ST2A8_MOUSE
ID ST2A8_MOUSE Reviewed; 282 AA.
AC Q8BGL3; B1PQU4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Sulfotransferase 2A8 {ECO:0000303|PubMed:28442498};
DE Short=SULT2A8 {ECO:0000303|PubMed:28442498};
DE AltName: Full=Glycochenodeoxycholate sulfotransferase 2A8;
DE EC=2.8.2.34 {ECO:0000269|PubMed:28442498};
DE AltName: Full=Liver sulfotransferase-like protein {ECO:0000303|PubMed:28442498};
DE Short=L-STL {ECO:0000303|PubMed:28442498};
GN Name=Sult2a8 {ECO:0000312|MGI:MGI:1924221};
GN Synonyms=2810007J24Rik {ECO:0000312|MGI:MGI:1924221};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=28442498; DOI=10.1194/jlr.m074302;
RA Feng L., Yuen Y.L., Xu J., Liu X., Chan M.Y., Wang K., Fong W.P.,
RA Cheung W.T., Lee S.S.;
RT "Identification and characterization of a novel PPARalpha-regulated and
RT 7alpha-hydroxyl bile acid-preferring cytosolic sulfotransferase mL-STL
RT (Sult2a8).";
RL J. Lipid Res. 58:1114-1131(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Lander E., Abouelleil A., Allen N., Anderson M.,
RA Anderson S., Arachchi H.M., Barna N., Bastien V., Bloom T., Boguslavkiy L.,
RA Boukhgalter B., Camarata J., Chang J., Choepel Y., Collymore A., Cook A.,
RA Cooke P., Corum B., DeArellano K., Diaz J.S., Dodge S., Dooley K.,
RA Dorris L., Erickson J., Faro S., Ferreira P., FitzGerald M., Gage D.,
RA Galagan J., Gardyna S., Graham L., Grand-Pierre N., Hafez N., Hagopian D.,
RA Hagos B., Hall J., Horton L., Hulme W., Iliev I., Johnson R., Jones C.,
RA Kamat A., Karatas A., Kells C., Landers T., Levine R., Lindblad-Toh K.,
RA Liu G., Liu X., Lui A., Mabbitt R., MacLean C., Macdonald P., Major J.,
RA Manning J., Matthews C., McCarthy M., Meldrim J., Meneus L., Mihova T.,
RA Mlenga V., Murphy T., Naylor J., Nguyen C., Nguyen T., Nicol R., Norbu C.,
RA O'Connor T., O'Donnell P., O'Neil D., Oliver J., Peterson K., Phunkhang P.,
RA Pierre N., Rachupka A., Ramasamy U., Raymond C., Retta R., Rise C.,
RA Rogov P., Roman J., Schauer S., Schupback R., Seaman S., Severy P.,
RA Smith C., Spencer B., Stange-Thomann N., Stojanovic N., Stubbs M.,
RA Talamas J., Tesfaye S., Theodore J., Topham K., Travers M., Vassiliev H.,
RA Venkataraman V.S., Viel R., Vo A., Wilson B., Wu X., Wyman D., Young G.,
RA Zainoun J., Zembek L., Zimmer A., Zody M.;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, ACTIVE SITE, AND
RP MUTAGENESIS OF HIS-48 AND LEU-99.
RX PubMed=29685090; DOI=10.1080/09168451.2018.1464897;
RA Shimohira T., Kurogi K., Liu M.C., Suiko M., Sakakibara Y.;
RT "The critical role of His48 in mouse cytosolic sulfotransferase SULT2A8 for
RT the 7alpha-hydroxyl sulfation of bile acids.";
RL Biosci. Biotechnol. Biochem. 82:1359-1365(2018).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE (PAP) AND CHOLATE, FUNCTION, PATHWAY, ACTIVE
RP SITE, AND MUTAGENESIS OF LYS-44; HIS-48; ASN-72; LEU-99; CYS-232; ILE-236;
RP GLU-237 AND HIS-239.
RX PubMed=33872606; DOI=10.1016/j.jlr.2021.100074;
RA Wang K., Chan Y.C., So P.K., Liu X., Feng L., Cheung W.T., Sau-Tuen Lee S.,
RA Wing-Ngor Au S.;
RT "Structure of mouse cytosolic sulfotransferase SULT2A8 provides insight
RT into sulfonation of 7alpha-hydroxyl bile acids.";
RL J. Lipid Res. 62:100074-100074(2021).
