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Protein

Sulfotransferase 1A1

Gene

Sult1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.

Catalytic activityi

3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton acceptorBy similarity
Binding sitei126 – 1261PAPSBy similarity
Binding sitei134 – 1341PAPSBy similarity
Binding sitei189 – 1891PAPSBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 496PAPSBy similarity
Nucleotide bindingi223 – 2286PAPSBy similarity
Nucleotide bindingi251 – 2555PAPSBy similarity

GO - Molecular functioni

  1. 3'-phosphoadenosine 5'-phosphosulfate binding Source: RGD
  2. aryl sulfotransferase activity Source: RGD
  3. protein homodimerization activity Source: RGD
  4. sulfotransferase activity Source: RGD

GO - Biological processi

  1. 4-nitrophenol metabolic process Source: RGD
  2. catecholamine metabolic process Source: RGD
  3. drug metabolic process Source: RGD
  4. estrogen metabolic process Source: RGD
  5. regulation of blood pressure Source: RGD
  6. response to activity Source: RGD
  7. response to glucocorticoid Source: RGD
  8. response to insecticide Source: RGD
  9. sulfation Source: RGD
  10. xenobiotic metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BRENDAi2.8.2.1. 5301.
ReactomeiREACT_341577. Cytosolic sulfonation of small molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfotransferase 1A1 (EC:2.8.2.1)
Short name:
ST1A1
Alternative name(s):
Aryl sulfotransferase
Aryl sulfotransferase IV
Short name:
ASTIV
Minoxidil sulfotransferase
Short name:
Mx-ST
PST-1
Phenol sulfotransferase
Sulfokinase
Tyrosine-ester sulfotransferase
Gene namesi
Name:Sult1a1
Synonyms:St1a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3767. Sult1a1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Sulfotransferase 1A1PRO_0000085131Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PaxDbiP17988.
PRIDEiP17988.

Expressioni

Tissue specificityi

Liver, kidney, heart and colon.

Inductioni

Induced by androgens and suppressed by estrogens. The expression is under the influence of pituitary growth hormone and thyroid hormone.

Gene expression databases

GenevestigatoriP17988.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-4563534.
STRINGi10116.ENSRNOP00000026186.

Structurei

3D structure databases

ProteinModelPortaliP17988.
SMRiP17988. Positions 4-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni102 – 1043Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiNOG260792.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiP17988.
KOiK01014.
OMAiKEWWELR.
OrthoDBiEOG7V49ZK.
PhylomeDBiP17988.
TreeFamiTF321745.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P17988-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFSRPPLVH VKGIPLIKYF AETIGPLQNF TAWPDDLLIS TYPKSGTTWM
60 70 80 90 100
SEILDMIYQG GKLEKCGRAP IYARVPFLEF KCPGVPSGLE TLEETPAPRL
110 120 130 140 150
LKTHLPLSLL PQSLLDQKVK VIYIARNAKD VVVSYYNFYN MAKLHPDPGT
160 170 180 190 200
WDSFLENFMD GEVSYGSWYQ HVKEWWELRH THPVLYLFYE DIKENPKREI
210 220 230 240 250
KKILEFLGRS LPEETVDSIV HHTSFKKMKE NCMTNYTTIP TEIMDHNVSP
260 270 280 290
FMRKGTTGDW KNTFTVAQNE RFDAHYAKTM TDCDFKFRCE L
Length:291
Mass (Da):33,906
Last modified:November 1, 1990 - v1
Checksum:i9EC66C72923DB872
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52883 mRNA. Translation: CAA37065.1.
L19998 mRNA. Translation: AAA41644.1.
L16241 Genomic DNA. No translation available.
AF394783 mRNA. Translation: AAK77559.1.
X68640 mRNA. Translation: CAA48604.1.
PIRiS10329.
RefSeqiNP_114022.1. NM_031834.1.
UniGeneiRn.1507.

