ID ST2A2_MOUSE Reviewed; 285 AA.
AC P50236; Q05A88;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 24-JAN-2024, entry version 121.
DE RecName: Full=Sulfotransferase 2A2 {ECO:0000305|PubMed:8033251};
DE Short=ST2A2 {ECO:0000303|PubMed:8033251};
DE EC=2.8.2.2 {ECO:0000269|PubMed:8033251};
DE AltName: Full=Hydroxysteroid sulfotransferase {ECO:0000303|PubMed:8033251};
DE Short=ST {ECO:0000303|PubMed:8033251};
GN Name=Sult2a2 {ECO:0000312|MGI:MGI:107550};
GN Synonyms=Sta2 {ECO:0000312|MGI:MGI:107550}, Sth2;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8033251; DOI=10.1016/0009-2797(94)90061-2;
RA Kong A.-N.T., Fei P.;
RT "Molecular cloning of three sulfotransferase cDNAs from mouse liver.";
RL Chem. Biol. Interact. 92:161-168(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a
CC potential wide variety of acceptor molecules bearing a hydroxyl group.
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. {ECO:0000269|PubMed:8033251}.
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:0000269|PubMed:8033251};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22553;
CC Evidence={ECO:0000305|PubMed:8033251};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17988}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; L27121; AAA40145.1; -; mRNA.
DR EMBL; BC125365; AAI25366.1; -; mRNA.
DR EMBL; BC125367; AAI25368.1; -; mRNA.
DR PIR; T10086; T10086.
DR AlphaFoldDB; P50236; -.
DR SMR; P50236; -.
DR iPTMnet; P50236; -.
DR PhosphoSitePlus; P50236; -.
DR jPOST; P50236; -.
DR MaxQB; P50236; -.
DR ProteomicsDB; 258633; -.
DR AGR; MGI:107550; -.
DR MGI; MGI:107550; Sult2a2.
DR InParanoid; P50236; -.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR PRO; PR:P50236; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P50236; Protein.
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; ISO:MGI.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; ISO:MGI.
DR GO; GO:0047704; F:bile-salt sulfotransferase activity; ISO:MGI.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:MGI.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:MGI.
DR GO; GO:0008202; P:steroid metabolic process; ISO:MGI.
DR GO; GO:0051923; P:sulfation; ISO: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.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid metabolism; Reference proteome; Steroid metabolism;
KW Transferase.
FT CHAIN 1..285
FT /note="Sulfotransferase 2A2"
FT /id="PRO_0000085148"
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"
FT CONFLICT 85
FT /note="S -> P (in Ref. 2; AAI25366/AAI25368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 33329 MW; C49D138FE2B04308 CRC64;
MMSDYNWFEG IPFPAISYQR EILEDIRNKF VVKEEDLLIL TYPKSGTNWL NEIVCLIQTK
GDPKWIQTVP IWDRSPWIET EIGYSAIINK EGPRLITSHL PIHLFSKSFF SSKAKAIYLM
RNPRDILVSG YFFWGNTNLV KNPGSLGTYF EWFLQGNVLF GSWFEHVRGW LSMREWDNFL
VLYYEDMKKD TKGTIKKICD FLGKNLGPDE LDLVLKYSSF QAMKENNMSN YSLIKEDRVT
NGLKLMRKGT TGDWKNHFTV AQAEAFDKVF QEKMAGFPPG MFPWE
//