ID   ST1E2_RAT               Reviewed;         295 AA.
AC   P52845;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Estrogen sulfotransferase, isoform 2;
DE            Short=EST-2;
DE            EC=2.8.2.4;
DE   AltName: Full=Estrone sulfotransferase;
DE   AltName: Full=Sulfotransferase, estrogen-preferring;
GN   Name=Ste2; Synonyms=Ste;
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. May play a role in the regulation of estrogen
CC       receptor activity by metabolizing free estradiol (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; U50205; AAB07681.1; -; mRNA.
DR   AlphaFoldDB; P52845; -.
DR   SMR; P52845; -.
DR   iPTMnet; P52845; -.
DR   PRIDE; P52845; -.
DR   RGD; 3776; Ste.
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; Lipid-binding; Phosphoprotein; Reference proteome;
KW   Steroid-binding; Transferase.
FT   CHAIN           1..295
FT                   /note="Estrogen sulfotransferase, isoform 2"
FT                   /id="PRO_0000085156"
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"
SQ   SEQUENCE   295 AA;  35365 MW;  149B5C9D46039AAF CRC64;
     METSMPEYYE VFGDFHGFLM DKLFTKYWED VETFSARPDD LLVVTYPKSG STWIGEIVDM
     IYKEGDVEKC KEDAIFNRIP YLECRNEDLI NGIKQLKEKE SPRIVKTHLP AKLLPASFWE
     KNCKIIYLCR NAKDVVVSYY YFFLIMKSYP NPKSFSEFVE KFMEGQVPYG SWYDHVKSWW
     EKSKNSRVLF MFYEDMKEDI RREVVKLIEF LERDPSAELV DRIIQHTSFQ EMKNNPCTNY
     SMLPETMIDL KVSPFMRKGI VGDWKNHFPE ALRERFEEHY QQQMKDCPVK FRAEL