A.;
RT   "Conservation of the hydroxysteroid sulfotransferase SULT2B1 gene structure
RT   in the mouse: pre- and postnatal expression, kinetic analysis of isoforms,
RT   and comparison with prototypical SULT2A1.";
RL   Endocrinology 144:1186-1193(2003).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and
CC       bile acids in the liver and adrenal glands (PubMed:12639899). Mediates
CC       the sulfation of a wide range of steroids and sterols, including
CC       pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well
CC       many xenobiotics that contain alcohol and phenol functional groups.
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. Plays an important role in
CC       maintening steroid and lipid homeostasis. Plays a key role in bile acid
CC       metabolism (By similarity). In addition, catalyzes the metabolic
CC       activation of potent carcinogenic polycyclic arylmethanols (By
CC       similarity). {ECO:0000250|UniProtKB:P15709,
CC       ECO:0000250|UniProtKB:Q06520, ECO:0000269|PubMed:12639899}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-
CC         bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22553;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + taurolithocholate = adenosine
CC         3',5'-bisphosphate + H(+) + taurolithocholate 3-sulfate;
CC         Xref=Rhea:RHEA:14013, ChEBI:CHEBI:15378, ChEBI:CHEBI:17179,
CC         ChEBI:CHEBI:58301, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=2.8.2.14;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14014;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-
CC         bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:133000;
CC         Evidence={ECO:0000269|PubMed:12639899};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357;
CC         Evidence={ECO:0000305|PubMed:12639899};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC         = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC         H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC         ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC         Evidence={ECO:0000269|PubMed:12639899};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217;
CC         Evidence={ECO:0000305|PubMed:12639899};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + lithocholate = adenosine 3',5'-
CC         bisphosphate + H(+) + lithocholate sulfate; Xref=Rhea:RHEA:51064,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29744, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:133940;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51065;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC         hydroxycholesterol 24-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:52344, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52345;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC         hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(24S)-hydroxycholesterol 24-sulfate + 3'-phosphoadenylyl
CC         sulfate = (24S)-hydroxycholesterol 3,24-disulfate + adenosine 3',5'-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:52352, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566,
CC         ChEBI:CHEBI:136568; Evidence={ECO:0000250|UniProtKB:Q06520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52353;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + androsterone = adenosine 3',5'-
CC         bisphosphate + androsterone 3alpha-sulfate + H(+);
CC         Xref=Rhea:RHEA:60644, ChEBI:CHEBI:15378, ChEBI:CHEBI:16032,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133003;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60645;
CC         Evidence={ECO:0000250|UniProtKB:Q06520};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06520}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06520}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver.
CC       {ECO:0000269|PubMed:12639899}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed until 19 dpc.
CC       {ECO:0000269|PubMed:12639899}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; L02335; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS52031.1; -.
DR   RefSeq; NP_001104766.1; NM_001111296.2.
DR   AlphaFoldDB; P52843; -.
DR   SMR; P52843; -.
DR   STRING; 10090.ENSMUSP00000104162; -.
DR   iPTMnet; P52843; -.
DR   PhosphoSitePlus; P52843; -.
DR   jPOST; P52843; -.
DR   MaxQB; P52843; -.
DR   PaxDb; 10090-ENSMUSP00000104162; -.
DR   ProteomicsDB; 258632; -.
DR   Ensembl; ENSMUST00000108522.5; ENSMUSP00000104162.4; ENSMUSG00000078798.5.
DR   GeneID; 20859; -.
DR   KEGG; mmu:20859; -.
DR   UCSC; uc009ffz.2; mouse.
DR   AGR; MGI:98430; -.
DR   CTD; 6822; -.
DR   MGI; MGI:98430; Sult2a1.
DR   VEuPathDB; HostDB:ENSMUSG00000078798; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   GeneTree; ENSGT00940000154432; -.
DR   HOGENOM; CLU_027239_1_0_1; -.
DR   InParanoid; P52843; -.
DR   OMA; IRERNIF; -.
DR   OrthoDB; 3083090at2759; -.
DR   PhylomeDB; P52843; -.
DR   TreeFam; TF321745; -.
DR   SABIO-RK; P52843; -.
DR   BioGRID-ORCS; 20859; 3 hits in 45 CRISPR screens.
DR   PRO; PR:P52843; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P52843; Protein.
DR   Bgee; ENSMUSG00000078798; Expressed in primary palate and 24 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISS:UniProtKB.
DR   GO; GO:0004027; F:alcohol sulfotransferase activity; IDA:UniProtKB.
DR   GO; GO:0047704; F:bile-salt sulfotransferase activity; ISS:UniProtKB.
DR   GO; GO:0050294; F:steroid sulfotransferase activity; IDA:UniProtKB.
DR   GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR   GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:MGI.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR   GO; GO:0006068; P:ethanol catabolic process; ISO:MGI.
DR   GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
DR   GO; GO:0051923; P:sulfation; IDA:MGI.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; ISO:MGI.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISO:MGI.
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:SF8; SULFOTRANSFERASE 2A1; 1.
DR   PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; P52843; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lipid metabolism; Reference proteome; Steroid metabolism;
KW   Transferase.
FT   CHAIN           1..285
FT                   /note="Sulfotransferase 2A1"
FT                   /id="PRO_0000085147"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         44
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         45
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         46
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         47
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         48
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         49
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         121
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         129
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         184
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         218
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         223
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         247
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         248
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
FT   BINDING         249
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:Q06520"
SQ   SEQUENCE   285 AA;  33213 MW;  FB71D587A2F4F4A4 CRC64;
     MMSDYNWFEG IPFPAISYQR EILEDIRNKF VVKEEDLLIL TYPKSGTNWL IEIVCLIQTK
     GDPKWIQTVP IWNRSPWIET DIGYSALINK EGPRLITSHL PIHLFSKSFF SSKAKAIYLV
     RNPRDILVSG YFFWGNTNLV KNPGSLGTYF EWFLKGNVLF GSWFEHVRGW LSMREWDNFL
     VLYYEDIKKD TKGTIKKICD FLGKNLGPDE LDLVLKYSSF QAMKENNMSN FSLIKEDQVT
     NGLKLMRKGT IGDWKNHFTV AQAEAFDKVF QEKMAGFPPG IFPWE
//