GENTAUR Molecular Products.

 ST1E1_HUMAN             Reviewed;         294 AA.
 P49888; Q8N6X5;
 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
 01-OCT-1996, sequence version 1.
 16-JAN-2019, entry version 165.
 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:
     Reaction=3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-
       bisphosphate + estrone 3-sulfate + H(+); Xref=Rhea:RHEA:15973,
       ChEBI:CHEBI:15378, ChEBI:CHEBI:17263, ChEBI:CHEBI:58339,
       ChEBI:CHEBI:58343, ChEBI:CHEBI:60050; EC=2.8.2.4;
       Evidence={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.
 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; -.
 EPD; P49888; -.
 PaxDb; P49888; -.
 PeptideAtlas; P49888; -.
 PRIDE; P49888; -.
 ProteomicsDB; 56163; -.
 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; ENSGT00940000162261; -.
 HOGENOM; HOG000037209; -.
 HOVERGEN; HBG001195; -.
 InParanoid; P49888; -.
 KO; K01016; -.
 OMA; VETFQAR; -.
 OrthoDB; 780670at2759; -.
 PhylomeDB; P49888; -.
 TreeFam; TF321745; -.
 BRENDA; 2.8.2.4; 2681.
 Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
 SIGNOR; P49888; -.
 ChiTaRS; SULT1E1; human.
 EvolutionaryTrace; P49888; -.
 GeneWiki; SULT1E1; -.
 GenomeRNAi; 6783; -.
 PRO; PR:P49888; -.
 Proteomes; UP000005640; Chromosome 4.
 Bgee; ENSG00000109193; Expressed in 106 organ(s), highest expression level in kidney.
 CleanEx; HS_SULT1E1; -.
 ExpressionAtlas; P49888; baseline and differential.
 Genevisible; P49888; HS.
 GO; GO:0005829; C:cytosol; IDA:HPA.
 GO; GO:0031965; C:nuclear membrane; IDA:HPA.
 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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