ST1A1_HUMAN
ID ST1A1_HUMAN Reviewed; 295 AA.
AC P50225; Q2NL71; Q86U58; Q92818; Q9BVU6; Q9UGG7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Sulfotransferase 1A1;
DE Short=ST1A1;
DE EC=2.8.2.1 {ECO:0000269|PubMed:10199779, ECO:0000269|PubMed:12471039, ECO:0000269|PubMed:16221673, ECO:0000269|PubMed:21723874, ECO:0000269|PubMed:22069470, ECO:0000269|PubMed:7834621};
DE AltName: Full=Aryl sulfotransferase 1 {ECO:0000303|PubMed:8363592};
DE AltName: Full=HAST1/HAST2;
DE AltName: Full=Phenol sulfotransferase 1;
DE AltName: Full=Phenol-sulfating phenol sulfotransferase 1 {ECO:0000303|PubMed:8423770};
DE Short=P-PST 1 {ECO:0000303|PubMed:8423770};
DE AltName: Full=ST1A3;
DE AltName: Full=Thermostable phenol sulfotransferase;
DE Short=Ts-PST;
GN Name=SULT1A1; Synonyms=STP, STP1; ORFNames=OK/SW-cl.88;
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] (ISOFORM 1), AND VARIANT MET-223.
RC TISSUE=Brain;
RX PubMed=8363592; DOI=10.1006/bbrc.1993.2018;
RA Zhu X., Veronese M.E., Bernard C.C., Sansom L.N., McManus M.E.;
RT "Identification of two human brain aryl sulfotransferase cDNAs.";
RL Biochem. Biophys. Res. Commun. 195:120-127(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-223.
RC TISSUE=Liver;
RX PubMed=8484775; DOI=10.1006/bbrc.1993.1467;
RA Zhu X., Veronese M.E., Sansom L.N., McManus M.E.;
RT "Molecular characterisation of a human aryl sulfotransferase cDNA.";
RL Biochem. Biophys. Res. Commun. 192:671-676(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANTS MET-223 AND LYS-282.
RC TISSUE=Liver;
RX PubMed=8423770;
RA Wilborn T.W., Comer K.A., Dooley T.P., Reardon I.M., Heinrikson R.L.,
RA Falany C.N.;
RT "Sequence analysis and expression of the cDNA for the phenol-sulfating form
RT of human liver phenol sulfotransferase.";
RL Mol. Pharmacol. 43:70-77(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-223.
RX PubMed=8033246; DOI=10.1016/0009-2797(94)90057-4;
RA Yamazoe Y., Nagata K., Ozawa S., Kato R.;
RT "Structural similarity and diversity of sulfotransferases.";
RL Chem. Biol. Interact. 92:107-117(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-223.
RC TISSUE=Hippocampus;
RX PubMed=7864863; DOI=10.1006/bbrc.1995.1244;
RA Hwang S.-R., Kohn A.B., Hook V.Y.H.;
RT "Molecular cloning of an isoform of phenol sulfotransferase from human
RT brain hippocampus.";
RL Biochem. Biophys. Res. Commun. 207:701-707(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-223.
RC TISSUE=Blood;
RX PubMed=7695643; DOI=10.1006/bbrc.1995.1414;
RA Jones A.L., Hagen M., Coughtrie M.W.H., Roberts R.C., Glatt H.;
RT "Human platelet phenolsulfotransferases: cDNA cloning, stable expression in
RT V79 cells and identification of a novel allelic variant of the phenol-
RT sulfating form.";
RL Biochem. Biophys. Res. Commun. 208:855-862(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-223.
RC TISSUE=Liver;
RX PubMed=7581483; DOI=10.1097/00008571-199512001-00015;
RA Ozawa S., Nagata K., Shimada M., Ueda M., Tsuzuki T., Yamazoe Y., Kato R.;
RT "Primary structures and properties of two related forms of aryl
RT sulfotransferases in human liver.";
RL Pharmacogenetics 5:S135-S140(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT MET-223.
