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P17988 (ST1A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfotransferase 1A1

Short name=ST1A1
EC=2.8.2.1
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 names
Name:Sult1a1
Synonyms:St1a1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Liver, kidney, heart and colon.

Induction

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

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the sulfotransferase 1 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Sulfotransferase 1A1
PRO_0000085131

Regions

Nucleotide binding44 – 496PAPS By similarity
Nucleotide binding223 – 2286PAPS By similarity
Nucleotide binding251 – 2555PAPS By similarity
Region102 – 1043Substrate binding By similarity

Sites

Active site1041Proton acceptor By similarity
Binding site1261PAPS By similarity
Binding site1341PAPS By similarity
Binding site1891PAPS By similarity

Sequences

Sequence LengthMass (Da)Tools
P17988 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 9EC66C72923DB872

FASTA29133,906
        10         20         30         40         50         60 
MEFSRPPLVH VKGIPLIKYF AETIGPLQNF TAWPDDLLIS TYPKSGTTWM SEILDMIYQG 

        70         80         90        100        110        120 
GKLEKCGRAP IYARVPFLEF KCPGVPSGLE TLEETPAPRL LKTHLPLSLL PQSLLDQKVK 

       130        140        150        160        170        180 
VIYIARNAKD VVVSYYNFYN MAKLHPDPGT WDSFLENFMD GEVSYGSWYQ HVKEWWELRH 

       190        200        210        220        230        240 
THPVLYLFYE DIKENPKREI KKILEFLGRS LPEETVDSIV HHTSFKKMKE NCMTNYTTIP 

       250        260        270        280        290 
TEIMDHNVSP FMRKGTTGDW KNTFTVAQNE RFDAHYAKTM TDCDFKFRCE L 

« Hide

References

[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(1990) [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(1992) [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(1993) [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 (JUL-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(1992) [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(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 63-68, CHARACTERIZATION.
[7]"cDNA expression studies of rat liver aryl sulphotransferase."
Cruickshank D., Sansom L.N., Veronese M.E., Mojarrabi B., McManus M.E., Zhu X.
Biochem. Biophys. Res. Commun. 191:295-301(1993) [PubMed] [Europe PMC] [Abstract]
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(1994) [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(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS10329.
RefSeqNP_114022.1. NM_031834.1.
UniGeneRn.1507.

3D structure databases

ProteinModelPortalP17988.
SMRP17988. Positions 4-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4563534.
STRING10116.ENSRNOP00000026186.

Chemistry

ChEMBLCHEMBL4886.

Proteomic databases

PaxDbP17988.
PRIDEP17988.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026186; ENSRNOP00000026186; ENSRNOG00000019342.
GeneID83783.
KEGGrno:83783.
UCSCRGD:3767. rat.

Organism-specific databases

CTD6817.
RGD3767. Sult1a1.

Phylogenomic databases

eggNOGNOG260792.
GeneTreeENSGT00740000115442.
HOGENOMHOG000037209.
HOVERGENHBG001195.
InParanoidP17988.
KOK01014.
OMAISAPPKC.
OrthoDBEOG7V49ZK.
TreeFamTF321745.

Enzyme and pathway databases

BRENDA2.8.2.1. 5301.

Gene expression databases

GenevestigatorP17988.

Family and domain databases

InterProIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

NextBio616347.
PROP17988.

Entry information

Entry nameST1A1_RAT
AccessionPrimary (citable) accession number: P17988
Secondary accession number(s): Q548D2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 19, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families