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Estrogen sulfotransferase (EC 2.8.2.4) (EST-1) (Sulfotransferase 1E1) (ST1E1) (Sulfotransferase, estrogen-preferring)

 ST1E1_HUMAN             Reviewed;         294 AA.
P49888; Q8N6X5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 157.
RecName: Full=Estrogen sulfotransferase;
EC=2.8.2.4;
AltName: Full=EST-1;
AltName: Full=Sulfotransferase 1E1;
Short=ST1E1;
AltName: Full=Sulfotransferase, estrogen-preferring;
Name=SULT1E1; Synonyms=STE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8185618; DOI=10.1006/bbrc.1994.1637;
Aksoy I.A., Wood T.C., Weinshilboum R.M.;
"Human liver estrogen sulfotransferase: identification by cDNA cloning
and expression.";
Biochem. Biophys. Res. Commun. 200:1621-1629(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=8530066; DOI=10.1006/geno.1995.1210;
Her C., Aksoy I.A., Kimura S., Brandriff B.F., Wasmuth J.J.,
Weinshilboum R.M.;
"Human estrogen sulfotransferase gene (STE): cloning, structure, and
chromosomal localization.";
Genomics 29:16-23(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7779757; DOI=10.1016/0960-0760(95)00015-R;
Falany C.N., Krasnykh V., Falany J.L.;
"Bacterial expression and characterization of a cDNA for human liver
estrogen sulfotransferase.";
J. Steroid Biochem. Mol. Biol. 52:529-539(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10541560; DOI=10.1093/molehr/5.11.995;
Rubin G.L., Harrold A.J., Mills J.A., Falany C.N., Coughtrie M.W.H.;
"Regulation of sulphotransferase expression in the endometrium during
the menstrual cycle, by oral contraceptives and during early
pregnancy.";
Mol. Hum. Reprod. 5:995-1002(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-22.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 182-294.
TISSUE=Liver, and Spleen;
Her C., Szumlanski C., Aksoy I., Weinshilboum R.M.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[8]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT VAL-269 IN COMPLEX
WITH 3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE (PAPS), FUNCTION,
CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-137.
PubMed=11884392; DOI=10.1074/jbc.M111651200;
Pedersen L.C., Petrotchenko E., Shevtsov S., Negishi M.;
"Crystal structure of the human estrogen sulfotransferase-PAPS
complex: evidence for catalytic role of Ser137 in the sulfuryl
transfer reaction.";
J. Biol. Chem. 277:17928-17932(2002).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ADENOSINE
3',5'-BISPHOSPHATE (PAP) AND A HYDROXYLATED POLYCHLORINATED BIPHENYL
(OH-PCB).
PubMed=12782487; DOI=10.1289/ehp.6056;
Shevtsov S., Petrotchenko E.V., Pedersen L.C., Negishi M.;
"Crystallographic analysis of a hydroxylated polychlorinated biphenyl
(OH-PCB) bound to the catalytic estrogen binding site of human
estrogen sulfotransferase.";
Environ. Health Perspect. 111:884-888(2003).
-!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
sulfate (PAPS) as sulfonate donor to catalyze the sulfate
conjugation of estradiol and estrone. May play a role in the
regulation of estrogen receptor activity by metabolizing free
estradiol. Maximally sulfates beta-estradiol and estrone at
concentrations of 20 nM. Also sulfates dehydroepiandrosterone,
pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and
1-naphthol, at significantly higher concentrations; however,
cortisol, testosterone and dopamine are not sulfated.
{ECO:0000269|PubMed:11884392}.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + estrone =
adenosine 3',5'-bisphosphate + estrone 3-sulfate.
{ECO:0000269|PubMed:11884392}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11884392,
ECO:0000269|PubMed:12782487}.
-!- INTERACTION:
O76083:PDE9A; NbExp=3; IntAct=EBI-712512, EBI-742764;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Liver, intestine and at lower level in the
kidney.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ste/";
-----------------------------------------------------------------------
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EMBL; U08098; AAA82125.1; -; mRNA.
EMBL; U20521; AAC50286.1; -; Genomic_DNA.
EMBL; U20515; AAC50286.1; JOINED; Genomic_DNA.