RX PubMed=8912648; DOI=10.1006/bbrc.1996.1628;
RA Dooley T.P., Huang Z.;
RT "Genomic organization and DNA sequences of two human phenol
RT sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16.";
RL Biochem. Biophys. Res. Commun. 228:134-140(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS MET-223 AND
RP LYS-282.
RX PubMed=8924211; DOI=10.1089/dna.1996.15.367;
RA Bernier F., Soucy P., Luu-The V.;
RT "Human phenol sulfotransferase gene contains two alternative promoters:
RT structure and expression of the gene.";
RL DNA Cell Biol. 15:367-375(1996).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-223.
RC TISSUE=Liver;
RX PubMed=9855620; DOI=10.1124/mol.54.6.942;
RA Dajani R., Hood A.M., Coughtrie M.W.;
RT "A single amino acid, Glu146, governs the substrate specificity of a human
RT dopamine sulfotransferase, SULT1A3.";
RL Mol. Pharmacol. 54:942-948(1998).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT MET-223.
RA Raftogianis R.B., Her C., Weinshilboum R.M.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-213 AND MET-223.
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-213.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [16]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-223.
RC TISSUE=Colon, and Placenta;
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 [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107 (ISOFORM 1).
RX PubMed=8288252; DOI=10.1006/geno.1993.1494;
RA Dooley T.P., Obermoeller R.D., Leiter E.H., Chapman H.D., Falany C.N.,
RA Deng Z., Siciliano M.J.;
RT "Mapping of the phenol sulfotransferase gene (STP) to human chromosome
RT 16p12.1-p11.2 and to mouse chromosome 7.";
RL Genomics 18:440-443(1993).
RN [18]
RP CHARACTERIZATION.
RX PubMed=8093002; DOI=10.1042/bj3020497;
RA Veronese M.E., Burgess W., Zhu X., McManus M.E.;
RT "Functional characterization of two human sulphotransferase cDNAs that
RT encode monoamine- and phenol-sulphating forms of phenol sulphotransferase:
RT substrate kinetics, thermal-stability and inhibitor-sensitivity studies.";
RL Biochem. J. 302:497-502(1994).
RN [19]
RP MUTAGENESIS OF CYS-70.
RX PubMed=8033270; DOI=10.1016/0009-2797(94)90053-1;
RA Falany C.N., Zhuang W., Falany J.L.;
RT "Characterization of expressed human phenol-sulfating phenol
RT sulfotransferase: effect of mutating cys70 on activity and
RT thermostability.";
RL Chem. Biol. Interact. 92:57-66(1994).
RN [20]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=7834621;
RA Chou H.C., Lang N.P., Kadlubar F.F.;
RT "Metabolic activation of N-hydroxy arylamines and N-hydroxy heterocyclic
RT amines by human sulfotransferase(s).";
RL Cancer Res. 55:525-529(1995).
RN [21]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10199779; DOI=10.1210/jcem.84.4.5590;
RA Kester M.H., Kaptein E., Roest T.J., van Dijk C.H., Tibboel D., Meinl W.,
RA Glatt H., Coughtrie M.W., Visser T.J.;
RT "Characterization of human iodothyronine sulfotransferases.";
RL J. Clin. Endocrinol. Metab. 84:1357-1364(1999).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
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 [25]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE (PAP) AND P-NITROPHENOL, CATALYTIC ACTIVITY,
RP AND FUNCTION.
RX PubMed=12471039; DOI=10.1074/jbc.m207246200;
RA Gamage N.U., Duggleby R.G., Barnett A.C., Tresillian M., Latham C.F.,
RA Liyou N.E., McManus M.E., Martin J.L.;
RT "Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and
RT kinetic implications of substrate inhibition.";
RL J. Biol. Chem. 278:7655-7662(2003).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE AND ESTRADIOL, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=16221673; DOI=10.1074/jbc.m508289200;
RA Gamage N.U., Tsvetanov S., Duggleby R.G., McManus M.E., Martin J.L.;
RT "The structure of human SULT1A1 crystallized with estradiol. An insight
RT into active site plasticity and substrate inhibition with multi-ring
RT substrates.";
RL J. Biol. Chem. 280:41482-41486(2005).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE.
