ST6B1_DANRE
ID ST6B1_DANRE Reviewed; 296 AA.
AC F1QYJ6; Q567N1; Q800X2;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Sulfotransferase 6B1 {ECO:0000305};
DE EC=2.8.2.- {ECO:0000269|PubMed:12507510};
DE AltName: Full=Thyroxine sulfotransferase;
DE EC=2.8.2.n2 {ECO:0000269|PubMed:12507510};
GN Name=sult6b1 {ECO:0000312|ZFIN:ZDB-GENE-050417-228};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:AAO49010.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12507510; DOI=10.1016/s0006-291x(02)02915-7;
RA Sugahara T., Liu C.C., Govind Pai T., Liu M.C.;
RT "Molecular cloning, expression, and functional characterization of a novel
RT zebrafish cytosolic sulfotransferase.";
RL Biochem. Biophys. Res. Commun. 300:725-730(2003).
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:AAH93112.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-259.
RC TISSUE=Larva {ECO:0000312|EMBL:AAH93112.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a
CC variety of xenobiotic and endogenous compounds, including dopamine, T3
CC (triiodo-L-thyronine), T4 (thyroxine), flavonoids, isoflavonoids, and
CC other phenolic compounds. {ECO:0000269|PubMed:12507510}.
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 -!- ACTIVITY REGULATION: Strongly inhibited by the divalent metal cations
CC Fe(2+), Hg(2+), Co(2+), Zn(2+), Cu(2+) and Cd(2+).
CC {ECO:0000269|PubMed:12507510}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:12507510};
CC Temperature dependence:
CC Thermostable between 20-43 degrees Celsius.
CC {ECO:0000269|PubMed:12507510};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P0CC03}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC {ECO:0000255|RuleBase:RU361155}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH93112.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Contains sequence from chromosome 22 in the C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY180110; AAO49010.1; -; mRNA.
DR EMBL; CU929458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093112; AAH93112.1; ALT_SEQ; mRNA.
DR RefSeq; NP_999851.1; NM_214686.1.
DR AlphaFoldDB; F1QYJ6; -.
DR SMR; F1QYJ6; -.
DR STRING; 7955.ENSDARP00000105990; -.
DR PaxDb; F1QYJ6; -.
DR Ensembl; ENSDART00000130131; ENSDARP00000105990; ENSDARG00000086826.
DR GeneID; 322462; -.
DR KEGG; dre:322462; -.
DR CTD; 391365; -.
DR ZFIN; ZDB-GENE-050417-228; sult6b1.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000159084; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; F1QYJ6; -.
DR OMA; HLFFTYQ; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; F1QYJ6; -.
DR TreeFam; TF321745; -.
DR Reactome; R-DRE-156584; Cytosolic sulfonation of small molecules.
DR PRO; PR:F1QYJ6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000086826; Expressed in gastrula and 40 other tissues.
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; IDA:ZFIN.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:ZFIN.
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..296
FT /note="Sulfotransferase 6B1"
FT /id="PRO_0000444632"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 134
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 142
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 197
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT BINDING 253..255
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:P49891"
FT CONFLICT 140
FT /note="V -> L (in Ref. 1; AAO49010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 33995 MW; CD68D171FB8C4DB5 CRC64;
MSQMKSRMET AAKMKDEDKL YRRDGILYST VLSPPETLDK LKDLQAREDD LILVAYPKCG
FNWMVAVLRK IINASTGKDE KPPERPPLVE FLPPTVQEEM AQMPPPRLLG THLHPDNMPA
TFFTKKPKIL VVFRNPKDTV VSYYHFMNKN PVLPNAESWD KFFSDFMTGD VSWGSYFDHA
LAWEKRIDDP NVMIVMYEDL KQNLPEGVKK ISEFFSLPLT DEQVSSIAGQ STFSAMVENS
QKSHGNFGSI FFRKGEVGDW KNHFSEAQSK QMDELYHSKL AGTKLAARMN YDLYCQ
