ST1E1_BOVIN
ID ST1E1_BOVIN Reviewed; 295 AA.
AC P19217;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sulfotransferase 1E1;
DE Short=ST1E1;
DE EC=2.8.2.4 {ECO:0000269|PubMed:1900200};
DE AltName: Full=Estrogen sulfotransferase;
DE AltName: Full=Sulfotransferase, estrogen-preferring;
GN Name=SULT1E1; Synonyms=OST, STE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=3271383; DOI=10.1071/bi9880507;
RA Nash A.R., Glenn W.K., Moore S.S., Kerr J., Thompson A.R., Thompson E.O.P.;
RT "Oestrogen sulfotransferase: molecular cloning and sequencing of cDNA for
RT the bovine placental enzyme.";
RL Aust. J. Biol. Sci. 41:507-516(1988).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=3270501; DOI=10.1071/bi9880333;
RA Moore S.S., Thompson E.O.P., Nash A.R.;
RT "Oestrogen sulfotransferase: isolation of a high specific activity species
RT from bovine placenta.";
RL Aust. J. Biol. Sci. 41:333-341(1988).
RN [3]
RP PROTEIN SEQUENCE OF 146-160 AND 206-220, SUBUNIT, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RC TISSUE=Placenta;
RX PubMed=1900200; DOI=10.1016/0167-4838(91)90279-9;
RA Adams J.B.;
RT "Enzymic synthesis of steroid sulphates. XVII. On the structure of bovine
RT estrogen sulphotransferase.";
RL Biochim. Biophys. Acta 1076:282-288(1991).
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 (PubMed:1900200) (By similarity). Is a key enzyme
CC in estrogen homeostasis, the sulfation of estrogens leads to their
CC inactivation. Also sulfates dehydroepiandrosterone (DHEA),
CC pregnenolone, (24S)-hydroxycholesterol and xenobiotic compounds like
CC ethinylestradiol, equalenin, diethyl stilbesterol and 1-naphthol at
CC significantly lower efficiency. Does not sulfonate cortisol,
CC testosterone and dopamine (By similarity). 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 ECO:0000269|PubMed:1900200}.
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:0000269|PubMed:1900200};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000305|PubMed:1900200};
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:0000269|PubMed:1900200}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P49887}.
CC -!- INDUCTION: By progesterone.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; M54942; AAA30679.1; -; mRNA.
DR EMBL; X56395; CAA39806.1; -; mRNA.
DR PIR; S29045; S29045.
DR AlphaFoldDB; P19217; -.
DR SMR; P19217; -.
DR STRING; 9913.ENSBTAP00000015862; -.
DR BindingDB; P19217; -.
DR ChEMBL; CHEMBL2244; -.
DR PaxDb; P19217; -.
DR PRIDE; P19217; -.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; P19217; -.
DR BRENDA; 2.8.2.4; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
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; Direct protein sequencing; Lipid metabolism; Lipid-binding;
KW Phosphoprotein; Reference proteome; Steroid-binding; Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1E1"
FT /id="PRO_0000085151"
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 216
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 228
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT CONFLICT 117
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="M -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 34640 MW; 69147C73146913FD CRC64;
MSSSKPSFSD YFGKLGGIPM YKKFIEQFHN VEEFEARPDD LVIVTYPKSG TTWLSEIICM
IYNNGDVEKC KEDVIFNRVP YLECSTEHVM KGVKQLNEMA SPRIVKSHLP VKLLPVSFWE
KNCKIIYLSR NAKDVVVSYY FLILMVTAIP DPDSFQDFVE KFMDGEVPYG SWFEHTKSWW
EKSKNPQVLF LFYEDMKENI RKEVMKLLEF LGRKASDELV DKIIKHTSFQ EMKNNPSTNY
TTLPDEVMNQ KVSPFMRKGD VGDWKNHFTV ALNEKFDMHY EQQMKGSTLK FRTKI
