ST1E1_HUMAN
ID ST1E1_HUMAN Reviewed; 294 AA.
AC P49888; Q8N6X5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Sulfotransferase 1E1;
DE Short=ST1E1;
DE EC=2.8.2.4 {ECO:0000269|PubMed:11884392, ECO:0000269|PubMed:7779757};
DE AltName: Full=EST-1 {ECO:0000303|PubMed:7779757};
DE AltName: Full=Estrogen sulfotransferase {ECO:0000303|PubMed:8185618};
DE AltName: Full=Sulfotransferase, estrogen-preferring;
GN Name=SULT1E1; Synonyms=STE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8185618; DOI=10.1006/bbrc.1994.1637;
RA Aksoy I.A., Wood T.C., Weinshilboum R.M.;
RT "Human liver estrogen sulfotransferase: identification by cDNA cloning and
RT expression.";
RL Biochem. Biophys. Res. Commun. 200:1621-1629(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8530066; DOI=10.1006/geno.1995.1210;
RA Her C., Aksoy I.A., Kimura S., Brandriff B.F., Wasmuth J.J.,
RA Weinshilboum R.M.;
RT "Human estrogen sulfotransferase gene (STE): cloning, structure, and
RT chromosomal localization.";
RL Genomics 29:16-23(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
RP FUNCTION.
RC TISSUE=Liver;
RX PubMed=7779757; DOI=10.1016/0960-0760(95)00015-r;
RA Falany C.N., Krasnykh V., Falany J.L.;
RT "Bacterial expression and characterization of a cDNA for human liver
RT estrogen sulfotransferase.";
RL J. Steroid Biochem. Mol. Biol. 52:529-539(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10541560; DOI=10.1093/molehr/5.11.995;
RA Rubin G.L., Harrold A.J., Mills J.A., Falany C.N., Coughtrie M.W.H.;
RT "Regulation of sulphotransferase expression in the endometrium during the
RT menstrual cycle, by oral contraceptives and during early pregnancy.";
RL Mol. Hum. Reprod. 5:995-1002(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-22.
RG NIEHS SNPs program;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 182-294.
RC TISSUE=Liver, and Spleen;
RA Her C., Szumlanski C., Aksoy I., Weinshilboum R.M.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP MUTAGENESIS OF LYS-85; HIS-107 AND VAL-145, CATALYTIC ACTIVITY, FUNCTION,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP AND ACTIVE SITE.
RX PubMed=11006110; DOI=10.1006/bbrc.2000.3473;
RA Hempel N., Barnett A.C., Bolton-Grob R.M., Liyou N.E., McManus M.E.;
RT "Site-directed mutagenesis of the substrate-binding cleft of human estrogen
RT sulfotransferase.";
RL Biochem. Biophys. Res. Commun. 276:224-230(2000).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=19589875; DOI=10.1124/dmd.108.025759;
RA Cook I.T., Duniec-Dmuchowski Z., Kocarek T.A., Runge-Morris M.,
RA Falany C.N.;
RT "24-hydroxycholesterol sulfation by human cytosolic sulfotransferases:
RT formation of monosulfates and disulfates, molecular modeling, sulfatase
RT sensitivity, and inhibition of liver x receptor activation.";
RL Drug Metab. Dispos. 37:2069-2078(2009).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=35165440; DOI=10.1038/s41586-022-04396-8;
RA Needham B.D., Funabashi M., Adame M.D., Wang Z., Boktor J.C., Haney J.,
RA Wu W.L., Rabut C., Ladinsky M.S., Hwang S.J., Guo Y., Zhu Q.,
RA Griffiths J.A., Knight R., Bjorkman P.J., Shapiro M.G., Geschwind D.H.,
RA Holschneider D.P., Fischbach M.A., Mazmanian S.K.;
RT "A gut-derived metabolite alters brain activity and anxiety behaviour in
RT mice.";
RL Nature 602:647-653(2022).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT VAL-269 IN COMPLEX WITH
RP 3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE (PAPS), FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF SER-137, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=11884392; DOI=10.1074/jbc.m111651200;
RA Pedersen L.C., Petrotchenko E., Shevtsov S., Negishi M.;
RT "Crystal structure of the human estrogen sulfotransferase-PAPS complex:
RT evidence for catalytic role of Ser137 in the sulfuryl transfer reaction.";
RL J. Biol. Chem. 277:17928-17932(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ADENOSINE
RP 3',5'-BISPHOSPHATE (PAP) AND A HYDROXYLATED POLYCHLORINATED BIPHENYL
RP (OH-PCB).
RX PubMed=12782487; DOI=10.1289/ehp.6056;
RA Shevtsov S., Petrotchenko E.V., Pedersen L.C., Negishi M.;
RT "Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-
RT PCB) bound to the catalytic estrogen binding site of human estrogen
RT sulfotransferase.";
RL Environ. Health Perspect. 111:884-888(2003).