CC -!- FUNCTION: Hepatic sulfotransferase involved in the maintenance of bile
CC acid homeostasis and energy balance. Catalyzes the transfer of
CC sulfonate group from 3'-phosphoadenylyl sulfate (PAPS) to the 7-alpha
CC hydroxy group of primary bile acids to form 7-monosulfate derivatives
CC in the pathway of bile acid elimination. Displays high catalytic
CC efficiency toward cholate, chenodeoxycholate and their glycine and
CC taurine conjugates. {ECO:0000269|PubMed:28442498,
CC ECO:0000269|PubMed:29685090, ECO:0000269|PubMed:33872606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + cholate = adenosine 3',5'-
CC bisphosphate + cholate 7-sulfate + H(+); Xref=Rhea:RHEA:67552,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172392;
CC Evidence={ECO:0000269|PubMed:28442498, ECO:0000269|PubMed:29685090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67553;
CC Evidence={ECO:0000305|PubMed:28442498, ECO:0000305|PubMed:29685090};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + glycocholate = adenosine 3',5'-
CC bisphosphate + glycocholate 7-sulfate + H(+); Xref=Rhea:RHEA:67556,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172393;
CC Evidence={ECO:0000269|PubMed:28442498, ECO:0000269|PubMed:29685090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67557;
CC Evidence={ECO:0000305|PubMed:28442498, ECO:0000305|PubMed:29685090};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + taurocholate = adenosine 3',5'-
CC bisphosphate + H(+) + taurocholate 7-sulfate; Xref=Rhea:RHEA:67560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36257, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172394;
CC Evidence={ECO:0000269|PubMed:28442498, ECO:0000269|PubMed:29685090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67561;
CC Evidence={ECO:0000305|PubMed:28442498, ECO:0000305|PubMed:29685090};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + chenodeoxycholate = adenosine
CC 3',5'-bisphosphate + chenodeoxycholate 7-sulfate + H(+);
CC Xref=Rhea:RHEA:67564, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:172395;
CC Evidence={ECO:0000269|PubMed:28442498, ECO:0000269|PubMed:29685090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67565;
CC Evidence={ECO:0000305|PubMed:28442498, ECO:0000305|PubMed:29685090};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + glycochenodeoxycholate =
CC adenosine 3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate +
CC H(+); Xref=Rhea:RHEA:17689, ChEBI:CHEBI:15378, ChEBI:CHEBI:36252,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58877; EC=2.8.2.34;
CC Evidence={ECO:0000269|PubMed:28442498};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17690;
CC Evidence={ECO:0000305|PubMed:28442498};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + taurochenodeoxycholate =
CC adenosine 3',5'-bisphosphate + H(+) + taurochenodeoxycholate 7-
CC sulfate; Xref=Rhea:RHEA:67568, ChEBI:CHEBI:9407, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:172396;
CC Evidence={ECO:0000269|PubMed:28442498, ECO:0000269|PubMed:29685090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67569;
CC Evidence={ECO:0000305|PubMed:28442498, ECO:0000305|PubMed:29685090};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-muricholate = adenosine
CC 3',5'-bisphosphate + alpha-muricholate 7-sulfate + H(+);
CC Xref=Rhea:RHEA:67572, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:134116, ChEBI:CHEBI:172398;
CC Evidence={ECO:0000269|PubMed:28442498};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67573;
CC Evidence={ECO:0000305|PubMed:29685090};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for cholate (at pH 6.27) {ECO:0000269|PubMed:29685090};
CC KM=5.3 uM for glycocholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC KM=4.75 uM for chenodeoxycholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC KM=21.1 uM for taurocholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC KM=3.6 uM for taurochenodeoxycholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC Vmax=73.5 pmol/min/mg enzyme toward cholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC Vmax=82.7 pmol/min/mg enzyme glycocholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC Vmax=31.5 pmol/min/mg enzyme chenodeoxycholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC Vmax=100 pmol/min/mg enzyme taurocholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC Vmax=60.1 pmol/min/mg enzyme taurochenodeoxycholate (at pH 6.27)
CC {ECO:0000269|PubMed:29685090};
CC Note=The catalytic activity decreases as pH increases from 5.5 to
CC 7.5. {ECO:0000269|PubMed:28442498, ECO:0000269|PubMed:29685090};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:28442498};
CC -!- PATHWAY: Lipid metabolism; bile acid degradation.
