ST1C4_MACFA
ID ST1C4_MACFA Reviewed; 302 AA.
AC A0A2K5X3B6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Sulfotransferase 1C4;
DE Short=ST1C4;
DE EC=2.8.2.1 {ECO:0000269|PubMed:31100221};
GN Name=SULT1C4;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=31100221; DOI=10.1016/j.bcp.2019.05.018;
RA Uno Y., Murayama N., Yamazaki H.;
RT "Molecular and functional characterization of cytosolic sulfotransferases
RT in cynomolgus macaque.";
RL Biochem. Pharmacol. 166:153-162(2019).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC phenolic compounds and estrogen (E2) (PubMed:31100221). Can also
CC sulfonate estrogenic compounds, however, the dietary flavonoids
CC (phytoestrogen) and environmental estrogens, like bisphenol A are
CC better substrates than 17beta-estradiol (E2) (By similarity).
CC {ECO:0000250|UniProtKB:O75897, ECO:0000269|PubMed:31100221}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC Evidence={ECO:0000269|PubMed:31100221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:31100221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-
CC estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582;
CC Evidence={ECO:0000269|PubMed:31100221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000305|PubMed:31100221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + bisphenol A = adenosine 3',5'-
CC bisphosphate + bisphenyl A sulfate + H(+); Xref=Rhea:RHEA:66580,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33216, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:167171;
CC Evidence={ECO:0000250|UniProtKB:O75897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66581;
CC Evidence={ECO:0000250|UniProtKB:O75897};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:31100221}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney and jejunum.
CC {ECO:0000269|PubMed:31100221}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AQIA01016952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; A0A2K5X3B6; -.
DR STRING; 9541.XP_005575266.1; -.
DR Ensembl; ENSMFAT00000073312; ENSMFAP00000060137; ENSMFAG00000039337.
DR VEuPathDB; HostDB:ENSMFAG00000039337; -.
DR BRENDA; 2.8.2.2; 1793.
DR Proteomes; UP000233100; Chromosome 13.
DR Bgee; ENSMFAG00000039337; Expressed in liver and 10 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:UniProtKB.
DR GO; GO:0009812; P:flavonoid metabolic process; ISS: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 Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="Sulfotransferase 1C4"
FT /id="PRO_0000453622"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 55..60
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 113..115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 145
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 200
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 234..239
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
FT BINDING 262..266
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O75897"
SQ SEQUENCE 302 AA; 35660 MW; 17EE35A25D3D53B4 CRC64;
TALHKMEDFT FDGTKRLSVN YVKGILQPTV TCDIWDEIWN FQAKPDDLLI STYPKAGTTW
TQEIVELIQN EGDVEKSKRA PTHQRFPFLE WKIPSLGSGL EQAQAMPSPR ILKTHLPFHL
LPPSFLEKNC KIIYVARNPK DNMVSYYHFQ RMNKALPDPG TWEEYFETFL AGKVCWGSWH
EHVKGWWEAK DKHRILYLFY EDMKKNPKHE VQKLTEFIEK KLDDKVLDKI VHYTSFDVMK
QNSMANYSSI PAEIMDHSIS PFMRKGAVGD WKKHFTVAQN ERFDEDYKKK MADTRLTFHF
QF
