ST1E3_RAT
ID ST1E3_RAT Reviewed; 295 AA.
AC P49889; Q9QWS0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Estrogen sulfotransferase, isoform 3;
DE Short=EST-3;
DE EC=2.8.2.4 {ECO:0000269|PubMed:7857871};
DE AltName: Full=Estrone sulfotransferase;
DE AltName: Full=Sulfotransferase, estrogen-preferring;
GN Name=Ste {ECO:0000312|RGD:3776};
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], AND PROTEIN SEQUENCE OF 258-265.
RC TISSUE=Liver;
RX PubMed=1374839; DOI=10.1210/mend.6.4.1374839;
RA Demyan W.F., Song C.S., Kim D.S., Her S., Gallwitz W., Rao T.R.,
RA Slomczynska M., Chatterjee B., Roy A.K.;
RT "Estrogen sulfotransferase of the rat liver: complementary DNA cloning and
RT age- and sex-specific regulation of messenger RNA.";
RL Mol. Endocrinol. 6:589-597(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7857871; DOI=10.1016/0960-0760(94)00147-e;
RA Falany J.L., Krasnykh V., Mikheeva G., Falany C.N.;
RT "Isolation and expression of an isoform of rat estrogen sulfotransferase.";
RL J. Steroid Biochem. Mol. Biol. 52:35-44(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12173467;
RA Astapova I.I., Smirnov A.N., Rubtsov P.M.;
RT "PCR amplification and structural analysis of two paralogous rat estrogen
RT sulfotransferase genes.";
RL Mol. Biol. (Mosk.) 36:635-642(2002).
RN [4]
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 (PubMed:7857871). May play a role in the
CC regulation of estrogen receptor activity by metabolizing free estradiol
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:7857871}.
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:0000269|PubMed:7857871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15974;
CC Evidence={ECO:0000305|PubMed:7857871};
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:7857871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000305|PubMed:7857871};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Liver of young mature males and uterus.
CC {ECO:0000269|PubMed:1374839}.
CC -!- DEVELOPMENTAL STAGE: Expressed only in the liver of young adult animals
CC (100 days old) and is absent in the prepubertal male (27 days old),
CC senescent male (800 days old) and female liver.
CC -!- INDUCTION: Induced by androgens and suppressed by estrogens. The
CC expression is under the influence of pituitary growth hormone and
CC thyroid hormone. Is regulated by progesterone in the uterus.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; M86758; AAA41128.1; -; mRNA.
DR EMBL; S76489; AAB33441.1; -; mRNA.
DR EMBL; AJ131835; CAA10515.2; -; Genomic_DNA.
DR EMBL; AJ298109; CAA10515.2; JOINED; Genomic_DNA.
DR EMBL; AJ298110; CAA10515.2; JOINED; Genomic_DNA.
DR EMBL; AJ298111; CAA10515.2; JOINED; Genomic_DNA.
DR EMBL; AJ298112; CAA10515.2; JOINED; Genomic_DNA.
DR EMBL; AJ298113; CAA10515.2; JOINED; Genomic_DNA.
DR EMBL; AJ298114; CAA10515.2; JOINED; Genomic_DNA.
DR PIR; A41930; A41930.
DR PIR; I56606; I56606.
DR RefSeq; NP_037015.1; NM_012883.1.
DR AlphaFoldDB; P49889; -.
DR SMR; P49889; -.
DR ChEMBL; CHEMBL4831; -.
DR iPTMnet; P49889; -.
DR PhosphoSitePlus; P49889; -.
DR PRIDE; P49889; -.
DR GeneID; 360268; -.
DR KEGG; rno:360268; -.
DR UCSC; RGD:3776; rat.
DR CTD; 6783; -.
DR RGD; 3776; Ste.
DR InParanoid; P49889; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P49889; -.
DR Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
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; Direct protein sequencing; Lipid-binding; Phosphoprotein;
KW Reference proteome; Steroid-binding; Transferase.
FT CHAIN 1..295
FT /note="Estrogen sulfotransferase, isoform 3"
FT /id="PRO_0000085157"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 227..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 257..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 150
FT /note="P -> Q (in Ref. 2; AAB33441)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="T -> I (in Ref. 2; AAB33441)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="L -> P (in Ref. 2; AAB33441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 35416 MW; A77807A21DD2E7EB CRC64;
METSMPEYYD VFGDFHGFLM DKRFTKYWED VETFLARPDD LLIVTYPKSG STWISEIVDM
IYKEGDVEKC KEDALFNRIP DLECRNEDLI NGIKQLKEKE SPRIVKTHLP AKLLPASFWE
KNCKIIYLCR NAKDVVVSYY YFFLIMKSYP NPKSFSEFVE KFMEGQVPYG SWYDHVKSWW
EKSKNSRVLF MFYEDMKEDI RREVVKLIEF LERDPSAELV DRIIQHTSFQ EMKNNPCTNY
SMLPETMIDL KVSPFMRKGI VGDWKNHFPE ALRERFEEHY QQQMKDCPVK FRAEL