CC {ECO:0000269|PubMed:28442498, ECO:0000269|PubMed:29685090,
CC ECO:0000269|PubMed:33872606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28442498}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L-STL1 {ECO:0000303|PubMed:28442498};
CC IsoId=Q8BGL3-1; Sequence=Displayed;
CC Name=2; Synonyms=L-STL2 {ECO:0000303|PubMed:28442498};
CC IsoId=Q8BGL3-2; Sequence=VSP_061163;
CC -!- TISSUE SPECIFICITY: Liver (at protein level).
CC {ECO:0000269|PubMed:28442498}.
CC -!- DEVELOPMENTAL STAGE: Not detected in 8.5 and 14.5 dpc embryos.
CC Expressed early in postnatal liver reaching maximal levels at one month
CC of age in both male and female mice. The expression in female mice is
CC lower than in males across the lifespan. {ECO:0000269|PubMed:28442498}.
CC -!- INDUCTION: Down-regulated by PPARA agonist Wy-14.643.
CC {ECO:0000269|PubMed:28442498}.
CC -!- MISCELLANEOUS: The short isoform L-STL2 appears to be a minor form. It
CC is likely non-functional as it lacks a conserved C-terminus region
CC required for PAPS binding and sulfotransferase activity.
CC {ECO:0000305|PubMed:28442498}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; EU486166; ACA53371.1; -; mRNA.
DR EMBL; EU486167; ACA53372.1; -; mRNA.
DR EMBL; AK041070; BAC30809.1; -; mRNA.
DR EMBL; AK050422; BAC34247.1; -; mRNA.
DR EMBL; AC110880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS20833.1; -. [Q8BGL3-1]
DR RefSeq; NP_001186235.1; NM_001199306.1.
DR RefSeq; NP_780459.1; NM_175250.5.
DR RefSeq; XP_006540489.1; XM_006540426.1.
DR RefSeq; XP_006540490.1; XM_006540427.2.
DR RefSeq; XP_006540491.1; XM_006540428.1.
DR PDB; 7D1X; X-ray; 2.50 A; A/B=4-282.
DR PDB; 7EOV; X-ray; 2.60 A; A=3-279.
DR PDBsum; 7D1X; -.
DR PDBsum; 7EOV; -.
DR AlphaFoldDB; Q8BGL3; -.
DR SMR; Q8BGL3; -.
DR STRING; 10090.ENSMUSP00000066897; -.
DR PhosphoSitePlus; Q8BGL3; -.
DR jPOST; Q8BGL3; -.
DR MaxQB; Q8BGL3; -.
DR PaxDb; Q8BGL3; -.
DR PeptideAtlas; Q8BGL3; -.
DR PRIDE; Q8BGL3; -.
DR ProteomicsDB; 337419; -.
DR ProteomicsDB; 338519; -.
DR DNASU; 76971; -.
DR Ensembl; ENSMUST00000063509; ENSMUSP00000066897; ENSMUSG00000030378. [Q8BGL3-1]
DR Ensembl; ENSMUST00000168252; ENSMUSP00000128428; ENSMUSG00000030378. [Q8BGL3-1]
DR Ensembl; ENSMUST00000209425; ENSMUSP00000147301; ENSMUSG00000030378. [Q8BGL3-2]
DR GeneID; 76971; -.
DR KEGG; mmu:76971; -.
DR UCSC; uc009fgb.2; mouse. [Q8BGL3-1]
DR CTD; 76971; -.
DR MGI; MGI:1924221; Sult2a8.
DR VEuPathDB; HostDB:ENSMUSG00000030378; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000154432; -.
DR HOGENOM; CLU_027239_1_0_1; -.
DR InParanoid; Q8BGL3; -.
DR OMA; WNSINWI; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q8BGL3; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.14; 3474.
DR UniPathway; UPA00279; -.
DR BioGRID-ORCS; 76971; 0 hits in 71 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGL3; protein.
DR Bgee; ENSMUSG00000030378; Expressed in left lobe of liver and 32 other tissues.