EMBL; U20516; AAC50286.1; JOINED; Genomic_DNA.
EMBL; U20517; AAC50286.1; JOINED; Genomic_DNA.
EMBL; U20518; AAC50286.1; JOINED; Genomic_DNA.
EMBL; U20519; AAC50286.1; JOINED; Genomic_DNA.
EMBL; U20520; AAC50286.1; JOINED; Genomic_DNA.
EMBL; S77383; AAB34601.1; -; mRNA.
EMBL; Y11195; CAA72079.1; -; mRNA.
EMBL; AY436634; AAQ97179.1; -; Genomic_DNA.
EMBL; BC027956; AAH27956.1; -; mRNA.
EMBL; U55764; AAB51658.1; -; mRNA.
CCDS; CCDS3531.1; -.
PIR; JC2229; JC2229.
RefSeq; NP_005411.1; NM_005420.2.
UniGene; Hs.479898; -.
PDB; 1G3M; X-ray; 1.70 A; A/B=1-294.
PDB; 1HY3; X-ray; 1.80 A; A/B=1-294.
PDB; 4JVL; X-ray; 1.94 A; A/B=1-294.
PDB; 4JVM; X-ray; 1.99 A; A/B=1-294.
PDB; 4JVN; X-ray; 2.05 A; A/B=1-294.
PDBsum; 1G3M; -.
PDBsum; 1HY3; -.
PDBsum; 4JVL; -.
PDBsum; 4JVM; -.
PDBsum; 4JVN; -.
ProteinModelPortal; P49888; -.
SMR; P49888; -.
BioGrid; 112660; 14.
IntAct; P49888; 12.
MINT; MINT-1368473; -.
STRING; 9606.ENSP00000226444; -.
BindingDB; P49888; -.
ChEMBL; CHEMBL2346; -.
DrugBank; DB02902; 3'-Phosphate-Adenosine-5'-Phosphate Sulfate.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB01812; Adenosine-3'-5'-Diphosphate.
DrugBank; DB01176; Cyclizine.
SwissLipids; SLP:000001693; -.
iPTMnet; P49888; -.
PhosphoSitePlus; P49888; -.
BioMuta; SULT1E1; -.
DMDM; 1711604; -.
PaxDb; P49888; -.
PeptideAtlas; P49888; -.
PRIDE; P49888; -.
Ensembl; ENST00000226444; ENSP00000226444; ENSG00000109193.
GeneID; 6783; -.
KEGG; hsa:6783; -.
CTD; 6783; -.
DisGeNET; 6783; -.
EuPathDB; HostDB:ENSG00000109193.10; -.
GeneCards; SULT1E1; -.
HGNC; HGNC:11377; SULT1E1.
HPA; CAB047344; -.
HPA; HPA028213; -.
HPA; HPA028728; -.
MIM; 600043; gene.
neXtProt; NX_P49888; -.
OpenTargets; ENSG00000109193; -.
PharmGKB; PA340; -.
eggNOG; KOG1584; Eukaryota.
eggNOG; ENOG4111H56; LUCA.
GeneTree; ENSGT00760000118932; -.
HOGENOM; HOG000037209; -.
HOVERGEN; HBG001195; -.
InParanoid; P49888; -.
KO; K01016; -.
OMA; NQKVSPF; -.
OrthoDB; EOG091G0D5F; -.
PhylomeDB; P49888; -.
TreeFam; TF321745; -.
BRENDA; 2.8.2.4; 2681.
Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
EvolutionaryTrace; P49888; -.
GeneWiki; SULT1E1; -.
GenomeRNAi; 6783; -.
PRO; PR:P49888; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109193; -.
CleanEx; HS_SULT1E1; -.
ExpressionAtlas; P49888; baseline and differential.
Genevisible; P49888; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0004062; F:aryl sulfotransferase activity; TAS:Reactome.
GO; GO:0004304; F:estrone sulfotransferase activity; TAS:Reactome.
GO; GO:0047894; F:flavonol 3-sulfotransferase activity; IDA:BHF-UCL.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0050294; F:steroid sulfotransferase activity; IDA:UniProtKB.
GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
GO; GO:0006711; P:estrogen catabolic process; IDA:CAFA.
GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:CACAO.
GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc.
GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
Pfam; PF00685; Sulfotransfer_1; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Lipid-binding;
Polymorphism; Reference proteome; Steroid-binding; Transferase.
CHAIN 1 294 Estrogen sulfotransferase.
/FTId=PRO_0000085153.
NP_BIND 47 52 PAPS.
NP_BIND 226 231 PAPS.
NP_BIND 256 258 PAPS.
REGION 105 107 Substrate binding. {ECO:0000250}.
ACT_SITE 107 107 Proton acceptor. {ECO:0000250}.
BINDING 129 129 PAPS.
BINDING 137 137 PAPS.
BINDING 192 192 PAPS.
VARIANT 22 22 D -> Y (in dbSNP:rs11569705).
{ECO:0000269|Ref.5}.
/FTId=VAR_018907.
MUTAGEN 137 137 S->A: Decreased gradually the catalytic
activity. {ECO:0000269|PubMed:11884392}.
MUTAGEN 137 137 S->C: Decreased gradually the catalytic
activity. {ECO:0000269|PubMed:11884392}.
MUTAGEN 269 269 V->E: Does not prevent the formation of
homodimer.
CONFLICT 154 154 F -> L (in Ref. 6; AAH27956).
{ECO:0000305}.
HELIX 4 10 {ECO:0000244|PDB:1G3M}.
STRAND 11 14 {ECO:0000244|PDB:1G3M}.
STRAND 17 20 {ECO:0000244|PDB:1G3M}.
HELIX 21 25 {ECO:0000244|PDB:1G3M}.
HELIX 27 31 {ECO:0000244|PDB:1G3M}.
STRAND 40 45 {ECO:0000244|PDB:1G3M}.
HELIX 50 61 {ECO:0000244|PDB:1G3M}.
TURN 62 64 {ECO:0000244|PDB:1G3M}.
HELIX 66 69 {ECO:0000244|PDB:1G3M}.
STRAND 70 72 {ECO:0000244|PDB:1G3M}.
HELIX 74 77 {ECO:0000244|PDB:1G3M}.
TURN 86 88 {ECO:0000244|PDB:1G3M}.
HELIX 91 96 {ECO:0000244|PDB:1G3M}.
STRAND 103 106 {ECO:0000244|PDB:1G3M}.
HELIX 110 112 {ECO:0000244|PDB:1G3M}.
HELIX 115 119 {ECO:0000244|PDB:1G3M}.
STRAND 123 128 {ECO:0000244|PDB:1G3M}.
HELIX 131 144 {ECO:0000244|PDB:1G3M}.
HELIX 154 162 {ECO:0000244|PDB:1G3M}.
HELIX 171 181 {ECO:0000244|PDB:1G3M}.
STRAND 187 191 {ECO:0000244|PDB:1G3M}.
HELIX 192 197 {ECO:0000244|PDB:1G3M}.
HELIX 199 209 {ECO:0000244|PDB:1G3M}.
HELIX 216 225 {ECO:0000244|PDB:1G3M}.
HELIX 228 233 {ECO:0000244|PDB:1G3M}.
TURN 235 237 {ECO:0000244|PDB:1G3M}.
TURN 244 246 {ECO:0000244|PDB:1G3M}.
TURN 249 251 {ECO:0000244|PDB:1G3M}.
HELIX 262 265 {ECO:0000244|PDB:1G3M}.
HELIX 269 283 {ECO:0000244|PDB:1G3M}.
SEQUENCE 294 AA; 35126 MW; 9EC8923D20757D57 CRC64;
MNSELDYYEK FEEVHGILMY KDFVKYWDNV EAFQARPDDL VIATYPKSGT TWVSEIVYMI
YKEGDVEKCK EDVIFNRIPF LECRKENLMN GVKQLDEMNS PRIVKTHLPP ELLPASFWEK
DCKIIYLCRN AKDVAVSFYY FFLMVAGHPN PGSFPEFVEK FMQGQVPYGS WYKHVKSWWE
KGKSPRVLFL FYEDLKEDIR KEVIKLIHFL ERKPSEELVD RIIHHTSFQE MKNNPSTNYT
TLPDEIMNQK LSPFMRKGIT GDWKNHFTVA LNEKFDKHYE QQMKESTLKF RTEI


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