SULT1A3

Sulfotransferase 1A3/1A4 is an enzyme that in humans is encoded by the SULT1A3 gene.[3][4][5]

SULT1A3
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1CJM, 2A3R,%%s1CJM
Identifiers
Aliases	SULT1A3, HAST, HAST3, M-PST, ST1A3/ST1A4, ST1A5, STM, TL-PST, ST1A3, sulfotransferase family 1A member 3, ST1A4
External IDs	OMIM: 600641 HomoloGene: 133085 GeneCards: SULT1A3
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p11.2 Start 30,199,228 bp[1] End 30,204,310 bp[1]
Gene ontology Molecular function • transferase activity • sulfotransferase activity • GO:0001948 protein binding • aryl sulfotransferase activity • sulfate binding • amine sulfotransferase activity Cellular component • cytoplasm • cytosol Biological process • steroid metabolic process • IRE1-mediated unfolded protein response • catecholamine metabolic process • sulfation • lipid metabolism • flavonoid metabolic process • xenobiotic metabolic process • ethanol catabolic process • dopamine receptor signaling pathway • dopamine catabolic process • 3'-phosphoadenosine 5'-phosphosulfate metabolic process • ERK1 and ERK2 cascade • calcineurin-mediated signaling • NMDA selective glutamate receptor signaling pathway • negative regulation of neuron death • cellular response to dopamine Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6818	n/a
Ensembl	ENSG00000261052	n/a
UniProt	P0DMM9 P0DMN0	n/a
RefSeq (mRNA)	NM_001017387 NM_003166 NM_177552	n/a
RefSeq (protein)	NP_808220 NP_001017390 NP_001017390.1 NP_808220.1 NP_001017390	n/a
Location (UCSC)	Chr 16: 30.2 – 30.2 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes a phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16; this gene and SULT1A4 arose from a segmental duplication. This gene is the most centromeric of the four sulfotransferase genes. Exons of this gene overlap with exons of a gene that encodes a protein containing GIY-YIG domains (GIYD1). Three alternatively spliced variants that encode the same protein have been described.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000261052 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Wood TC, Aksoy IA, Aksoy S, Weinshilboum RM (Mar 1994). "Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization". Biochem Biophys Res Commun. 198 (3): 1119–27. doi:10.1006/bbrc.1994.1159. PMID 8117269.
4. Aksoy IA, Callen DF, Apostolou S, Her C, Weinshilboum RM (Feb 1995). "Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2". Genomics. 23 (1): 275–7. doi:10.1006/geno.1994.1494. PMID 7829089.
5. "Entrez Gene: SULT1A3 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3".

Further reading

• Weinshilboum RM, Otterness DM, Aksoy IA, et al. (1997). "Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes". FASEB J. 11 (1): 3–14. doi:10.1096/fasebj.11.1.9034160. PMID 9034160.
• Glatt H, Engelke CE, Pabel U, et al. (2000). "Sulfotransferases: genetics and role in toxicology". Toxicol. Lett. 112–113: 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID 10720750.
• Glatt H (2001). "Sulfotransferases in the bioactivation of xenobiotics". Chem. Biol. Interact. 129 (1–2): 141–70. doi:10.1016/S0009-2797(00)00202-7. PMID 11154739.
• Glatt H, Boeing H, Engelke CE, et al. (2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutat. Res. 482 (1–2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID 11535246.
• Aksoy IA, Weinshilboum RM (1995). "Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization". Biochem. Biophys. Res. Commun. 208 (2): 786–95. doi:10.1006/bbrc.1995.1406. PMID 7695637.
• Jones AL, Hagen M, Coughtrie MW, et al. (1995). "Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form". Biochem. Biophys. Res. Commun. 208 (2): 855–62. doi:10.1006/bbrc.1995.1414. PMID 7695643.
• Dooley TP, Probst P, Munroe PB, et al. (1995). "Genomic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM)". Biochem. Biophys. Res. Commun. 205 (2): 1325–32. doi:10.1006/bbrc.1994.2810. PMID 7802665.
• Bernier F, Leblanc G, Labrie F, Luu-The V (1994). "Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene". J. Biol. Chem. 269 (45): 28200–5. PMID 7961757.
• Veronese ME, Burgess W, Zhu X, McManus ME (1994). "Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies". Biochem. J. 302 (Pt 2): 497–502. doi:10.1042/bj3020497. PMC 1137255. PMID 8093002.
• Bernier F, Lopez Solache I, Labrie F, Luu-The V (1994). "Cloning and expression of cDNA encoding human placental estrogen sulfotransferase". Mol. Cell. Endocrinol. 99 (1): R11–5. doi:10.1016/0303-7207(94)90159-7. PMID 8187949.
• Zhu X, Veronese ME, Bernard CC, et al. (1993). "Identification of two human brain aryl sulfotransferase cDNAs". Biochem. Biophys. Res. Commun. 195 (1): 120–7. doi:10.1006/bbrc.1993.2018. PMID 8363592.
• Her C, Raftogianis R, Weinshilboum RM (1996). "Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization". Genomics. 33 (3): 409–20. doi:10.1006/geno.1996.0216. PMID 8661000.
• Dooley TP, Huang Z (1996). "Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16". Biochem. Biophys. Res. Commun. 228 (1): 134–40. doi:10.1006/bbrc.1996.1628. PMID 8912648.
• Dajani R, Sharp S, Graham S, et al. (1999). "Kinetic properties of human dopamine sulfotransferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: comparison with the recombinant enzyme purified from Escherichia coli". Protein Expr. Purif. 16 (1): 11–8. doi:10.1006/prep.1999.1030. PMID 10336855.
• Bidwell LM, McManus ME, Gaedigk A, et al. (1999). "Crystal structure of human catecholamine sulfotransferase". J. Mol. Biol. 293 (3): 521–30. doi:10.1006/jmbi.1999.3153. PMID 10543947.
• Dajani R, Cleasby A, Neu M, et al. (2000). "X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity". J. Biol. Chem. 274 (53): 37862–8. doi:10.1074/jbc.274.53.37862. PMID 10608851.
• Harris RM, Waring RH, Kirk CJ, Hughes PJ (2000). "Sulfation of "estrogenic" alkylphenols and 17beta-estradiol by human platelet phenol sulfotransferases". J. Biol. Chem. 275 (1): 159–66. doi:10.1074/jbc.275.1.159. PMID 10617600.

External links

• Overview of all the structural information available in the PDB for UniProt: P0DMM9 (Sulfotransferase 1A3) at the PDBe-KB.