ID   ST1S1_DANRE             Reviewed;         299 AA.
AC   Q6PH37; Q7T1C8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cytosolic sulfotransferase 1;
DE            EC=2.8.2.-;
DE   AltName: Full=SULT1 ST1;
GN   Name=sult1st1 {ECO:0000312|EMBL:AAH56729.1};
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:AAO64983.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY
RP   REGULATION.
RX   PubMed=12755695; DOI=10.1046/j.1432-1033.2003.03608.x;
RA   Sugahara T., Liu C.-C., Pai T.G., Collodi P., Suiko M., Sakakibara Y.,
RA   Nishiyama K., Liu M.-C.;
RT   "Sulfation of hydroxychlorobiphenyls. Molecular cloning, expression, and
RT   functional characterization of zebrafish SULT1 sulfotransferases.";
RL   Eur. J. Biochem. 270:2404-2411(2003).
RN   [2] {ECO:0000312|EMBL:AAH56729.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH56729.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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 2-naphthol,
CC       hydroxychlorobiphenyls, dopamine and T3 (triiodo-L-thyronine).
CC       {ECO:0000269|PubMed:12755695}.
CC   -!- ACTIVITY REGULATION: Inhibited by Co(2+), Zn(2+), Cd(2+) and Pb(2+)
CC       ions. Inactivated by Hg(2+) and Cu(2+) ions.
CC       {ECO:0000269|PubMed:12755695}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0-9.0.;
CC       Temperature dependence:
CC         Thermostable from 20 to 43 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:12755695}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; AY181064; AAO64983.1; -; mRNA.
DR   EMBL; BC056729; AAH56729.1; -; mRNA.
DR   RefSeq; NP_891986.1; NM_182941.1.
DR   AlphaFoldDB; Q6PH37; -.
DR   SMR; Q6PH37; -.
DR   STRING; 7955.ENSDARP00000034116; -.
DR   PaxDb; Q6PH37; -.
DR   GeneID; 323424; -.
DR   KEGG; dre:323424; -.
DR   CTD; 323424; -.
DR   ZFIN; ZDB-GENE-030131-2144; sult1st1.
DR   eggNOG; KOG1584; Eukaryota.
DR   InParanoid; Q6PH37; -.
DR   OrthoDB; 780670at2759; -.
DR   PhylomeDB; Q6PH37; -.
DR   Reactome; R-DRE-156584; Cytosolic sulfonation of small molecules.
DR   Reactome; R-DRE-9753281; Paracetamol ADME.
DR   PRO; PR:Q6PH37; -.
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: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; Reference proteome; Transferase.
FT   CHAIN           1..299
FT                   /note="Cytosolic sulfotransferase 1"
FT                   /id="PRO_0000085173"
FT   ACT_SITE        113
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         51..56
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         233..238
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         261..263
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        3
FT                   /note="I -> M (in Ref. 1; AAO64983)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="N -> T (in Ref. 1; AAO64983)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   299 AA;  35035 MW;  805D82915B45EB6A CRC64;
     MDIPDFSSIS SRPTIFEFEG ISMINHFTEN WEKVKNFQAR PDDILIATYP KAGTTWVSYI
     LDLLYFGENA PEEHTSQPIY MRVPFLESCF KVIASGTELA DNMTTSPRLI KTHLPVQLIP
     KSFWEQNSRV VYVARNAKDN VVSYFHFDRM NIVEPDPGDW NTFLHRFMDG KSVFGPWYDH
     VNGYWEKKQT YSNLLYLFYE DLVEDTGREV DRLCSFLGLS TSVSDREKIT KDVQFDAMKQ
     NKMTNYSTLP VMDFKISPFM RKGKVGDWKN HFTVAQNEQF DEVYKEKMKN ATVKFRTEI