ST1A3_HUMAN
ID ST1A3_HUMAN Reviewed; 295 AA.
AC P0DMM9; B4DNV0; O95603; P50224; Q1ET66; Q6ZWJ5;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Sulfotransferase 1A3;
DE Short=ST1A3;
DE EC=2.8.2.1 {ECO:0000269|PubMed:8093002};
DE AltName: Full=Aryl sulfotransferase 1A3/1A4;
DE AltName: Full=Catecholamine-sulfating phenol sulfotransferase;
DE AltName: Full=HAST3;
DE AltName: Full=M-PST;
DE AltName: Full=Monoamine-sulfating phenol sulfotransferase;
DE AltName: Full=Placental estrogen sulfotransferase;
DE AltName: Full=Sulfotransferase 1A3/1A4;
DE AltName: Full=Sulfotransferase, monoamine-preferring;
DE AltName: Full=Thermolabile phenol sulfotransferase;
DE Short=TL-PST;
GN Name=SULT1A3; Synonyms=STM;
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).
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).
RC TISSUE=Placenta;
RX PubMed=8187949; DOI=10.1016/0303-7207(94)90159-7;
RA Bernier F., Lopez-Solache I., Labrie F., Luu-The V.;
RT "Cloning and expression of cDNA encoding human placental estrogen
RT sulfotransferase.";
RL Mol. Cell. Endocrinol. 99:R11-R15(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7802665; DOI=10.1006/bbrc.1994.2810;
RA Dooley T.P., Probst P., Munroe P.B., Mole S.E., Liu Z., Doggett N.A.;
RT "Genomic organization and DNA sequence of the human catecholamine-sulfating
RT phenol sulfotransferase gene (STM).";
RL Biochem. Biophys. Res. Commun. 205:1325-1332(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 84-101, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8117269; DOI=10.1006/bbrc.1994.1159;
RA Wood T.C., Aksoy I.A., Aksoy S., Weinshilboum R.M.;
RT "Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression
RT and characterization.";
RL Biochem. Biophys. Res. Commun. 198:1119-1127(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=7695637; DOI=10.1006/bbrc.1995.1406;
RA Aksoy I.A., Weinshilboum R.M.;
RT "Human thermolabile phenol sulfotransferase gene (STM): molecular cloning
RT and structural characterization.";
RL Biochem. Biophys. Res. Commun. 208:786-795(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Leukocyte;
RX PubMed=7961757; DOI=10.1016/s0021-9258(18)46914-1;
RA Bernier F., Leblanc G., Labrie F., Luu-The V.;
RT "Structure of human estrogen and aryl sulfotransferase gene. Two mRNA
RT species issued from a single gene.";
RL J. Biol. Chem. 269:28200-28205(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Gaedigk A., Grant D.M.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
RA Terazawa R., Shimada M., Nagata K., Yamazoe Y.;
RT "Isolation of seven variants of catecholamine sulfotransferase cDNAs from
RT human kidney.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
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 [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Pancreas;
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 [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-198.
RC TISSUE=Lymphocyte;
RX PubMed=7829089; DOI=10.1006/geno.1994.1494;
RA Aksoy I.A., Callen D.F., Apostolou S., Her C., Weinshilboum R.M.;
RT "Thermolabile phenol sulfotransferase gene (STM): localization to human
RT chromosome 16p11.2.";
RL Genomics 23:275-277(1994).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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 [15]
RP IDENTIFICATION BY MASS 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).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC TISSUE=Brain;
RX PubMed=10543947; DOI=10.1006/jmbi.1999.3153;
RA Bidwell L.M., McManus M.E., Gaedigk A., Kakuta Y., Negishi M., Pedersen L.,
RA Martin J.L.;
RT "Crystal structure of human catecholamine sulfotransferase.";
RL J. Mol. Biol. 293:521-530(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE AND L-DOPAMINE.
RX PubMed=16083857; DOI=10.1016/j.bbrc.2005.07.091;
RA Lu J.H., Li H.T., Liu M.C., Zhang J.P., Li M., An X.M., Chang W.R.;
RT "Crystal structure of human sulfotransferase SULT1A3 in complex with
RT dopamine and 3'-phosphoadenosine 5'-phosphate.";
RL Biochem. Biophys. Res. Commun. 335:417-423(2005).
RN [18]
RP VARIANT ASN-234, AND CHARACTERIZATION OF VARIANT ASN-234.
RX PubMed=14622112; DOI=10.1046/j.1471-4159.2003.02027.x;
RA Thomae B.A., Rifki O.F., Theobald M.A., Eckloff B.W., Wieben E.D.,
RA Weinshilboum R.M.;
RT "Human catecholamine sulfotransferase (SULT1A3) pharmacogenetics:
RT functional genetic polymorphism.";
RL J. Neurochem. 87:809-819(2003).
RN [19]
RP VARIANTS LEU-101; HIS-101 AND CYS-144, FUNCTION, AND CHARACTERIZATION OF
RP VARIANTS LEU-101; HIS-101 AND CYS-144.
