ID   SUH3_RAT                Reviewed;         285 AA.
AC   P50235; Q04169;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Alcohol sulfotransferase;
DE            EC=2.8.2.2;
DE   AltName: Full=Hydroxysteroid sulfotransferase;
DE            Short=ST;
DE   AltName: Full=ST-60;
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; TISSUE=Liver;
RX   PubMed=8033273; DOI=10.1016/0009-2797(94)90056-6;
RA   Watabe T., Ogura K., Satsukawa M., Okuda H., Hiratsuka A.;
RT   "Molecular cloning and functions of rat liver hydroxysteroid
RT   sulfotransferases catalysing covalent binding of carcinogenic polycyclic
RT   arylmethanols to DNA.";
RL   Chem. Biol. Interact. 92:87-105(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 2-68.
RX   PubMed=2302387; DOI=10.1021/bi00454a031;
RA   Song C.S., Kim J.M., Roy A.K., Chatterjee B.;
RT   "Structure and regulation of the senescence marker protein 2 gene
RT   promoter.";
RL   Biochemistry 29:542-551(1990).
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   -!- INDUCTION: Induced by estrogens and suppressed by androgens. Expression
CC       is under the influence of pituitary growth hormone and thyroid hormone.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; D14989; BAA03634.1; -; mRNA.
DR   EMBL; M29302; AAA42152.1; -; Genomic_DNA.
DR   PIR; I65760; I65760.
DR   RefSeq; NP_001020302.1; NM_001025131.2.
DR   AlphaFoldDB; P50235; -.
DR   SMR; P50235; -.
DR   STRING; 10116.ENSRNOP00000045076; -.
DR   PRIDE; P50235; -.
DR   Ensembl; ENSRNOT00000110958; ENSRNOP00000082415; ENSRNOG00000062869.
DR   GeneID; 361510; -.
DR   KEGG; rno:361510; -.
DR   CTD; 100043194; -.
DR   VEuPathDB; HostDB:ENSRNOG00000063815; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   GeneTree; ENSGT00940000154432; -.
DR   OMA; PNMGFRS; -.
DR   OrthoDB; 780670at2759; -.
DR   PhylomeDB; P50235; -.
DR   Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR   Reactome; R-RNO-9753281; Paracetamol ADME.
DR   PRO; PR:P50235; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000047986; Expressed in liver and 16 other tissues.
DR   ExpressionAtlas; P50235; baseline and differential.
DR   Genevisible; P50235; RN.
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="Alcohol sulfotransferase"
FT                   /id="PRO_0000085146"
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;  33531 MW;  5ACA58A859F9D4D5 CRC64;
     MMSDYTWFEG IPFPAFWFSK EILENSCKKF VVKEDDLIIL TYPKSGTNWL IEIVCLIQTK
     GDPKWIQSMP IWDRSPWIET GSGYDKLTKM EGPRLMTSHL PMHLFSKSLF SSKAKVIYLI
     RNPRDVLVSA YFFWSKIALE KKPDSLGTYV EWFLKGNVAY GSWFEHIRGW LSMREWDNFL
     VLYYEDMKKD TMGSIKKICD FLGKKLEPDE LNLVLKYSSF QVVKENNMSN YSLMEKELIL
     TGFTFMRKGT TNDWKNHFTV AQAEAFDKVF QEKMAGFPPG MFPWE