ST1E1_RAT
ID ST1E1_RAT Reviewed; 295 AA.
AC P52844;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Sulfotransferase 1E1;
DE Short=ST1E1;
DE EC=2.8.2.4 {ECO:0000250|UniProtKB:P49888};
DE AltName: Full=Estrogen sulfotransferase, isoform 1;
DE Short=EST-1;
DE AltName: Full=Estrone sulfotransferase;
DE AltName: Full=Sulfotransferase, estrogen-preferring;
GN Name=Sult1e1; Synonyms=Ste, Ste1;
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=Fischer 344; TISSUE=Liver;
RX PubMed=8688469; DOI=10.1016/0167-4781(96)00065-6;
RA Rikke B.A., Roy A.K.;
RT "Structural relationships among members of the mammalian sulfotransferase
RT gene family.";
RL Biochim. Biophys. Acta 1307:331-338(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC estradiol and estrone. Is a key enzyme in estrogen homeostasis, the
CC sulfation of estrogens leads to their inactivation. Also sulfates
CC dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesterol
CC and xenobiotic compounds like ethinylestradiol, equalenin, diethyl
CC stilbesterol and 1-naphthol at significantly lower efficiency. Does not
CC sulfonate cortisol, testosterone and dopamine. May play a role in gut
CC microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-
CC EP), a dietary tyrosine-derived metabolite produced by gut bacteria.
CC The product 4-EPS crosses the blood-brain barrier and may negatively
CC regulate oligodendrocyte maturation and myelination, affecting the
CC functional connectivity of different brain regions associated with the
CC limbic system. {ECO:0000250|UniProtKB:P49888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-
CC bisphosphate + estrone 3-sulfate + H(+); Xref=Rhea:RHEA:15973,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17263, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:60050; EC=2.8.2.4;
CC Evidence={ECO:0000250|UniProtKB:P49888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15974;
CC Evidence={ECO:0000250|UniProtKB:P49888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567;
CC Evidence={ECO:0000250|UniProtKB:P49888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC Evidence={ECO:0000250|UniProtKB:P49888};
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:0000250|UniProtKB:P49888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000250|UniProtKB:P49888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC Evidence={ECO:0000250|UniProtKB:P49888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl
CC sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133681;
CC Evidence={ECO:0000250|UniProtKB:P49888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC Evidence={ECO:0000250|UniProtKB:P49888};
CC -!- ACTIVITY REGULATION: Inhibited by estradiol.
CC {ECO:0000250|UniProtKB:P49888}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49888}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P49887}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; U50204; AAB07680.1; -; mRNA.
DR AlphaFoldDB; P52844; -.
DR SMR; P52844; -.
DR iPTMnet; P52844; -.
DR PRIDE; P52844; -.
DR RGD; 3776; Sult1e1.
DR BRENDA; 2.8.2.4; 5301.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0004304; F:estrone sulfotransferase activity; IDA:RGD.
DR GO; GO:0047894; F:flavonol 3-sulfotransferase activity; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:RGD.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
DR GO; GO:0006711; P:estrogen catabolic process; ISO:RGD.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; ISO:RGD.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0051923; P:sulfation; ISO:RGD.
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; Lipid metabolism; Lipid-binding; Phosphoprotein;
KW Reference proteome; Steroid-binding; Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1E1"
FT /id="PRO_0000085155"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 227..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 257..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 295 AA; 35509 MW; 696A12FDA923A12E CRC64;
METSMPEYYE VFGDFHGFLM DKRFTKYWED IETFLARPDD LLIVTYPKSG STWISEIVDM
IYKEGDVEKC KEDALFNRIP DLECRNEDLI NGIKQLKEKE SPRIVKTHLP AKLLPASFWE
KNCKIIYLCR NAKDVVVSYY YFFLIMKSYP NPKSFSEFVE KFMEGQVPYG SWYDHVKSWW
EKSKNSRVLF MFYEDMKEDI RREVVKLIEF LERDPSAELV DRIIQHTSFQ EMKNNPCTNY
SMLPETMIDL KVSPFMRKGI VGDWRNHFPE ALRERFEEHY QRHMKDCPVK FRAEL
