ST6B1_MOUSE
ID ST6B1_MOUSE Reviewed; 303 AA.
AC P0CC03;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Sulfotransferase 6B1;
DE Short=ST6B1;
DE AltName: Full=Thyroxine sulfotransferase;
DE EC=2.8.2.n2 {ECO:0000269|PubMed:19505954};
GN Name=Sult6b1;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=19505954; DOI=10.1093/jb/mvp087;
RA Takahashi S., Sakakibara Y., Mishiro E., Kouriki H., Nobe R., Kurogi K.,
RA Yasuda S., Liu M.C., Suiko M.;
RT "Molecular cloning, expression and characterization of a novel mouse SULT6
RT cytosolic sulfotransferase.";
RL J. Biochem. 146:399-405(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-303.
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).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC thyroxine. Involved in the metabolism of thyroxine.
CC {ECO:0000269|PubMed:19505954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + thyroxine = adenosine 3',5'-
CC bisphosphate + H(+) + thyroxine sulfate; Xref=Rhea:RHEA:26422,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:58910, ChEBI:CHEBI:305790; EC=2.8.2.n2;
CC Evidence={ECO:0000269|PubMed:19505954};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=143.7 uM for thyroxine {ECO:0000269|PubMed:19505954};
CC Vmax=40.4 pmol/min/mg enzyme {ECO:0000269|PubMed:19505954};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:19505954};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19505954}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, thymus, lung,
CC liver and testis. {ECO:0000269|PubMed:19505954}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AC154274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK010729; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS50182.1; -.
DR RefSeq; NP_001157097.1; NM_001163625.1.
DR AlphaFoldDB; P0CC03; -.
DR SMR; P0CC03; -.
DR STRING; 10090.ENSMUSP00000132823; -.
DR PhosphoSitePlus; P0CC03; -.
DR PaxDb; P0CC03; -.
DR PRIDE; P0CC03; -.
DR ProteomicsDB; 257084; -.
DR Antibodypedia; 29393; 25 antibodies from 14 providers.
DR Ensembl; ENSMUST00000169544; ENSMUSP00000132823; ENSMUSG00000038045.
DR GeneID; 73671; -.
DR KEGG; mmu:73671; -.
DR UCSC; uc012axk.1; mouse.
DR CTD; 391365; -.
DR MGI; MGI:1920921; Sult6b1.
DR VEuPathDB; HostDB:ENSMUSG00000038045; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000159084; -.
DR InParanoid; P0CC03; -.
DR OMA; HLFFTYQ; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P0CC03; -.
DR TreeFam; TF321745; -.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR BioGRID-ORCS; 73671; 1 hit in 72 CRISPR screens.
DR PRO; PR:P0CC03; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P0CC03; protein.
DR Bgee; ENSMUSG00000038045; Expressed in olfactory epithelium and 165 other tissues.
DR ExpressionAtlas; P0CC03; baseline and differential.
DR Genevisible; P0CC03; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="Sulfotransferase 6B1"
FT /id="PRO_0000389506"
FT ACT_SITE 118
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 65..70
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 140
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 148
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 203
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 237..242
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 259..261
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT CONFLICT 134
FT /note="K -> E (in Ref. 3; AK010729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 35077 MW; 674DBEE6F3329FDD CRC64;
MADKSKFIDY IDDALEKSKE TTLSQLFLTY QGIPYPVTMC TQETFRALDA FEARSDDVLL
ASYPKCGSNW ILHIVSELIF AVSKKKYACP EFPVLECGDA EKYQRMKLFP SPRILTTHLH
YDKLPQSIFK NKAKILVIFR NPKDTAVSFF HFHNDVPDIP SYASWDEFFR QFIKGQVSWG
SYFDFAINWN KHIDDENVKF ILYEDLKENL VVGIKQISEF LGFSLTDEQI ETISTQSTFL
AMRANSQETH GAIGPFLFRK GEVGDWKRLF NETQNQEMDE RFKECLAGTS LGDKLKYEAY
CLA