RX PubMed=15358107; DOI=10.1016/j.bbrc.2004.07.038;
RA Hildebrandt M.A.T., Salavaggione O.E., Martin Y.N., Flynn H.C., Jalal S.,
RA Wieben E.D., Weinshilboum R.M.;
RT "Human SULT1A3 pharmacogenetics: gene duplication and functional genomic
RT studies.";
RL Biochem. Biophys. Res. Commun. 321:870-878(2004).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC phenolic monoamines (neurotransmitters such as dopamine, norepinephrine
CC and serotonin) and phenolic and catechol drugs.
CC {ECO:0000269|PubMed:15358107, ECO:0000269|PubMed:8093002}.
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:8093002};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16083857}.
CC -!- INTERACTION:
CC P0DMM9; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-10196922, EBI-742808;
CC P0DMM9; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-10196922, EBI-740897;
CC P0DMM9; P34896: SHMT1; NbExp=3; IntAct=EBI-10196922, EBI-715117;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8093002}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P0DMM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DMM9-2; Sequence=VSP_012326;
CC Name=3;
CC IsoId=P0DMM9-3; Sequence=VSP_047771;
CC -!- TISSUE SPECIFICITY: Liver, colon, kidney, lung, brain, spleen, small
CC intestine, placenta and leukocyte. {ECO:0000269|PubMed:8117269}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- CAUTION: Found in a segmental duplication on p arm of chromosome 16
CC giving rise to two identical copies of this gene sharing exons with
CC SLX1A and SLX1B. The ORFs of SULT1A3 and SULT1A4 differ with only a
CC single nucleotide change that does not alter the encoded amino acid. It
CC is not possible to determine whether any individual polymorphism is
CC present within SULT1A3 or SULT1A4 (PubMed:15358107).
CC {ECO:0000305|PubMed:15358107}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=BAC85507.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L19956; AAA02943.1; -; mRNA.
DR EMBL; L25275; AAA36523.1; -; mRNA.
DR EMBL; L19956; AAA17723.1; -; mRNA.
DR EMBL; U20499; AAA64490.1; -; Genomic_DNA.
DR EMBL; X84653; CAA59146.1; -; mRNA.
DR EMBL; L34160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U37686; AAA86536.1; -; Genomic_DNA.
DR EMBL; U34199; AAC99987.1; -; mRNA.
DR EMBL; AK122733; BAC85507.1; ALT_FRAME; mRNA.
DR EMBL; AK298073; BAG60362.1; -; mRNA.
DR EMBL; AC106782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB111094; BAE94928.1; -; mRNA.
DR EMBL; BC014471; AAH14471.1; -; mRNA.
DR EMBL; BC078144; AAH78144.1; -; mRNA.
DR EMBL; U08099; AAA82126.1; -; Genomic_DNA.
DR CCDS; CCDS10674.1; -. [P0DMM9-1]
DR CCDS; CCDS32427.1; -. [P0DMM9-1]
DR PIR; A55451; A55451.
DR RefSeq; NP_001017390.1; NM_001017390.2. [P0DMM9-1]
DR RefSeq; NP_808220.1; NM_177552.3. [P0DMM9-1]
DR RefSeq; XP_011506903.1; XM_011508601.1.
DR RefSeq; XP_016855108.1; XM_016999619.1.
DR PDB; 1CJM; X-ray; 2.40 A; A=1-295.
DR PDB; 2A3R; X-ray; 2.60 A; A/B=1-295.
DR PDBsum; 1CJM; -.
DR PDBsum; 2A3R; -.
DR AlphaFoldDB; P0DMM9; -.
DR SMR; P0DMM9; -.
DR BioGRID; 112687; 24.
DR BioGRID; 138644; 5.
DR IntAct; P0DMM9; 4.
DR STRING; 9606.ENSP00000353600; -.
DR ChEMBL; CHEMBL1743293; -.
DR DrugBank; DB00316; Acetaminophen.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB00977; Ethinylestradiol.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00388; Phenylephrine.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB09288; Propacetamol.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB09100; Thyroid, porcine.
DR GlyGen; P0DMM9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0DMM9; -.
DR PhosphoSitePlus; P0DMM9; -.
DR BioMuta; SULT1A3; -.
DR jPOST; P0DMM9; -.
DR MassIVE; P0DMM9; -.
DR PaxDb; P0DMM9; -.
DR PeptideAtlas; P0DMM9; -.
DR PRIDE; P0DMM9; -.
DR TopDownProteomics; P0DMM9-2; -. [P0DMM9-2]
DR Antibodypedia; 57796; 254 antibodies from 21 providers.
DR DNASU; 6818; -.
DR Ensembl; ENST00000338971.10; ENSP00000343645.6; ENSG00000261052.6. [P0DMM9-1]
DR Ensembl; ENST00000395138.6; ENSP00000378570.2; ENSG00000261052.6. [P0DMM9-1]
DR Ensembl; ENST00000563322.5; ENSP00000454518.1; ENSG00000261052.6. [P0DMM9-3]
DR GeneID; 445329; -.