Genome annotation databases

EnsembliENSRNOT00000026186; ENSRNOP00000026186; ENSRNOG00000019342.
GeneIDi83783.
KEGGirno:83783.
UCSCiRGD:3767. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52883 mRNA. Translation: CAA37065.1.
L19998 mRNA. Translation: AAA41644.1.
L16241 Genomic DNA. No translation available.
AF394783 mRNA. Translation: AAK77559.1.
X68640 mRNA. Translation: CAA48604.1.
PIRiS10329.
RefSeqiNP_114022.1. NM_031834.1.
UniGeneiRn.1507.

3D structure databases

ProteinModelPortaliP17988.
SMRiP17988. Positions 4-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4563534.
STRINGi10116.ENSRNOP00000026186.

Chemistry

ChEMBLiCHEMBL4886.

Proteomic databases

PaxDbiP17988.
PRIDEiP17988.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026186; ENSRNOP00000026186; ENSRNOG00000019342.
GeneIDi83783.
KEGGirno:83783.
UCSCiRGD:3767. rat.

Organism-specific databases

CTDi6817.
RGDi3767. Sult1a1.

Phylogenomic databases

eggNOGiNOG260792.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiP17988.
KOiK01014.
OMAiKEWWELR.
OrthoDBiEOG7V49ZK.
PhylomeDBiP17988.
TreeFamiTF321745.

Enzyme and pathway databases

BRENDAi2.8.2.1. 5301.
ReactomeiREACT_341577. Cytosolic sulfonation of small molecules.

Miscellaneous databases

NextBioi616347.
PROiP17988.

Gene expression databases

GenevestigatoriP17988.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of a full-length cDNA (PST-1) for aryl sulfotransferase from rat liver."
    Ozawa S., Nagata K., Gong D., Yamazoe Y., Kato R.
    Nucleic Acids Res. 18:4001-4001(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Sequence analysis, in vitro translation and expression of the cDNA for rat liver minoxidil sulfotransferase."
    Hirshey S.J., Dooley T.P., Reardon I.M., Heinrikson R.L., Falany C.N.
    Mol. Pharmacol. 42:257-264(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Genomic structure of rat liver aryl sulfotransferase IV-encoding gene."
    Khan A.S., Taylor B.R., Chung K., Etheredge J., Gonzales R., Ringer D.P.
    Gene 137:321-326(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "Cloning, bacterial expression and characterization of rat brain phenol sulfotransferase SULT1A1: an enzyme involved in neurosteroid and dopamine sulfonation."
    Mao C., Sanchez R.I., Clairmont K., Coughtrie M.W.H., Kauffman F.C.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  5. "Characterization of a complementary DNA for rat liver aryl sulfotransferase IV and use in evaluating the hepatic gene transcript levels of rats at various stages of 2-acetylaminofluorene-induced hepatocarcinogenesis."
    Yerokun T., Etheredge J.L., Norton T.R., Carter H.A., Chung K.H., Birckbichler P.J., Ringer D.P.
    Cancer Res. 52:4779-4786(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-291.
  6. "Affinity labeling of aryl sulfotransferase IV. Identification of a peptide sequence at the binding site for 3'-phosphoadenosine-5'-phosphosulfate."
    Zheng Y., Bergold A., Duffel M.W.
    J. Biol. Chem. 269:30313-30319(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 63-68, CHARACTERIZATION.
  7. Cited for: CHARACTERIZATION.
    Tissue: Liver.
  8. "Characterization and expression of hepatic sulfotransferase involved in the metabolism of N-substituted aryl compounds."
    Yamazoe Y., Ozawa S., Nagata K., Gong D.-W., Kato R.
    Environ. Health Perspect. 102:99-103(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Sulfotransferase gene expression in rat hepatic and extrahepatic tissues."
    Runge-Morris M.A.
    Chem. Biol. Interact. 92:67-76(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiST1A1_RAT
AccessioniPrimary (citable) accession number: P17988
Secondary accession number(s): Q548D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 1, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.