ST1B1_CANLF
ID ST1B1_CANLF Reviewed; 296 AA.
AC Q95JD5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sulfotransferase 1B1;
DE Short=ST1B1;
DE Short=cSULT1B1;
DE EC=2.8.2.1 {ECO:0000269|PubMed:11368519};
DE AltName: Full=Sulfotransferase family cytosolic 1B member 1;
GN Name=SULT1B1; Synonyms=ST1B2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=11368519; DOI=10.1006/abbi.2001.2373;
RA Tsoi C., Falany C.N., Morgenstern R., Swedmark S.;
RT "Molecular cloning, expression, and characterization of a canine
RT sulfotransferase that is a human ST1B2 ortholog.";
RL Arch. Biochem. Biophys. 390:87-92(2001).
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:11368519). May play a role
CC in gut microbiota-host metabolic interaction. O-sulfonates 4-
CC ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by
CC gut bacteria. The product 4-EPS crosses the blood-brain barrier and may
CC negatively regulate oligodendrocyte maturation and myelination,
CC affecting the functional connectivity of different brain regions
CC associated with the limbic system (By similarity).
CC {ECO:0000250|UniProtKB:O43704, ECO:0000269|PubMed:11368519}.
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:11368519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:11368519};
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:11368519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC Evidence={ECO:0000305|PubMed:11368519};
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:0000269|PubMed:11368519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67889;
CC Evidence={ECO:0000305|PubMed:11368519};
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:11368519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC Evidence={ECO:0000305|PubMed:11368519};
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=9.3 uM for 1-naphthol {ECO:0000269|PubMed:11368519};
CC KM=37 uM for 3,3',5-triiodo-L-thyronine (T3)
CC {ECO:0000269|PubMed:11368519};
CC KM=33 uM for 3,3'-diiodo-L-thyronine (T2)
CC {ECO:0000269|PubMed:11368519};
CC KM=31 uM for 3,3',5'-triiodo-L-thyronine (rT3)
CC {ECO:0000269|PubMed:11368519};
CC Vmax=8 nmol/min/mg enzyme with 3,3'-diiodo-L-thyronine as substrate
CC {ECO:0000269|PubMed:11368519};
CC Vmax=5.1 nmol/min/mg enzyme with 3,3',5-triiodo-L-thyronine as
CC substrate {ECO:0000269|PubMed:11368519};
CC Vmax=0.45 nmol/min/mg enzyme with 3,3',5'-triiodo-L-thyronine as
CC substrate {ECO:0000269|PubMed:11368519};
CC Vmax=11 nmol/min/mg enzyme with 1-naphthol as substrate
CC {ECO:0000269|PubMed:11368519};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43704}.
CC -!- TISSUE SPECIFICITY: Expressed highly in the colon, kidney and small
CC intestine of male and female dogs. Highly expressed in the jejunum and
CC ileum of the male dog than the female dog, which displayed more
CC expression in duodenum (at protein level).
CC {ECO:0000269|PubMed:11368519}.
CC -!- MISCELLANEOUS: Contrary to other mammalian orthologs the canine SULT1B1
CC does not shown sulfotransferase activity toward dopamine.
CC {ECO:0000269|PubMed:11368519}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AY004332; AAF86583.1; -; mRNA.
DR RefSeq; NP_001182764.1; NM_001195835.1.
DR AlphaFoldDB; Q95JD5; -.
DR SMR; Q95JD5; -.
DR STRING; 9612.ENSCAFP00000004246; -.
DR PaxDb; Q95JD5; -.
DR Ensembl; ENSCAFT00040008330; ENSCAFP00040007237; ENSCAFG00040004374.
DR Ensembl; ENSCAFT00845017670; ENSCAFP00845013756; ENSCAFG00845010048.
DR GeneID; 403636; -.
DR KEGG; cfa:403636; -.
DR CTD; 27284; -.
DR VEuPathDB; HostDB:ENSCAFG00845010048; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000161848; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; Q95JD5; -.
DR OMA; CAFVSNW; -.
DR OrthoDB; 780670at2759; -.
DR TreeFam; TF321745; -.
DR Reactome; R-CFA-156584; Cytosolic sulfonation of small molecules.
DR Proteomes; UP000002254; Chromosome 13.
DR Bgee; ENSCAFG00000002871; Expressed in jejunum and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:Ensembl.
DR GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl.
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; IEA:Ensembl.
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; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Sulfotransferase 1B1"
FT /id="PRO_0000085160"
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"
SQ SEQUENCE 296 AA; 34869 MW; 3D54CF003BF09365 CRC64;
MISPKDFLRK NLKMIHGYPI IYTFANNWEN IEQFHSRPDD IIIATYPKSG TTWVSEIVDM
VLNNGDVEKC KRDFITVKVP MLEMAVPGLR TSGIEQLEKN PSPRLVKTHL PIALLPKSFW
ENNCKMIYLA RNAKDVAVSY YHFDLMNNLE PAPGPWEEYL ERFMTGNVAY GSWFNHVKSW
WKKKEEHPIL FLYYEDMKEN PKREVQKIAR FLEKNLNDEV LDKIIHHTSF EMMKDNPLVN
YTHLPSTVMD HSKSSFMRKG IAGDWKNYFT VAQNEKFDVI YKKEMSGTTL QFRTEI