RX PubMed=20417180; DOI=10.1016/j.bbrc.2010.04.109;
RA Lu J., Li H., Zhang J., Li M., Liu M.Y., An X., Liu M.C., Chang W.;
RT "Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate
RT inhibition and the role of Tyr149 in SULT1A2.";
RL Biochem. Biophys. Res. Commun. 396:429-434(2010).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE AND P-NITROPHENOL, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=21723874; DOI=10.1016/j.jmb.2011.06.037;
RA Alcolombri U., Elias M., Tawfik D.S.;
RT "Directed evolution of sulfotransferases and paraoxonases by ancestral
RT libraries.";
RL J. Mol. Biol. 411:837-853(2011).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE AND P-NITROPHENOL, CATALYTIC ACTIVITY,
RP FUNCTION, AND MUTAGENESIS OF ASP-249.
RX PubMed=22069470; DOI=10.1371/journal.pone.0026794;
RA Berger I., Guttman C., Amar D., Zarivach R., Aharoni A.;
RT "The molecular basis for the broad substrate specificity of human
RT sulfotransferase 1A1.";
RL PLoS ONE 6:E26794-E26794(2011).
RN [30]
RP VARIANTS GLN-37; HIS-213 AND MET-223.
RX PubMed=9345314; DOI=10.1006/bbrc.1997.7466;
RA Raftogianis R.B., Wood T.C., Otterness D.M., Van Loon J.A.,
RA Weinshilboum R.M.;
RT "Phenol sulfotransferase pharmacogenetics in humans: association of common
RT SULT1A1 alleles with TS PST phenotype.";
RL Biochem. Biophys. Res. Commun. 239:298-304(1997).
RN [31]
RP VARIANT HIS-213.
RX PubMed=10762004; DOI=10.1097/00008571-200003000-00008;
RA Engelke C.E., Meinl W., Boeing H., Glatt H.;
RT "Association between functional genetic polymorphisms of human
RT sulfotransferases 1A1 and 1A2.";
RL Pharmacogenetics 10:163-169(2000).
RN [32]
RP VARIANT [LARGE SCALE ANALYSIS] MET-223, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide
CC variety of acceptor molecules bearing a hydroxyl or an amine groupe.
CC Sulfonation increases the water solubility of most compounds, and
CC therefore their renal excretion, but it can also result in
CC bioactivation to form active metabolites. Displays broad substrate
CC specificity for small phenolic compounds. Plays an important role in
CC the sulfonation of endogenous molecules such as steroid hormones and
CC 3,3'-diiodothyronin (PubMed:16221673, PubMed:12471039, PubMed:22069470,
CC PubMed:21723874, PubMed:10199779, PubMed:7834621). Mediates the sulfate
CC conjugation of a variety of xenobiotics, including the drugs
CC acetaminophen and minoxidil (By similarity). Mediates also the
CC metabolic activation of carcinogenic N-hydroxyarylamines leading to
CC highly reactive intermediates capable of forming DNA adducts,
CC potentially resulting in mutagenesis (PubMed:7834621). May play a role
CC 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:0000250|UniProtKB:P17988,
CC ECO:0000269|PubMed:10199779, ECO:0000269|PubMed:12471039,
CC ECO:0000269|PubMed:16221673, ECO:0000269|PubMed:21723874,
CC ECO:0000269|PubMed:22069470, ECO:0000269|PubMed:35165440,
CC ECO:0000269|PubMed:7834621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC Evidence={ECO:0000269|PubMed:10199779, ECO:0000269|PubMed:12471039,
CC ECO:0000269|PubMed:16221673, ECO:0000269|PubMed:21723874,
CC ECO:0000269|PubMed:22069470, ECO:0000269|PubMed:7834621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:16221673};
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:16221673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC Evidence={ECO:0000305|PubMed:16221673};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 uM for 3,3'-diiodothyronin {ECO:0000269|PubMed:10199779};
CC Vmax=465 umol/min/mg enzyme with 3,3'-diiodothyronin as substrate
CC {ECO:0000269|PubMed:10199779};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12471039,
CC ECO:0000269|PubMed:16221673, ECO:0000269|PubMed:20417180}.
