ST1B1_MOUSE
ID ST1B1_MOUSE Reviewed; 299 AA.
AC Q9QWG7; Q8C301; Q9Z2T0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Sulfotransferase 1B1;
DE Short=ST1B1;
DE EC=2.8.2.1 {ECO:0000269|PubMed:9644246};
DE AltName: Full=DOPA/tyrosine sulfotransferase;
DE AltName: Full=Sulfotransferase family cytosolic 1B member 1;
GN Name=Sult1b1 {ECO:0000312|MGI:MGI:2136282};
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND CATALYTIC ACTIVITY.
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=9644246; DOI=10.1093/oxfordjournals.jbchem.a022097;
RA Saeki Y., Sakakibara Y., Araki Y., Yanagisawa K., Suiko M., Nakajima H.,
RA Liu M.-C.;
RT "Molecular cloning, expression, and characterization of a novel mouse liver
RT SULT1B1 sulfotransferase.";
RL J. Biochem. 124:55-64(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:9644246). May play a role in
CC gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol
CC (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria.
CC The product 4-EPS crosses the blood-brain barrier and may negatively
CC regulate oligodendrocyte maturation and myelination, affecting the
CC functional connectivity of different brain regions associated with the
CC limbic system (By similarity). {ECO:0000250|UniProtKB:O43704,
CC ECO:0000269|PubMed:9644246}.
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:9644246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC Evidence={ECO:0000305|PubMed:9644246};
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:9644246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877;
CC Evidence={ECO:0000305|PubMed:9644246};
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:0000250|UniProtKB:O43704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893;
CC Evidence={ECO:0000250|UniProtKB:O43704};
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:0000269|PubMed:9644246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67881;
CC Evidence={ECO:0000305|PubMed:9644246};
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:0000269|PubMed:9644246};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67885;
CC Evidence={ECO:0000305|PubMed:9644246};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43704}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QWG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QWG7-2; Sequence=VSP_012509;
CC -!- TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:9644246}.
CC -!- DEVELOPMENTAL STAGE: Expression was detected at very low level in liver
CC from 1 day-old and then gradually increased to the maximum level at 4
CC weeks old. {ECO:0000269|PubMed:9644246}.
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; U92076; AAD09249.1; -; mRNA.
DR EMBL; AF022894; AAD01746.1; -; mRNA.
DR EMBL; AK033498; BAC28321.1; -; mRNA.
DR EMBL; AK087595; BAC39939.1; -; mRNA.
DR EMBL; BC024361; AAH24361.1; -; mRNA.
DR CCDS; CCDS19391.1; -. [Q9QWG7-1]
DR PIR; JE0186; JE0186.
DR RefSeq; NP_063931.1; NM_019878.4. [Q9QWG7-1]
DR RefSeq; XP_006535213.1; XM_006535150.2.
DR RefSeq; XP_006535214.1; XM_006535151.1.
DR RefSeq; XP_006535215.1; XM_006535152.3. [Q9QWG7-1]
DR AlphaFoldDB; Q9QWG7; -.
DR SMR; Q9QWG7; -.
DR STRING; 10090.ENSMUSP00000031199; -.
DR iPTMnet; Q9QWG7; -.
DR PhosphoSitePlus; Q9QWG7; -.
DR jPOST; Q9QWG7; -.
DR MaxQB; Q9QWG7; -.
DR PaxDb; Q9QWG7; -.
DR PeptideAtlas; Q9QWG7; -.
DR PRIDE; Q9QWG7; -.
DR ProteomicsDB; 257426; -. [Q9QWG7-1]
DR ProteomicsDB; 257427; -. [Q9QWG7-2]
DR Antibodypedia; 951; 218 antibodies from 25 providers.
DR DNASU; 56362; -.
DR Ensembl; ENSMUST00000031199; ENSMUSP00000031199; ENSMUSG00000029269. [Q9QWG7-1]
DR Ensembl; ENSMUST00000117455; ENSMUSP00000112679; ENSMUSG00000029269. [Q9QWG7-1]
DR Ensembl; ENSMUST00000120150; ENSMUSP00000112844; ENSMUSG00000029269. [Q9QWG7-1]
DR GeneID; 56362; -.
DR KEGG; mmu:56362; -.
DR UCSC; uc008xym.1; mouse. [Q9QWG7-1]
DR CTD; 27284; -.
DR MGI; MGI:2136282; Sult1b1.
DR VEuPathDB; HostDB:ENSMUSG00000029269; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000161848; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; Q9QWG7; -.
DR OMA; CAFVSNW; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q9QWG7; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 3474.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR BioGRID-ORCS; 56362; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9QWG7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9QWG7; protein.
DR Bgee; ENSMUSG00000029269; Expressed in small intestine Peyer's patch and 48 other tissues.
DR Genevisible; Q9QWG7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:MGI.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0006068; P:ethanol catabolic process; ISO:MGI.
DR GO; GO:0009812; P:flavonoid metabolic process; ISO:MGI.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; ISO:MGI.
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:MGI.
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 Alternative splicing; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="Sulfotransferase 1B1"
FT /id="PRO_0000085162"
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 VAR_SEQ 299
FT /note="A -> ALNFTNFEIIIGFSLKFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012509"
FT CONFLICT 55
FT /note="S -> T (in Ref. 2; BAC39939)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> P (in Ref. 1; AAD09249)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="E -> K (in Ref. 2; BAC39939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34901 MW; BFD0E0909AD8482D CRC64;
MSASEDVWRK DLKMIHGYPM IYAFALNWER IEEFQSTPGD IVITTYPKSG TTWLSEIVDM
VLNDGNVEKC KRDVITSKVP MLELSVPGIR ISGVELLKKT PSPRIIKTHL PIDLLPKSFW
ENKCKMIYLA RNGKDVAVSY YHFDLMNSIN PLPGTWEEYL EKFLAGNVAY GSWFDHVKSW
WEKREEHPLL YLYYEELKQN PKKEIKKIAS FLDKTLDEEA LDRIVHHTSF EMMKENPLVN
YTHLPTAMMD HSKSPFMRKG IVGDWKNYFT MTQTEQFDAV YKKKMSGTTL EFCTDIQSA
