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 03-AUG-2022, entry version 116.
DE RecName: Full=Bile salt sulfotransferase 2;
DE EC=2.8.2.14;
DE AltName: Full=Hydroxysteroid sulfotransferase;
DE Short=ST;
DE AltName: Full=Sulfotransferase 2A2;
DE Short=ST2A2;
GN Name=Sult2a2; Synonyms=Sta2, 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].
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 sulfonation of hydroxysteroids
CC and xenobiotics. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + glycolithocholate = adenosine
CC 3',5'-bisphosphate + H(+) + sulfoglycolithocholate;
CC Xref=Rhea:RHEA:10908, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:60007, ChEBI:CHEBI:60008; EC=2.8.2.14;
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
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 PRIDE; P50236; -.
DR ProteomicsDB; 258633; -.
DR MGI; MGI:107550; Sult2a2.
DR InParanoid; P50236; -.
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; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipid metabolism; Reference proteome; Steroid metabolism;
KW Transferase.
FT CHAIN 1..285
FT /note="Bile salt sulfotransferase 2"
FT /id="PRO_0000085148"
FT ACT_SITE 99
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"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 218..223
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 247..249
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
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
