ID   SUH2_RAT                Reviewed;         285 AA.
AC   P07631; O09038;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable alcohol sulfotransferase;
DE            EC=2.8.2.2;
DE   AltName: Full=Androgen-repressible liver protein;
DE   AltName: Full=Dehydroepiandrosterone sulfotransferase;
DE            Short=DST;
DE   AltName: Full=Hydroxysteroid sulfotransferase;
DE            Short=ST;
DE   AltName: Full=Senescence marker protein 2;
DE            Short=SMP-2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=3805009; DOI=10.1016/s0021-9258(19)75860-8;
RA   Chatterjee B., Majumdar D., Ozbilen O., Murty C.V.R., Roy A.K.;
RT   "Molecular cloning and characterization of cDNA for androgen-repressible
RT   rat liver protein, SMP-2.";
RL   J. Biol. Chem. 262:822-825(1987).
RN   [2]
RP   SEQUENCE REVISION TO 68-91; 192; 214 AND 238-241.
RA   Chatterjee B., Majumdar D., Ozbilen O., Murty C.V.R., Roy A.K.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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 + 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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: There is a marked sex difference (female >> male)
CC       in the cytosolic level of this protein. Not age-specific.
CC   -!- INDUCTION: Induced by estrogens and suppressed by androgens (By
CC       similarity). The expression is under the influence of pituitary growth
CC       hormone and thyroid hormone. Synthesis influenced by aging.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; J02643; AAB57741.1; -; mRNA.
DR   PIR; A26136; A26136.
DR   AlphaFoldDB; P07631; -.
DR   SMR; P07631; -.
DR   PRIDE; P07631; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004027; F:alcohol sulfotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0051923; P:sulfation; IBA:GO_Central.
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="Probable alcohol sulfotransferase"
FT                   /id="PRO_0000085145"
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"
SQ   SEQUENCE   285 AA;  33339 MW;  78AC4D2F1E811C0B CRC64;
     MMSDYNWFEG IPFPAISYQR EILEDIRNKF VVKEEDLLIL TYPKSGTNWL NEIVCLIQTK
     GDPKWIQTVP IWDRSPWIET EIGYPAIINK EGPRLITSHL PIHLFSKSFF SSKAKAIYLM
     RNPRDILVSG YFFWGNTNLV KNPGSLGTYF EWFLQGNVLF GSWFEHVRGW LSMREWDNFL
     VLYYEDMKKD TKGTIKKICD FLGKNLGPDE LDLVLKYSSF QAMKENNMSN YSLIKEDRVT
     NGLKLMRKGT TGDWKNHFTV AQAEAFDKVF QEKMAGFPPG MFPWE