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:7779757, PubMed:11884392,
CC PubMed:11006110). Is a key enzyme in estrogen homeostasis, the
CC sulfation of estrogens leads to their inactivation. Also sulfates
CC dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesterol
CC and xenobiotic compounds like ethinylestradiol, equalenin, diethyl
CC stilbesterol and 1-naphthol at significantly lower efficiency
CC (PubMed:11006110, PubMed:19589875). Does not sulfonate cortisol,
CC testosterone and dopamine (PubMed:7779757, PubMed:11006110). May play a
CC role in gut microbiota-host metabolic interaction. O-sulfonates 4-
CC ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by
CC gut bacteria. The product 4-EPS crosses the blood-brain barrier and may
CC negatively regulate oligodendrocyte maturation and myelination,
CC affecting the functional connectivity of different brain regions
CC associated with the limbic system. {ECO:0000269|PubMed:11006110,
CC ECO:0000269|PubMed:11884392, ECO:0000269|PubMed:19589875,
CC ECO:0000269|PubMed:35165440, ECO:0000269|PubMed:7779757}.
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:11006110, ECO:0000269|PubMed:11884392,
CC ECO:0000269|PubMed:7779757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15974;
CC Evidence={ECO:0000305|PubMed:11884392};
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:0000269|PubMed:19589875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC Evidence={ECO:0000305|PubMed:19589875};
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:11006110, ECO:0000269|PubMed:7779757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000305|PubMed:7779757};
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:0000269|PubMed:11006110};
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:0000269|PubMed:35165440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC Evidence={ECO:0000305|PubMed:35165440};
CC -!- ACTIVITY REGULATION: Inhibited by estradiol.
CC {ECO:0000269|PubMed:11006110}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 uM for 17beta-estradiol {ECO:0000269|PubMed:11006110};
CC KM=0.2 uM for estrone {ECO:0000269|PubMed:11006110};
CC KM=0.2 uM for DHEA {ECO:0000269|PubMed:11006110};
CC KM=32220 uM for dopamine {ECO:0000269|PubMed:11006110};
CC KM=76.6 uM for p-nitrophenol {ECO:0000269|PubMed:11006110};
CC KM=0.9 uM for (24S)-hydroxycholesterol {ECO:0000269|PubMed:19589875};
CC KM=0.66 uM for PAPS {ECO:0000269|PubMed:11884392};
CC KM=0.46 uM for PAPS {ECO:0000269|PubMed:11006110};
CC Vmax=37.2 nmol/min/mg enzyme with 17beta-estradiol
CC {ECO:0000269|PubMed:11006110};
CC Vmax=16.3 nmol/min/mg enzyme with estrone
CC {ECO:0000269|PubMed:11006110};
CC Vmax=5.5 nmol/min/mg enzyme with DHEA {ECO:0000269|PubMed:11006110};
CC Vmax=13.3 nmol/min/mg enzyme with dopaminne;
CC Vmax=135.9 nmol/min/mg enzyme with p-nitrophenol
CC {ECO:0000269|PubMed:11006110};
CC Note=kcat is 55 min(-1) with (24S)-hydroxycholesterol.
CC {ECO:0000269|PubMed:19589875};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11884392,
CC ECO:0000269|PubMed:12782487}.
CC -!- INTERACTION:
CC P49888; O76083: PDE9A; NbExp=3; IntAct=EBI-712512, EBI-742764;
CC P49888; O76083-2: PDE9A; NbExp=3; IntAct=EBI-712512, EBI-11524542;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11006110}.
CC -!- TISSUE SPECIFICITY: Liver, intestine and at lower level in the kidney.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ste/";
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DR EMBL; U08098; AAA82125.1; -; mRNA.
DR EMBL; U20521; AAC50286.1; -; Genomic_DNA.
DR EMBL; U20515; AAC50286.1; JOINED; Genomic_DNA.
DR EMBL; U20516; AAC50286.1; JOINED; Genomic_DNA.
DR EMBL; U20517; AAC50286.1; JOINED; Genomic_DNA.
DR EMBL; U20518; AAC50286.1; JOINED; Genomic_DNA.
DR EMBL; U20519; AAC50286.1; JOINED; Genomic_DNA.
DR EMBL; U20520; AAC50286.1; JOINED; Genomic_DNA.
DR EMBL; S77383; AAB34601.1; -; mRNA.
DR EMBL; Y11195; CAA72079.1; -; mRNA.
DR EMBL; AY436634; AAQ97179.1; -; Genomic_DNA.
DR EMBL; BC027956; AAH27956.1; -; mRNA.
DR EMBL; U55764; AAB51658.1; -; mRNA.
DR CCDS; CCDS3531.1; -.
DR PIR; JC2229; JC2229.
DR RefSeq; NP_005411.1; NM_005420.2.
DR PDB; 1G3M; X-ray; 1.70 A; A/B=1-294.
DR PDB; 1HY3; X-ray; 1.80 A; A/B=1-294.
DR PDB; 4JVL; X-ray; 1.94 A; A/B=1-294.
DR PDB; 4JVM; X-ray; 1.99 A; A/B=1-294.
DR PDB; 4JVN; X-ray; 2.05 A; A/B=1-294.
DR PDBsum; 1G3M; -.
DR PDBsum; 1HY3; -.
DR PDBsum; 4JVL; -.
DR PDBsum; 4JVM; -.
