ID   ST1S3_DANRE             Reviewed;         301 AA.
AC   Q7T2V2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cytosolic sulfotransferase 3;
DE            EC=2.8.2.-;
DE   AltName: Full=SULT1 ST3;
GN   Name=sult1st3 {ECO:0000312|ZFIN:ZDB-GENE-030804-28};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAP55637.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY
RP   REGULATION.
RX   PubMed=12745256; DOI=10.1016/s0003-9861(03)00172-3;
RA   Sugahara T., Liu C.-C., Carter G., Pai T.G., Liu M.-C.;
RT   "cDNA cloning, expression, and functional characterization of a zebrafish
RT   SULT1 cytosolic sulfotransferase.";
RL   Arch. Biochem. Biophys. 414:67-73(2003).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a
CC       variety of xenobiotic and endogenous compounds, including dopamine, T3
CC       (triiodo-L-thyronine), T4 (thyroxine), estrone, DHEA
CC       (dehydroepiandrosterone), flavonoids, isoflavonoids and other phenolic
CC       compounds. {ECO:0000269|PubMed:12745256}.
CC   -!- ACTIVITY REGULATION: Inhibited by Hg(2+), Co(2+), Zn(2+), Cd(2+),
CC       Cu(2+) and Pb(2+) ions. Activated slightly by Mn(2+), Ca(2+) and Mg(2+)
CC       ions. {ECO:0000269|PubMed:12745256}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 5.0 with n-propyl gallate as substrate, and
CC         another smaller pH optimum is observed spanning pH 9.5-10.5. Optimum
CC         pH is 10.5 with dopamine as substrate.;
CC       Temperature dependence:
CC         Active from 20 to 43 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY196985; AAP55637.1; -; mRNA.
DR   AlphaFoldDB; Q7T2V2; -.
DR   SMR; Q7T2V2; -.
DR   STRING; 7955.ENSDARP00000006665; -.
DR   PaxDb; Q7T2V2; -.
DR   ZFIN; ZDB-GENE-030804-28; sult1st3.
DR   eggNOG; KOG1584; Eukaryota.
DR   InParanoid; Q7T2V2; -.
DR   PhylomeDB; Q7T2V2; -.
DR   Reactome; R-DRE-156584; Cytosolic sulfonation of small molecules.
DR   Reactome; R-DRE-9753281; Paracetamol ADME.
DR   PRO; PR:Q7T2V2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004062; F:aryl sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR   GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Catecholamine metabolism; Cytoplasm; Lipid metabolism; Reference proteome;
KW   Steroid metabolism; Transferase.
FT   CHAIN           1..301
FT                   /note="Cytosolic sulfotransferase 3"
FT                   /id="PRO_0000085175"
FT   ACT_SITE        115
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..58
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..240
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         263..265
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  35377 MW;  2E4D05D4A38EB741 CRC64;
     MEISDFSSMK LNSRPELIDF EGISMIHYFT DNWEKVKNFQ ARPDDILIAT YPKAGTTWVS
     YILDLLYFGN ESPERQTSQP IYMRVPFLEA CFEGIPFGTE LADNLPTSPR LIKTHLPVQL
     VPKSFWEQNS KVVYVARNAK DNAVSYFHFD RMNMGQPEPG DWNTFLQKFM EGRNVFGPWY
     DHVNGYWKKK QTYSNILYMF YEDMVENTGR EVERLCSFLG LSTSAAERER ITKGVQFDAM
     KQNKMTNYST IPVMDFKISP FMRKGKVGDW RNHFTVAQNE QFDEVYKQKM KNTTVKFRTE
     L