CC -!- INTERACTION:
CC P50225; O00204: SULT2B1; NbExp=7; IntAct=EBI-2814403, EBI-749441;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17988}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50225-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50225-2; Sequence=VSP_040101;
CC -!- TISSUE SPECIFICITY: Liver, lung, adrenal, brain, platelets and skin.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC allele SULT1A1*3. {ECO:0000305|PubMed:10762004,
CC ECO:0000305|PubMed:9345314}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; U09031; AAA18613.1; -; mRNA.
DR EMBL; L19955; AAA02935.1; -; mRNA.
DR EMBL; L10819; AAA35562.1; -; mRNA.
DR EMBL; L19999; AAA99892.1; -; mRNA.
DR EMBL; U26309; AAA67895.1; -; mRNA.
DR EMBL; X84654; CAA59147.1; -; mRNA.
DR EMBL; X78283; CAA55089.1; -; mRNA.
DR EMBL; U71086; AAB09597.1; -; Genomic_DNA.
DR EMBL; U54701; AAC50480.1; -; Genomic_DNA.
DR EMBL; AJ007418; CAA07495.1; -; mRNA.
DR EMBL; U52852; AAC51816.1; -; Genomic_DNA.
DR EMBL; AB062428; BAB93491.1; -; mRNA.
DR EMBL; BT007324; AAP35988.1; -; mRNA.
DR EMBL; CR608214; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC020765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000923; AAH00923.1; -; mRNA.
DR EMBL; BC110887; AAI10888.1; -; mRNA.
DR EMBL; L15346; AAA60595.1; -; Genomic_DNA.
DR CCDS; CCDS32420.1; -. [P50225-1]
DR PIR; I57945; I57945.
DR PIR; JC2523; JC2523.
DR PIR; JC5248; JC5248.
DR PIR; S52399; S52399.
DR PIR; S52794; S52794.
DR RefSeq; NP_001046.2; NM_001055.3. [P50225-1]
DR RefSeq; NP_803565.1; NM_177529.2. [P50225-1]
DR RefSeq; NP_803566.1; NM_177530.2. [P50225-1]
DR RefSeq; NP_803878.1; NM_177534.2. [P50225-1]
DR RefSeq; NP_803880.1; NM_177536.3. [P50225-2]
DR RefSeq; XP_016879095.1; XM_017023606.1.
DR RefSeq; XP_016879100.1; XM_017023611.1. [P50225-1]
DR RefSeq; XP_016879101.1; XM_017023612.1. [P50225-1]
DR RefSeq; XP_016879102.1; XM_017023613.1. [P50225-1]
DR PDB; 1LS6; X-ray; 1.90 A; A=1-295.
DR PDB; 1Z28; X-ray; 2.30 A; A=1-295.
DR PDB; 2D06; X-ray; 2.30 A; A/B=1-295.
DR PDB; 3QVU; X-ray; 2.50 A; A/B=1-295.
DR PDB; 3QVV; X-ray; 2.35 A; A/B=1-295.
DR PDB; 3U3J; X-ray; 2.70 A; A/B=1-294.
DR PDB; 3U3K; X-ray; 2.36 A; A/B=1-295.
DR PDB; 3U3M; X-ray; 2.30 A; A=1-295.
DR PDB; 3U3O; X-ray; 2.00 A; A=1-295.
DR PDB; 3U3R; X-ray; 2.36 A; A=1-295.
DR PDB; 4GRA; X-ray; 2.56 A; A/B=1-295.
DR PDBsum; 1LS6; -.
DR PDBsum; 1Z28; -.
DR PDBsum; 2D06; -.
DR PDBsum; 3QVU; -.
DR PDBsum; 3QVV; -.
DR PDBsum; 3U3J; -.
DR PDBsum; 3U3K; -.
DR PDBsum; 3U3M; -.
DR PDBsum; 3U3O; -.
DR PDBsum; 3U3R; -.
DR PDBsum; 4GRA; -.
DR AlphaFoldDB; P50225; -.
DR SMR; P50225; -.
DR BioGRID; 112686; 60.
DR IntAct; P50225; 11.
DR MINT; P50225; -.
