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Database: UniProt
Entry: ST2A2_MOUSE
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Original site: ST2A2_MOUSE 
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
//
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