ST2A2_RAT
ID ST2A2_RAT Reviewed; 284 AA.
AC P22789; Q63551;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Alcohol sulfotransferase A;
DE EC=2.8.2.2;
DE AltName: Full=Androsterone-sulfating sulfotransferase;
DE Short=AD-ST;
DE AltName: Full=Hydroxysteroid sulfotransferase A;
DE Short=STA;
DE AltName: Full=ST-40;
DE AltName: Full=Senescence marker protein 2A;
DE AltName: Full=Sulfotransferase 2A2;
DE Short=ST2A2;
GN Name=St2a2; Synonyms=Smp2a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 174-184 AND 234-239.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2306259; DOI=10.1016/0006-291x(90)91036-r;
RA Ogura K., Kajita J., Narihata H., Watabe T., Ozawa S., Nagata K.,
RA Yamazoe Y., Kato R.;
RT "cDNA cloning of the hydroxysteroid sulfotransferase STa sharing a strong
RT homology in amino acid sequence with the senescence marker protein SMP-2 in
RT rat livers.";
RL Biochem. Biophys. Res. Commun. 166:1494-1500(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8033248; DOI=10.1016/0009-2797(94)90059-0;
RA Ogura K., Satsukawa M., Okuda H., Hiratsuka A., Watabe T.;
RT "Major hydroxysteroid sulfotransferase STa in rat liver cytosol may consist
RT of two microheterogeneous subunits.";
RL Chem. Biol. Interact. 92:129-144(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RX PubMed=2302387; DOI=10.1021/bi00454a031;
RA Song C.S., Kim J.M., Roy A.K., Chatterjee B.;
RT "Structure and regulation of the senescence marker protein 2 gene
RT promoter.";
RL Biochemistry 29:542-551(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-37.
RX PubMed=2754334;
RA Barnes S., Buchina E.S., King R.J., McBurnett T., Taylor K.B.;
RT "Bile acid sulfotransferase I from rat liver sulfates bile acids and 3-
RT hydroxy steroids: purification, N-terminal amino acid sequence, and kinetic
RT properties.";
RL J. Lipid Res. 30:529-540(1989).
RN [5]
RP PROTEIN SEQUENCE OF 2-46.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8352748; DOI=10.1042/bj2930795;
RA Takahashi M., Homma H., Matsui M.;
RT "Developmental changes in the isoelectric variants of rat hepatic
RT hydroxysteroid sulphotransferase.";
RL Biochem. J. 293:795-800(1993).
RN [6]
RP PROTEIN SEQUENCE OF 2-21.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2113604;
RA Ogura K., Sohtome T., Sugiyama A., Okuda H., Hiratsuka A., Watabe T.;
RT "Rat liver cytosolic hydroxysteroid sulfotransferase (sulfotransferase a)
RT catalyzing the formation of reactive sulfate esters from carcinogenic
RT polycyclic hydroxymethylarenes.";
RL Mol. Pharmacol. 37:848-854(1990).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze sulfonation of hydroxysteroids
CC and xenobiotics.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-
CC bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2;
CC -!- SUBUNIT: Oligomer consisting of several isoelectric variants with the
CC same molecular mass. Relative contents of these isoelectic variants are
CC different in weanling (20 days) than in young adults (110 days).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Liver, exhibiting a sex-dependent spatial
CC localization in the lobule of the liver.
CC -!- DEVELOPMENTAL STAGE: There is a marked sex difference (female >> male)
CC in the cytosolic level of this protein. Its activity increases after
CC birth in parallel in both sexes until the weanling stage. Thereafter
CC the activity decreases in males, whereas it declines temporarily in
CC females and increases again to a maximum level in adult females.
CC -!- INDUCTION: The ST activities display gender- and age-dependent
CC alterations and are known to be under the regulation of gonadal,
CC adrenal and growth hormones.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M33329; AAA42183.1; -; mRNA.
DR EMBL; X63410; CAA45007.1; -; mRNA.
DR EMBL; M29301; AAA42151.1; ALT_TERM; Genomic_DNA.
DR PIR; I60190; I60190.
DR RefSeq; NP_036827.3; NM_012695.3.
DR AlphaFoldDB; P22789; -.
DR SMR; P22789; -.
DR iPTMnet; P22789; -.
DR PhosphoSitePlus; P22789; -.
DR PaxDb; P22789; -.
DR PRIDE; P22789; -.
DR GeneID; 24902; -.
DR KEGG; rno:24902; -.
DR UCSC; RGD:3727; rat.
DR CTD; 629219; -.
DR RGD; 3727; Smp2a.
DR InParanoid; P22789; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P22789; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.2; 5301.
DR PRO; PR:P22789; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
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 Cytoplasm; Direct protein sequencing; Lipid metabolism; Reference proteome;
KW Steroid metabolism; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2113604,
FT ECO:0000269|PubMed:2754334, ECO:0000269|PubMed:8352748"
FT CHAIN 2..284
FT /note="Alcohol sulfotransferase A"
FT /id="PRO_0000085143"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 43..48
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 217..222
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 246..248
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="P -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..33
FT /note="NVCNKFVVKE -> DVNKSVKD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Y -> N (in Ref. 2; CAA45007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 33252 MW; 131F67150862E51D CRC64;
MPDYTWFEGI PFPAFGIPKE TLQNVCNKFV VKEEDLILLT YPKSGTNWLI EIVCLIQTKG
DPKWIQSVTI WDRSPWIETD LGYDMLIKKK GPRLITSHLP MHLFSKSLFS SKAKVIYLIR
NPRDVLVSGY YFWGKTTLAK KPDSLGTYVE WFLKGYVPYG SWFEHIRAWL SMRELDNFLL
LYYEDMKKDT MGTIKKICDF LGKKLEPDEL DLVLKYSSFQ VMKENNMSNY NLMEKELILP
GFTFMRNGTT GDWKNHFTVA QAEAFDKVFQ EKMAGFPPGM FPWD
