ST2A1_MOUSE
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 03-AUG-2022, entry version 152.
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 + 3alpha-hydroxy-5alpha-androstan-
CC 17-one = adenosine 3',5'-bisphosphate + androsterone 3alpha-sulfate +
CC H(+); 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}.
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; 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; P52843; -.
DR PRIDE; P52843; -.
DR ProteomicsDB; 258632; -.
DR Ensembl; ENSMUST00000108522; ENSMUSP00000104162; ENSMUSG00000078798.
DR GeneID; 20859; -.
DR KEGG; mmu:20859; -.
DR UCSC; uc009ffz.2; mouse.
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; HAMKENK; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P52843; -.
DR TreeFam; TF321745; -.
DR SABIO-RK; P52843; -.
DR BioGRID-ORCS; 20859; 3 hits in 40 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 tissues.
DR Genevisible; P52843; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0016740; F:transferase activity; ISO:MGI.
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; -; 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; 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..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..223
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 247..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