DR PDBsum; 4JVN; -.
DR AlphaFoldDB; P49888; -.
DR SMR; P49888; -.
DR BioGRID; 112660; 14.
DR IntAct; P49888; 12.
DR STRING; 9606.ENSP00000226444; -.
DR BindingDB; P49888; -.
DR ChEMBL; CHEMBL2346; -.
DR DrugBank; DB02902; 3'-phospho-5'-adenylyl sulfate.
DR DrugBank; DB03346; 3,3',5,5'-tetrachlorobiphenyl-4,4'-diol.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB01176; Cyclizine.
DR DrugBank; DB00977; Ethinylestradiol.
DR DrugBank; DB09288; Propacetamol.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB09100; Thyroid, porcine.
DR SwissLipids; SLP:000001693; -.
DR iPTMnet; P49888; -.
DR PhosphoSitePlus; P49888; -.
DR BioMuta; SULT1E1; -.
DR DMDM; 1711604; -.
DR EPD; P49888; -.
DR MassIVE; P49888; -.
DR PaxDb; P49888; -.
DR PeptideAtlas; P49888; -.
DR PRIDE; P49888; -.
DR ProteomicsDB; 56163; -.
DR Antibodypedia; 24249; 298 antibodies from 34 providers.
DR CPTC; P49888; 3 antibodies.
DR DNASU; 6783; -.
DR Ensembl; ENST00000226444.4; ENSP00000226444.3; ENSG00000109193.12.
DR GeneID; 6783; -.
DR KEGG; hsa:6783; -.
DR MANE-Select; ENST00000226444.4; ENSP00000226444.3; NM_005420.3; NP_005411.1.
DR CTD; 6783; -.
DR DisGeNET; 6783; -.
DR GeneCards; SULT1E1; -.
DR HGNC; HGNC:11377; SULT1E1.
DR HPA; ENSG00000109193; Tissue enhanced (intestine, liver, skin, vagina).
DR MIM; 600043; gene.
DR neXtProt; NX_P49888; -.
DR OpenTargets; ENSG00000109193; -.
DR PharmGKB; PA340; -.
DR VEuPathDB; HostDB:ENSG00000109193; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000162261; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; P49888; -.
DR OMA; VIKVIQF; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P49888; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.4; 2681.
DR PathwayCommons; P49888; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SABIO-RK; P49888; -.
DR SignaLink; P49888; -.
DR SIGNOR; P49888; -.
DR BioGRID-ORCS; 6783; 76 hits in 1076 CRISPR screens.
DR EvolutionaryTrace; P49888; -.
DR GeneWiki; SULT1E1; -.
DR GenomeRNAi; 6783; -.
DR Pharos; P49888; Tchem.
DR PRO; PR:P49888; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P49888; protein.
DR Bgee; ENSG00000109193; Expressed in penis and 107 other tissues.
DR ExpressionAtlas; P49888; baseline and differential.
DR Genevisible; P49888; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0004304; F:estrone sulfotransferase activity; TAS:ProtInc.
DR GO; GO:0047894; F:flavonol 3-sulfotransferase activity; IDA:BHF-UCL.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0050294; F:steroid sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
DR GO; GO:0006711; P:estrogen catabolic process; IDA:CAFA.
DR GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:CACAO.
DR GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc.
DR GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
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 3D-structure; Cytoplasm; Lipid metabolism; Lipid-binding;
KW Reference proteome; Steroid-binding; Transferase.
FT CHAIN 1..294
FT /note="Sulfotransferase 1E1"
FT /id="PRO_0000085153"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11006110"
FT BINDING 47..52
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 105..107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 129
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 137
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:11884392"
FT BINDING 192
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 226..231
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 256..258
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT VARIANT 22
FT /note="D -> Y (in dbSNP:rs11569705)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_018907"
FT MUTAGEN 85
FT /note="K->A: Does not have decreased sulfonation activity
FT towards the estrogens and DHEA."
FT /evidence="ECO:0000269|PubMed:11006110"
FT MUTAGEN 107
FT /note="H->A: Complete loss of sulfonation activity towards
FT all substrates tested."
FT /evidence="ECO:0000269|PubMed:11006110"
FT MUTAGEN 137
FT /note="S->A: Decreased gradually the sulfotransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:11884392"
FT MUTAGEN 137
FT /note="S->C: Decreased gradually the sulfotransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:11884392"
FT MUTAGEN 145
FT /note="V->E: Substrate specificity constants for estradiol
FT and estrone are reduced. Dramatic 400-fold increase in the
FT ability to sulfonate dopamine."
FT /evidence="ECO:0000269|PubMed:11006110"
FT MUTAGEN 269
FT /note="V->E: Does not prevent the formation of homodimer."
FT /evidence="ECO:0000269|PubMed:11884392"
FT CONFLICT 154
FT /note="F -> L (in Ref. 6; AAH27956)"
FT /evidence="ECO:0000305"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:1G3M"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1G3M"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:1G3M"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:1G3M"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1G3M"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1G3M"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:1G3M"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:1G3M"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:1G3M"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:1G3M"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1G3M"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1G3M"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1G3M"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:1G3M"
SQ 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
