ST1B1_RAT
ID ST1B1_RAT Reviewed; 299 AA.
AC P52847;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sulfotransferase 1B1;
DE Short=ST1B1;
DE EC=2.8.2.1 {ECO:0000269|PubMed:12773305, ECO:0000269|PubMed:8530477};
DE AltName: Full=DOPA/tyrosine sulfotransferase {ECO:0000303|PubMed:8530477};
DE AltName: Full=Sulfotransferase family cytosolic 1B member 1;
GN Name=Sult1b1 {ECO:0000312|RGD:708534}; Synonyms=St1b1;
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], PROTEIN SEQUENCE OF 108-117; 126-134 AND
RP 260-266, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8530477; DOI=10.1074/jbc.270.51.30470;
RA Sakakibara Y., Takami Y., Zwieb C., Nakayama T., Suiko M., Nakajima H.,
RA Liu M.-C.;
RT "Purification, characterization, and molecular cloning of a novel rat liver
RT Dopa/tyrosine sulfotransferase.";
RL J. Biol. Chem. 270:30470-30478(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8033246; DOI=10.1016/0009-2797(94)90057-4;
RA Yamazoe Y., Nagata K., Ozawa S., Kato R.;
RT "Structural similarity and diversity of sulfotransferases.";
RL Chem. Biol. Interact. 92:107-117(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9443824; DOI=10.1093/oxfordjournals.jbchem.a021846;
RA Fujita K., Nagata K., Ozawa S., Sasano H., Yamazoe Y.;
RT "Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs,
RT encoding thyroid hormone sulfotransferases.";
RL J. Biochem. 122:1052-1061(1997).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12773305; DOI=10.1152/ajpendo.00046.2003;
RA Kester M.H., Kaptein E., Roest T.J., van Dijk C.H., Tibboel D., Meinl W.,
RA Glatt H., Coughtrie M.W., Visser T.J.;
RT "Characterization of rat iodothyronine sulfotransferases.";
RL Am. J. Physiol. 285:E592-E598(2003).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC dopamine, small phenols such as 1-naphthol and p-nitrophenol and
CC thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3)
CC and reverse triiodothyronine (rT3) (PubMed:12773305, PubMed:8530477).
CC May play a role in gut microbiota-host metabolic interaction. O-
CC sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite
CC produced by gut bacteria. The product 4-EPS crosses the blood-brain
CC barrier and may negatively regulate oligodendrocyte maturation and
CC myelination, affecting the functional connectivity of different brain
CC regions associated with the limbic system (By similarity).
CC {ECO:0000250|UniProtKB:O43704, ECO:0000269|PubMed:12773305,
CC ECO:0000269|PubMed:8530477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC Evidence={ECO:0000269|PubMed:12773305, ECO:0000269|PubMed:8530477};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:8530477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3',5-triiodo-L-thyronine =
CC 3,3',5-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67876, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:176511, ChEBI:CHEBI:533015;
CC Evidence={ECO:0000269|PubMed:12773305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC Evidence={ECO:0000305|PubMed:12773305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3',5'-triiodo-L-thyronine =
CC 3,3',5'-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57261,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:176513;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67889;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3,3'-diiodo-L-thyronine = 3,3'-
CC diiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67892, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:176514, ChEBI:CHEBI:176515;
CC Evidence={ECO:0000269|PubMed:12773305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC Evidence={ECO:0000305|PubMed:12773305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-
CC bisphosphate + dopamine 3-O-sulfate + H(+); Xref=Rhea:RHEA:67880,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:133524;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67881;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-
CC bisphosphate + dopamine 4-O-sulfate + H(+); Xref=Rhea:RHEA:67884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:59905, ChEBI:CHEBI:133529;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67885;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl
CC sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133681;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC Evidence={ECO:0000250|UniProtKB:O43704};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.62 uM for 3,3'-diiodo-L-thyronine {ECO:0000269|PubMed:12773305};
CC KM=100 uM for 3,3',5-triiodo-L-thyronine
CC {ECO:0000269|PubMed:12773305};
CC KM=3.44 mM for D-dopamine {ECO:0000269|PubMed:8530477};
CC KM=30.9 mM for p-nitrophenol {ECO:0000269|PubMed:8530477};
CC KM=0.76 mM for L-dopamine {ECO:0000269|PubMed:8530477};
CC Vmax=125000 pmol/min/mg enzyme with p-nitrophenol as substrate
CC {ECO:0000269|PubMed:8530477};
CC Vmax=3521 pmol/min/mg enzyme with L-dopamine as substrate
CC {ECO:0000269|PubMed:8530477};
CC Vmax=13699 pmol/min/mg enzyme with D-dopamine as substrate
CC {ECO:0000269|PubMed:8530477};
CC Vmax=251 pmol/min/mg enzyme with 3,3'-diiodo-L-thyronine
CC {ECO:0000269|PubMed:12773305};
CC Vmax=50 pmol/min/mg enzyme with 3,3',5-triiodo-L-thyronine as
CC substrate {ECO:0000269|PubMed:12773305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8530477}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; U38419; AAC52387.1; -; mRNA.
DR EMBL; D89375; BAA24546.1; -; mRNA.
DR PIR; JC5884; JC5884.
DR RefSeq; NP_071958.1; NM_022513.2.
DR AlphaFoldDB; P52847; -.
DR SMR; P52847; -.
DR IntAct; P52847; 1.
DR STRING; 10116.ENSRNOP00000002699; -.
DR iPTMnet; P52847; -.
DR PhosphoSitePlus; P52847; -.
DR PaxDb; P52847; -.
DR PRIDE; P52847; -.
DR Ensembl; ENSRNOT00000002699; ENSRNOP00000002699; ENSRNOG00000001967.
DR GeneID; 64305; -.
DR KEGG; rno:64305; -.
DR UCSC; RGD:708534; rat.
DR CTD; 27284; -.
DR RGD; 708534; Sult1b1.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000161848; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; P52847; -.
DR OMA; CAFVSNW; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P52847; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 5301.
DR Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR PRO; PR:P52847; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000001967; Expressed in liver and 15 other tissues.
DR Genevisible; P52847; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:RGD.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:RGD.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:RGD.
DR GO; GO:0009812; P:flavonoid metabolic process; ISO:RGD.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; ISO:RGD.
DR GO; GO:0051923; P:sulfation; IDA:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR InterPro; IPR033289; SULT1B1.
DR PANTHER; PTHR11783:SF14; PTHR11783:SF14; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="Sulfotransferase 1B1"
FT /id="PRO_0000085163"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 139
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 228..233
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT BINDING 258..260
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O43704"
FT CONFLICT 68
FT /note="E -> G (in Ref. 1; AAC52387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34835 MW; FDECEC304EE788A8 CRC64;
MGTAEDVFRK DLKIIHGYPM VYAFALGWEK IEEFQSRPCD IVIPTYPKSG TTWLSEIVDM
VLNDGNVEKC KRDVITSKVP MLEQNVPGAR RSGVELLKKT PSPRIIKTHL PIDLLPKSFW
DNKCKMIYLA RNGKDVAVSY YHFDLMNNIQ PLPGTWEEYL EKFLAGNVAY GSWFDHVKSW
WEKREGHPIL FLYYEDLKKN PKKEIKKIAN FLDKTLDEHT LERIVHHTSF EVMKDNPLVN
YTHLPTEIMD HSKSPFMRKG VVGDWKNYFT MTQSEKFDAI YKKKLSGTTL EFCTDIQSA