DR STRING; 9606.ENSP00000378972; -.
DR BindingDB; P50225; -.
DR ChEMBL; CHEMBL1743291; -.
DR DrugBank; DB00316; Acetaminophen.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB04417; P-Nitrophenol.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB11077; Polyethylene glycol 400.
DR DrugBank; DB09288; Propacetamol.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB09100; Thyroid, porcine.
DR DrugBank; DB09070; Tibolone.
DR SwissLipids; SLP:000001651; -.
DR iPTMnet; P50225; -.
DR PhosphoSitePlus; P50225; -.
DR BioMuta; SULT1A1; -.
DR DMDM; 313104286; -.
DR OGP; P50225; -.
DR EPD; P50225; -.
DR jPOST; P50225; -.
DR MassIVE; P50225; -.
DR MaxQB; P50225; -.
DR PaxDb; P50225; -.
DR PeptideAtlas; P50225; -.
DR PRIDE; P50225; -.
DR ProteomicsDB; 56209; -. [P50225-1]
DR ProteomicsDB; 56210; -. [P50225-2]
DR Antibodypedia; 26492; 478 antibodies from 32 providers.
DR DNASU; 6817; -.
DR Ensembl; ENST00000314752.12; ENSP00000321988.7; ENSG00000196502.13. [P50225-1]
DR Ensembl; ENST00000350842.8; ENSP00000329399.4; ENSG00000196502.13. [P50225-2]
DR Ensembl; ENST00000569554.5; ENSP00000457912.1; ENSG00000196502.13. [P50225-1]
DR GeneID; 6817; -.
DR KEGG; hsa:6817; -.
DR MANE-Select; ENST00000314752.12; ENSP00000321988.7; NM_001055.4; NP_001046.2.
DR UCSC; uc002dqi.4; human. [P50225-1]
DR CTD; 6817; -.
DR DisGeNET; 6817; -.
DR GeneCards; SULT1A1; -.
DR HGNC; HGNC:11453; SULT1A1.
DR HPA; ENSG00000196502; Tissue enhanced (intestine, liver).
DR MIM; 171150; gene.
DR neXtProt; NX_P50225; -.
DR OpenTargets; ENSG00000196502; -.
DR PharmGKB; PA343; -.
DR VEuPathDB; HostDB:ENSG00000196502; -.
DR VEuPathDB; HostDB:ENSG00000288656; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000163450; -.
DR HOGENOM; CLU_027239_6_1_1; -.
DR InParanoid; P50225; -.
DR OMA; WHFANRA; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P50225; -.
DR TreeFam; TF321745; -.
DR BioCyc; MetaCyc:HS09898-MON; -.
DR BRENDA; 2.8.2.1; 2681.
DR BRENDA; 2.8.2.2; 2681.
DR PathwayCommons; P50225; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SABIO-RK; P50225; -.
DR SignaLink; P50225; -.
DR BioGRID-ORCS; 6817; 11 hits in 1013 CRISPR screens.
DR ChiTaRS; SULT1A1; human.
DR EvolutionaryTrace; P50225; -.
DR GeneWiki; SULT1A1; -.
DR GenomeRNAi; 6817; -.
DR Pharos; P50225; Tchem.
DR PRO; PR:P50225; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P50225; protein.
DR Bgee; ENSG00000196502; Expressed in mucosa of transverse colon and 114 other tissues.
DR ExpressionAtlas; P50225; baseline and differential.
DR Genevisible; P50225; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:UniProtKB.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0047894; F:flavonol 3-sulfotransferase activity; IDA:BHF-UCL.
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:UniProtKB.
DR GO; GO:0009308; P:amine metabolic process; TAS:ProtInc.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
DR GO; GO:0009812; P:flavonoid metabolic process; IDA:BHF-UCL.