DR GeneID; 6818; -.
DR KEGG; hsa:445329; -.
DR KEGG; hsa:6818; -.
DR MANE-Select; ENST00000338971.10; ENSP00000343645.6; NM_177552.4; NP_808220.1.
DR MANE-Select; ENST00000360423.12; ENSP00000353600.8; NM_001017390.3; NP_001017390.1.
DR UCSC; uc010bzt.4; human. [P0DMM9-1]
DR CTD; 445329; -.
DR CTD; 6818; -.
DR DisGeNET; 445329; -.
DR DisGeNET; 6818; -.
DR GeneCards; SULT1A3; -.
DR HGNC; HGNC:11455; SULT1A3.
DR HPA; ENSG00000261052; Tissue enhanced (intestine).
DR MIM; 600641; gene.
DR neXtProt; NX_P0DMM9; -.
DR OpenTargets; ENSG00000261052; -.
DR VEuPathDB; HostDB:ENSG00000261052; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000164316; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR PhylomeDB; P0DMM9; -.
DR BioCyc; MetaCyc:HS05608-MON; -.
DR BRENDA; 2.8.2.1; 2681.
DR PathwayCommons; P0DMM9; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SignaLink; P0DMM9; -.
DR BioGRID-ORCS; 445329; 18 hits in 583 CRISPR screens.
DR BioGRID-ORCS; 6818; 19 hits in 276 CRISPR screens.
DR Pharos; P0DMM9; Tbio.
DR PRO; PR:P0DMM9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P0DMM9; protein.
DR Bgee; ENSG00000261052; Expressed in duodenum and 91 other tissues.
DR ExpressionAtlas; P0DMM9; baseline and differential.
DR Genevisible; P0DMM9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0047685; F:amine sulfotransferase activity; IDA:CAFA.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IMP:CACAO.
DR GO; GO:0043199; F:sulfate binding; IDA:CAFA.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:BHF-UCL.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IDA:CAFA.
DR GO; GO:1903351; P:cellular response to dopamine; IMP:CAFA.
DR GO; GO:0042420; P:dopamine catabolic process; IDA:CAFA.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IDA:CAFA.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:CAFA.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
DR GO; GO:0009812; P:flavonoid metabolic process; IDA:BHF-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:CAFA.
DR GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; IDA:CAFA.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:BHF-UCL.
DR DisProt; DP00011; -.
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; Reference proteome;
KW Steroid metabolism; Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1A3"
FT /id="PRO_0000085159"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49888"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 227..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT BINDING 257..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:16083857,
FT ECO:0007744|PDB:2A3R"
FT VAR_SEQ 167..295
FT /note="VSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEE
FT TMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFD
FT ADYAEKMAGCSLSFRSEL -> GGLDWRKEGVKPRGGGYNVQQPCVGAPCPLL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012326"
FT VAR_SEQ 198
FT /note="E -> EEPSAAQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_047771"
FT VARIANT 101
FT /note="P -> H (decreases levels of sulfotransferase
FT activity; dbSNP:rs751527244)"
FT /evidence="ECO:0000269|PubMed:15358107"
FT /id="VAR_071108"
FT VARIANT 101
FT /note="P -> L (decreases levels of sulfotransferase
FT activity; dbSNP:rs751527244)"
FT /evidence="ECO:0000269|PubMed:15358107"
FT /id="VAR_071109"
FT VARIANT 144
FT /note="R -> C (no effect on sulfotransferase activity;
FT dbSNP:rs1293732453)"
FT /evidence="ECO:0000269|PubMed:15358107"
FT /id="VAR_071110"
FT VARIANT 234
FT /note="K -> N (decreases levels of sulfotransferase
FT activity; accelerates proteasome-dependent degradation;
FT dbSNP:rs1328799050)"
FT /evidence="ECO:0000269|PubMed:14622112"
FT /id="VAR_071111"
FT CONFLICT 220..225
FT /note="MDFMVQ -> VDLMVE (in Ref. 8; AAC99987)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="N -> T (in Ref. 8; AAC99987)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..245
FT /note="PQ -> RR (in Ref. 8; AAC99987)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> T (in Ref. 8; AAC99987)"
FT /evidence="ECO:0000305"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1CJM"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1CJM"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:1CJM"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2A3R"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2A3R"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2A3R"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:1CJM"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:1CJM"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1CJM"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1CJM"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:2A3R"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:2A3R"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2A3R"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2A3R"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:2A3R"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1CJM"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1CJM"
SQ SEQUENCE 295 AA; 34196 MW; ECDDEC03DBE30D46 CRC64;
MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLINTYPKSG TTWVSQILDM
IYQGGDLEKC NRAPIYVRVP FLEVNDPGEP SGLETLKDTP PPRLIKSHLP LALLPQTLLD
QKVKVVYVAR NPKDVAVSYY HFHRMEKAHP EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW
ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETM DFMVQHTSFK EMKKNPMTNY
TTVPQELMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL
