ST2A1_RAT
ID ST2A1_RAT Reviewed; 284 AA.
AC P15709; A0A0G2JYC0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 4.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sulfotransferase 2A1;
DE Short=ST2A1;
DE EC=2.8.2.2 {ECO:0000250|UniProtKB:Q06520};
DE AltName: Full=Bile salt sulfotransferase;
DE EC=2.8.2.14 {ECO:0000250|UniProtKB:Q06520};
DE AltName: Full=Hydroxysteroid sulfotransferase {ECO:0000303|PubMed:2590219};
DE Short=ST {ECO:0000303|PubMed:2590219};
DE AltName: Full=ST-20;
GN Name=Sult2a1; Synonyms=St2a1;
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], DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2590219; DOI=10.1016/0006-291x(89)91050-4;
RA Ogura K., Kajita J., Narihata H., Watabe T., Ozawa S., Nagata K.,
RA Yamazoe Y., Kato R.;
RT "Cloning and sequence analysis of a rat liver cDNA encoding hydroxysteroid
RT sulfotransferase.";
RL Biochem. Biophys. Res. Commun. 165:168-174(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8033273; DOI=10.1016/0009-2797(94)90056-6;
RA Watabe T., Ogura K., Satsukawa M., Okuda H., Hiratsuka A.;
RT "Molecular cloning and functions of rat liver hydroxysteroid
RT sulfotransferases catalysing covalent binding of carcinogenic polycyclic
RT arylmethanols to DNA.";
RL Chem. Biol. Interact. 92:87-105(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=7854148; DOI=10.1093/mutage/9.6.553;
RA Glatt H., Seidel A., Harvey R.G., Coughtrie M.W.;
RT "Activation of benzylic alcohols to mutagens by human hepatic
RT sulphotransferases.";
RL Mutagenesis 9:553-557(1994).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and
CC bile acids in the liver and adrenal glands (By similarity). Mediates
CC the sulfation of a wide range of steroids and sterols, including
CC pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well
CC many xenobiotics that contain alcohol and phenol functional groups
CC (PubMed:7854148). Sulfonation increases the water solubility of most
CC compounds, and therefore their renal excretion, but it can also result
CC in bioactivation to form active metabolites. Plays an important role in
CC maintening steroid and lipid homeostasis. Plays a key role in bile acid
CC metabolism (By similarity). In addition, catalyzes the metabolic
CC activation of potent carcinogenic polycyclic arylmethanols
CC (PubMed:7854148). {ECO:0000250|UniProtKB:Q06520,
CC ECO:0000269|PubMed:7854148}.
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 Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22553;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + taurolithocholate = adenosine
CC 3',5'-bisphosphate + H(+) + taurolithocholate 3-sulfate;
CC Xref=Rhea:RHEA:14013, ChEBI:CHEBI:15378, ChEBI:CHEBI:17179,
CC ChEBI:CHEBI:58301, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=2.8.2.14;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14014;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + lithocholate = adenosine 3',5'-
CC bisphosphate + H(+) + lithocholate sulfate; Xref=Rhea:RHEA:51064,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29744, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133940;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51065;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 24-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52344, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52345;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol 24-sulfate + 3'-phosphoadenylyl
CC sulfate = (24S)-hydroxycholesterol 3,24-disulfate + adenosine 3',5'-
CC bisphosphate + H(+); Xref=Rhea:RHEA:52352, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566,
CC ChEBI:CHEBI:136568; Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52353;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-
CC bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133000;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3alpha-hydroxy-5alpha-androstan-
CC 17-one = adenosine 3',5'-bisphosphate + androsterone 3alpha-sulfate +
CC H(+); Xref=Rhea:RHEA:60644, ChEBI:CHEBI:15378, ChEBI:CHEBI:16032,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133003;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60645;
CC Evidence={ECO:0000250|UniProtKB:Q06520};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2590219}.
CC -!- DEVELOPMENTAL STAGE: There is a marked sex difference (female >> male)
CC in the expressed level of mRNA for this protein.
CC {ECO:0000269|PubMed:2590219}.
CC -!- INDUCTION: Induced by estrogens and suppressed by androgens. Expression
CC is under the influence of pituitary growth hormone and thyroid hormone.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; M31363; AAA41356.1; -; mRNA.
DR EMBL; D14988; BAA03633.1; -; mRNA.
DR EMBL; D14987; BAA03632.1; -; mRNA.
DR EMBL; AABR07002517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07002518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A33569; A33569.
DR PIR; I52849; I52849.
DR RefSeq; NP_571978.1; NM_131903.1.
DR RefSeq; XP_008757114.1; XM_008758892.2.
DR AlphaFoldDB; P15709; -.
DR SMR; P15709; -.
DR STRING; 10116.ENSRNOP00000043445; -.
DR BindingDB; P15709; -.
DR ChEMBL; CHEMBL3007; -.
DR iPTMnet; P15709; -.
DR PhosphoSitePlus; P15709; -.
DR PaxDb; P15709; -.
DR PRIDE; P15709; -.
DR GeneID; 24912; -.
DR KEGG; rno:24912; -.
DR UCSC; RGD:621337; rat.
DR CTD; 6822; -.
DR RGD; 621337; Sult2a1.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; P15709; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P15709; -.
DR PRO; PR:P15709; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000047986; Expressed in liver and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:RGD.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; IDA:RGD.
DR GO; GO:0047704; F:bile-salt sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:RGD.
DR GO; GO:0016740; F:transferase activity; IDA:RGD.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IDA:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0008202; P:steroid metabolic process; IDA:RGD.
DR GO; GO:0051923; P:sulfation; IDA:RGD.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:RGD.
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; Lipid metabolism; Reference proteome; Steroid metabolism;
KW Transferase.
FT CHAIN 1..284
FT /note="Sulfotransferase 2A1"
FT /id="PRO_0000085144"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 43..48
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 120
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 128
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 183
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 217..222
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 246..248
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT CONFLICT 33
FT /note="D -> E (in Ref. 2; BAA03633/BAA03632)"
FT CONFLICT 81..85
FT /note="LGYDM -> VGYDI (in Ref. 1; AAA41356 and 2; BAA03633/
FT BAA03632)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="I -> M (in Ref. 1; AAA41356 and 2; BAA03633/
FT BAA03632)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="V -> I (in Ref. 2; BAA03633/BAA03632)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> V (in Ref. 2; BAA03633/BAA03632)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="R -> Q (in Ref. 1; AAA41356)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="I -> T (in Ref. 1; AAA41356)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="V -> I (in Ref. 2; BAA03633/BAA03632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 33135 MW; 9572B11D992DB0C4 CRC64;
MPDYTWFEGI PFHAFGISKE TLQNVCNKFV VKDEDLILLA YPKSGTNWLI EIVCLIQTKG
DPKWIQSVTI WDRSPWIETD LGYDMLIKKK GPRLITSHLP MHLFSKSLFS SKAKVIYLVR
NPRDVLVSGY YFWGNSTLAK KPDSLGTYVE WFLKGNVLYG SWFEHIRAWL SMREWDNFLL
LYYEDMKKDT MGTIKKICDF LGKKLEPDEL DLVLKYSSFQ VMKENDMSNY SLLMKKSIFT
GIGLMRKGTV GDWKNHFTVS QAEAFDKVFQ EKMAGFPPGM FPWE