DR ExpressionAtlas; Q8BGL3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:UniProtKB.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; ISO:MGI.
DR GO; GO:0047704; F:bile-salt sulfotransferase activity; ISO:MGI.
DR GO; GO:0050294; F:steroid sulfotransferase activity; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:MGI.
DR GO; GO:0030573; P:bile acid catabolic process; IDA:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; ISO:MGI.
DR GO; GO:0051923; P:sulfation; ISO:MGI.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:MGI.
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 3D-structure; Alternative splicing; Bile acid catabolism; Cytoplasm;
KW Lipid degradation; Lipid metabolism; Reference proteome;
KW Steroid metabolism; Transferase.
FT CHAIN 1..282
FT /note="Sulfotransferase 2A8"
FT /id="PRO_0000453530"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:29685090,
FT ECO:0000269|PubMed:33872606"
FT BINDING 44..48
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:33872606"
FT BINDING 121
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:33872606"
FT BINDING 129
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:33872606"
FT BINDING 184
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:33872606"
FT BINDING 218..223
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:33872606"
FT BINDING 244..246
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:33872606"
FT VAR_SEQ 158..282
FT /note="Missing (in isoform 2)"
FT /id="VSP_061163"
FT MUTAGEN 44
FT /note="K->A: Loss of sulfotransferase activity (at pH
FT 7.5)."
FT /evidence="ECO:0000269|PubMed:33872606"
FT MUTAGEN 48
FT /note="H->N: Decreases sulfotransferase activity (at pH
FT 6.27). Does not affect sulfotransferase activity (at pH
FT 7.5)."
FT /evidence="ECO:0000269|PubMed:29685090,
FT ECO:0000269|PubMed:33872606"
FT MUTAGEN 48
FT /note="H->T: Impairs sulfotransferase activity."
FT /evidence="ECO:0000269|PubMed:29685090,
FT ECO:0000269|PubMed:33872606"
FT MUTAGEN 72
FT /note="N->W: Increases sulfotransferase activity (at pH
FT 7.5)."
FT /evidence="ECO:0000269|PubMed:33872606"
FT MUTAGEN 99
FT /note="L->H: Decreases sulfotransferase activity (at pH
FT 6.27)."
FT /evidence="ECO:0000269|PubMed:29685090"
FT MUTAGEN 99
FT /note="L->T,V: Decreases sulfotransferase activity (at pH
FT 7.5)."
FT /evidence="ECO:0000269|PubMed:33872606"
FT MUTAGEN 232
FT /note="C->S: Decreases sulfotransferase activity (at pH
FT 7.5)."
FT /evidence="ECO:0000269|PubMed:33872606"
FT MUTAGEN 236
FT /note="I->S: Increases sulfotransferase activity."
FT /evidence="ECO:0000269|PubMed:33872606"
FT MUTAGEN 237
FT /note="E->A: Markedly decreases enzyme stability, both apo
FT and ligand-bound forms. Markedly decreases sulfotransferase
FT activity (at pH 7.5)."
FT /evidence="ECO:0000269|PubMed:33872606"
FT MUTAGEN 239
FT /note="H->G: Has little effect on sulfotransferase activity
FT (at pH 7.5)."
FT /evidence="ECO:0000269|PubMed:33872606"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:7EOV"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7EOV"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:7D1X"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:7D1X"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:7D1X"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:7D1X"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:7D1X"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:7D1X"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:7D1X"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:7D1X"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7EOV"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:7EOV"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:7D1X"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:7D1X"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:7EOV"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:7D1X"
SQ SEQUENCE 282 AA; 33295 MW; 89F950081862E33B CRC64;
MTDEFLWIEG IPFPTVYYSQ EIIREVRDRF VVRDEDTIIV TYPKSGTHWL NEIVCLILTK
GDPTWVQSTI ANERTPWIEF ENNYRILNSK EGPRLMASLL PIQLFPKSFF SSKAKVIYLI
RNPRDVLVSG YHYFNALKQG KEQVPWKIYF ENFLQGKSYF GSWFEHACGW ISLRKRENIL
VLSYEQLKKD TRNTIKKICE FLGENLESGE LELVLKNISF QIMKERMISQ SCLSNIEKHE
FIMRKGITGD WKNHFTVAQA EAFDKAFQEK AADFPQELFS WE
