ST2S2_DANRE
ID ST2S2_DANRE Reviewed; 301 AA.
AC Q7ZUS4; Q7T1C7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cytosolic sulfotransferase 2;
DE EC=2.8.2.-;
DE AltName: Full=SULT1 ST2;
GN Name=sult1st2 {ECO:0000312|EMBL:AAH47850.1};
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:AAO64984.1}
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:AAH47850.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-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, T3 (triiodo-L-thyronine), T4 (thyroxine),
CC estrone and DOPA. {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 4.75 and 10.5. These two pH optima may correspond to
CC two distinct conformational states of the enzyme.;
CC Temperature dependence:
CC Active 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}.
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; AY181065; AAO64984.1; -; mRNA.
DR EMBL; BC047850; AAH47850.1; -; mRNA.
DR RefSeq; NP_899190.2; NM_183347.2.
DR AlphaFoldDB; Q7ZUS4; -.
DR SMR; Q7ZUS4; -.
DR STRING; 7955.ENSDARP00000030476; -.
DR PaxDb; Q7ZUS4; -.
DR PRIDE; Q7ZUS4; -.
DR GeneID; 791732; -.
DR KEGG; dre:791732; -.
DR CTD; 791732; -.
DR ZFIN; ZDB-GENE-030804-27; sult1st2.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; Q7ZUS4; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q7ZUS4; -.
DR BRENDA; 2.8.2.15; 928.
DR Reactome; R-DRE-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-DRE-9753281; Paracetamol ADME.
DR PRO; PR:Q7ZUS4; -.
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:0004304; F:estrone sulfotransferase activity; IDA:ZFIN.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008210; P:estrogen metabolic process; IDA:ZFIN.
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 2"
FT /id="PRO_0000085174"
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"
FT CONFLICT 111
FT /note="P -> L (in Ref. 1; AAO64984)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="T -> A (in Ref. 1; AAO64984)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="V -> A (in Ref. 1; AAO64984)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="V -> D (in Ref. 1; AAO64984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 35364 MW; 5943B7C4E33C621C CRC64;
MEIPDFSSMK LDSRPELIDF EGVSMTRYFT DNWEKVKNFQ ARPDDILIAT YPKAGTTWVS
YILDLLYFGN ESPERQTSQP IYMRVPFLEM CFQGLPLGTE LADTLPTSPR PIKTHLPVQL
VPKSFWEQNS KVVYVARNAK DNAVSYFHFD RMNMGQPEPG DWNTFLQKFM DGRNVFGPWY
DHVNGYWKKK QTYSNILYMF YEDMVEDTGR EVARLCSFLG LSTSATERER ITKGVQFDVM
KQNKMTNYST LPVMDFKISP FMRKGKVGDW RNHFTVAQNE QFDEVYKQKM KNTTVKFRTE
I
