Overview
| Uniprot ID | P0DMN0 |
| Protein Name | Sulfotransferase 1A4 |
| Gene Name | SULT1A4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 106 |
TPPPRLIKSHLPLAL |
| 124 |
TLLDQKVKVVYVARN |
Function
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, (R)-adrenaline/epinephrine, (R)-noradrenaline/norepinephrine and serotonin) and phenolic and catechol drugs (PubMed:15358107, PubMed:29524394). Catalyzes the sulfation of T4 (L-thyroxine/3,5,3',5'-tetraiodothyronine), T3 (3,5,3'-triiodothyronine), rT3 (3,3',5'-triiodothyronine) and 3,3'-T2 (3,3'-diiodothyronine), with a substrate preference of 3,3'-T2 > rT3 > T3 > T4 (PubMed:10199779)
Protein Sequence
10
MELIQDTSRP
20
PLEYVKGVPL
30
IKYFAEALGP
40
LQSFQARPDD
50
LLINTYPKSG
60
TTWVSQILDM
70
IYQGGDLEKC
80
NRAPIYVRVP
90
FLEVNDPGEP
100
SGLETLKDTP
110
PPRLIKSHLP
120
LALLPQTLLD
130
QKVKVVYVAR
140
NPKDVAVSYY
150
HFHRMEKAHP
160
EPGTWDSFLE
170
KFMAGEVSYG
180
SWYQHVQEWW
190
ELSRTHPVLY
200
LFYEDMKENP
210
KREIQKILEF
220
VGRSLPEETM
230
DFMVQHTSFK
240
EMKKNPMTNY
250
TTVPQELMDH
260
SISPFMRKGM
270
AGDWKTTFTV
280
AQNERFDADY
290
AEKMAGCSLS
FRSEL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Molecular Function |
GO:0004062 |
aryl sulfotransferase activity |
| Molecular Function |
GO:0008146 |
sulfotransferase activity |
| Biological Process |
GO:0042417 |
dopamine metabolic process |
| Biological Process |
GO:0042414 |
epinephrine metabolic process |
| Biological Process |
GO:0042415 |
norepinephrine metabolic process |
| Biological Process |
GO:0042428 |
serotonin metabolic process |
| Biological Process |
GO:0008202 |
steroid metabolic process |
| Biological Process |
GO:0051923 |
sulfation |
| Biological Process |
GO:0042403 |
thyroid hormone metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.