DR GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
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; Alternative splicing; Catecholamine metabolism; Cytoplasm;
KW Direct protein sequencing; Lipid metabolism; Phosphoprotein;
KW Reference proteome; Steroid metabolism; Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1A1"
FT /id="PRO_0000085127"
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:0000269|PubMed:12471039,
FT ECO:0000269|PubMed:16221673"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12471039,
FT ECO:0000269|PubMed:16221673"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:12471039,
FT ECO:0000269|PubMed:16221673"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:12471039,
FT ECO:0000269|PubMed:16221673"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:12471039,
FT ECO:0000269|PubMed:16221673"
FT BINDING 227..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:12471039,
FT ECO:0000269|PubMed:16221673"
FT BINDING 255..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:12471039,
FT ECO:0000269|PubMed:16221673"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17988"
FT VAR_SEQ 1..124
FT /note="MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTT
FT WVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKAPGIPSGMETLKDTPAPRLLKTHLPL
FT ALLPQTLLDQKVK -> MLAKLLCDQVVGAPIAVSAFYAGMSILQGKDDIFLDLKQKFW
FT NTYM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.14"
FT /id="VSP_040101"
FT VARIANT 37
FT /note="R -> Q (in dbSNP:rs72547527)"
FT /evidence="ECO:0000269|PubMed:9345314"
FT /id="VAR_009302"
FT VARIANT 151
FT /note="E -> D (in dbSNP:rs1042014)"
FT /id="VAR_028721"
FT VARIANT 151
FT /note="E -> Q (in dbSNP:rs1042011)"
FT /id="VAR_057339"
FT VARIANT 213
FT /note="R -> H (in allele SULT1A1*2; has a lower
FT sulfotransferase activity; dbSNP:rs1042028)"
FT /evidence="ECO:0000269|PubMed:10762004,
FT ECO:0000269|PubMed:9345314, ECO:0000269|Ref.12,
FT ECO:0000269|Ref.13"
FT /id="VAR_007425"
FT VARIANT 223
FT /note="V -> M (in dbSNP:rs1801030)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7581483, ECO:0000269|PubMed:7695643,
FT ECO:0000269|PubMed:7864863, ECO:0000269|PubMed:8033246,
FT ECO:0000269|PubMed:8363592, ECO:0000269|PubMed:8423770,
FT ECO:0000269|PubMed:8484775, ECO:0000269|PubMed:8912648,
FT ECO:0000269|PubMed:8924211, ECO:0000269|PubMed:9345314,
FT ECO:0000269|PubMed:9855620, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.12, ECO:0007744|PubMed:21269460"
FT /id="VAR_009303"
FT VARIANT 235
FT /note="N -> T (in dbSNP:rs35728980)"
FT /id="VAR_014889"
FT VARIANT 282
FT /note="E -> K (in dbSNP:rs36043491)"
FT /evidence="ECO:0000269|PubMed:8423770,
FT ECO:0000269|PubMed:8924211"
FT /id="VAR_061886"
FT MUTAGEN 70
FT /note="C->S: Increased sensitivity of enzyme activity to
FT heat inactivation."
FT /evidence="ECO:0000269|PubMed:8033270"
FT MUTAGEN 249
FT /note="D->G: Increased activity towards p-nitrophenol."
FT /evidence="ECO:0000269|PubMed:22069470"
FT CONFLICT 90
FT /note="P -> L (in Ref. 3; AAA67895)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> T (in Ref. 5; CAA59147)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="E -> G (in Ref. 5; CAA59147)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="V -> A (in Ref. 3; AAA67895)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> T (in Ref. 3; AAA99892 and 9; AAC50480)"
FT /evidence="ECO:0000305"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1LS6"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:1LS6"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:1LS6"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1LS6"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4GRA"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:1LS6"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1LS6"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:1LS6"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1LS6"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1LS6"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:1LS6"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1LS6"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1LS6"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:1LS6"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1LS6"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1LS6"
SQ SEQUENCE 295 AA; 34165 MW; 7D4362A603A29176 CRC64;
MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG TTWVSQILDM
IYQGGDLEKC HRAPIFMRVP FLEFKAPGIP SGMETLKDTP APRLLKTHLP LALLPQTLLD
QKVKVVYVAR NAKDVAVSYY HFYHMAKVHP EPGTWDSFLE KFMVGEVSYG SWYQHVQEWW
ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETV DFVVQHTSFK EMKKNPMTNY
TTVPQEFMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL
