ST1D1_MOUSE
ID ST1D1_MOUSE Reviewed; 295 AA.
AC Q3UZZ6; O35401; Q6NZD1; Q9R2C2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Sulfotransferase 1 family member D1;
DE Short=ST1D1;
DE EC=2.8.2.-;
DE AltName: Full=Amine N-sulfotransferase;
DE Short=SULT-N;
DE AltName: Full=Dopamine sulfotransferase Sult1d1;
DE AltName: Full=Tyrosine-ester sulfotransferase;
GN Name=Sult1d1; Synonyms=St1d1;
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, AND TISSUE SPECIFICITY.
RX PubMed=9647753; DOI=10.1006/bbrc.1998.8872;
RA Sakakibara Y., Yanagisawa K., Takami Y., Nakayama T., Suiko M., Liu M.-C.;
RT "Molecular cloning, expression, and functional characterization of novel
RT mouse sulfotransferases.";
RL Biochem. Biophys. Res. Commun. 247:681-686(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9920733; DOI=10.1006/bbrc.1998.9872;
RA Liu M.C., Sakakibara Y., Liu C.C.;
RT "Bacterial expression, purification, and characterization of a novel mouse
RT sulfotransferase that catalyzes the sulfation of eicosanoids.";
RL Biochem. Biophys. Res. Commun. 254:65-69(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=15087475; DOI=10.1124/jpet.104.065532;
RA Shimada M., Terazawa R., Kamiyama Y., Honma W., Nagata K., Yamazoe Y.;
RT "Unique properties of a renal sulfotransferase, St1d1, in dopamine
RT metabolism.";
RL J. Pharmacol. Exp. Ther. 310:808-814(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RA Herrmann A., Stoffel W.;
RT "Molecular cloning of cDNA encoding tyrosine-ester sulfotransferase from
RT mouse kidney.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Lung;
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).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19966186; DOI=10.1210/en.2009-0590;
RA Wong S., Tan K., Carey K.T., Fukushima A., Tiganis T., Cole T.J.;
RT "Glucocorticoids stimulate hepatic and renal catecholamine inactivation by
RT direct rapid induction of the dopamine sulfotransferase Sult1d1.";
RL Endocrinology 151:185-194(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE, FUNCTION, AND MUTAGENESIS OF GLU-247.
RX PubMed=18977225; DOI=10.1016/j.febslet.2008.10.035;
RA Teramoto T., Sakakibara Y., Inada K., Kurogi K., Liu M.C., Suiko M.,
RA Kimura M., Kakuta Y.;
RT "Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase.";
RL FEBS Lett. 582:3909-3914(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEXES WITH 1-NAPHTHOL;
RP ADENOSINE-3'-5'-DIPHOSPHATE AND P-NITROPHENOL.
RX PubMed=19073143; DOI=10.1016/j.bbrc.2008.12.013;
RA Teramoto T., Sakakibara Y., Liu M.C., Suiko M., Kimura M., Kakuta Y.;
RT "Structural basis for the broad range substrate specificity of a novel
RT mouse cytosolic sulfotransferase--mSULT1D1.";
RL Biochem. Biophys. Res. Commun. 379:76-80(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH
RP 3'-PHOSPHO-5'-ADENYLYL SULFATE AND P-NITROPHENOL.
RX PubMed=19344693; DOI=10.1016/j.bbrc.2009.03.146;
RA Teramoto T., Sakakibara Y., Liu M.C., Suiko M., Kimura M., Kakuta Y.;
RT "Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal
RT structure of a mouse sulfotransferase, mSULT1D1, complexed with donor
RT substrate and accepter substrate.";
RL Biochem. Biophys. Res. Commun. 383:83-87(2009).
CC -!- FUNCTION: Sulfotransferase with broad substrate specificity that
CC utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to
CC catalyze the sulfate conjugation of catecholamines, such as dopamine,
CC prostaglandins, leukotriene E4, drugs and xenobiotic compounds. Has
CC sulfotransferase activity towards p-nitrophenol, 2-naphthylamine and
CC minoxidil (in vitro). Sulfonation increases the water solubility of
CC most compounds, and therefore their renal excretion, but it can also
CC result in bioactivation to form active metabolites.
CC {ECO:0000269|PubMed:15087475, ECO:0000269|PubMed:18977225,
CC ECO:0000269|PubMed:19966186, ECO:0000269|PubMed:9647753,
CC ECO:0000269|PubMed:9920733}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19966186}.
CC -!- TISSUE SPECIFICITY: Detected in kidney and liver. Detected in kidney
CC collecting duct cells. {ECO:0000269|PubMed:19966186,
CC ECO:0000269|PubMed:9647753}.
CC -!- INDUCTION: Up-regulated in liver and kidney by dexamethasone, a
CC glucocorticoid analog. {ECO:0000269|PubMed:19966186}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC99889.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF026073; AAC69919.1; -; mRNA.
DR EMBL; U32371; AAC99889.1; ALT_FRAME; mRNA.
DR EMBL; AK133530; BAE21709.1; -; mRNA.
DR EMBL; AC158917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066190; AAH66190.1; -; mRNA.
DR CCDS; CCDS39130.1; -.
DR PIR; JE0197; JE0197.
DR RefSeq; NP_058051.3; NM_016771.3.
DR PDB; 2ZPT; X-ray; 1.15 A; X=1-295.
DR PDB; 2ZVP; X-ray; 1.30 A; X=1-295.
DR PDB; 2ZVQ; X-ray; 1.30 A; X=1-295.
DR PDB; 2ZYT; X-ray; 1.55 A; X=1-295.
DR PDB; 2ZYU; X-ray; 1.80 A; X=1-295.
DR PDB; 2ZYV; X-ray; 1.81 A; X=1-295.
DR PDB; 2ZYW; X-ray; 1.80 A; X=1-295.
DR PDBsum; 2ZPT; -.
DR PDBsum; 2ZVP; -.
DR PDBsum; 2ZVQ; -.
DR PDBsum; 2ZYT; -.
DR PDBsum; 2ZYU; -.
DR PDBsum; 2ZYV; -.
DR PDBsum; 2ZYW; -.
DR AlphaFoldDB; Q3UZZ6; -.
DR SMR; Q3UZZ6; -.
DR BioGRID; 207279; 2.
DR IntAct; Q3UZZ6; 1.
DR MINT; Q3UZZ6; -.
DR STRING; 10090.ENSMUSP00000108940; -.
DR iPTMnet; Q3UZZ6; -.
DR PhosphoSitePlus; Q3UZZ6; -.
DR jPOST; Q3UZZ6; -.
DR MaxQB; Q3UZZ6; -.
DR PaxDb; Q3UZZ6; -.
DR PeptideAtlas; Q3UZZ6; -.
DR PRIDE; Q3UZZ6; -.
DR ProteomicsDB; 257428; -.
DR DNASU; 53315; -.
DR Ensembl; ENSMUST00000113314; ENSMUSP00000108940; ENSMUSG00000029273.
DR GeneID; 53315; -.
DR KEGG; mmu:53315; -.
DR UCSC; uc008xyo.2; mouse.
DR CTD; 53315; -.
DR MGI; MGI:1926341; Sult1d1.
DR VEuPathDB; HostDB:ENSMUSG00000029273; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000162879; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; Q3UZZ6; -.
DR OMA; AQYEKFE; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q3UZZ6; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 3474.
DR BRENDA; 2.8.2.9; 3474.
DR BioGRID-ORCS; 53315; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q3UZZ6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3UZZ6; protein.
DR Bgee; ENSMUSG00000029273; Expressed in olfactory epithelium and 85 other tissues.
DR Genevisible; Q3UZZ6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IDA:MGI.
DR GO; GO:0051923; P:sulfation; IDA:MGI.
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 3D-structure; Catecholamine metabolism; Cytoplasm; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1 family member D1"
FT /id="PRO_0000416459"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 81
FT /ligand="substrate"
FT BINDING 106..108
FT /ligand="substrate"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 142
FT /ligand="substrate"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 227..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 257..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT MUTAGEN 247
FT /note="E->A: No effect on enzyme activity against
FT dopamine."
FT /evidence="ECO:0000269|PubMed:18977225"
FT MUTAGEN 247
FT /note="E->L: Reduces enzyme activity against dopamine."
FT /evidence="ECO:0000269|PubMed:18977225"
FT CONFLICT 206
FT /note="K -> Q (in Ref. 1; AAC69919)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="F -> Y (in Ref. 1; AAC69919)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="E -> G (in Ref. 5; AAH66190)"
FT /evidence="ECO:0000305"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2ZPT"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:2ZPT"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:2ZPT"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2ZPT"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:2ZPT"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:2ZPT"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:2ZPT"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:2ZPT"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:2ZPT"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2ZPT"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2ZPT"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:2ZPT"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:2ZPT"
SQ SEQUENCE 295 AA; 35083 MW; A60A9AF60CC2736F CRC64;
MDNKLDVFRR ELVDVEGIPL FWSIAEHWSQ VESFEARPDD ILISTYPKSG TTWVSEILDL
IYNNGDAEKC KRDAIYKRVP FMELIIPGIT NGVEMLNNMP SPRIVKTHLP VQLLPSSFWK
NDCKIIYVAR NAKDVVVSYY YFYQMAKIHP EPGTWEEFLE KFMAGQVSFG PWYDHVKSWW
EKRKEYRILY LFYEDMKENP KCEIQKILKF LEKDIPEEIL NKILYHSSFS VMKENPSANY
TTMMKEEMDH SVSPFMRKGI SGDWKNQFTV AQYEKFEEDY VKKMEDSTLK FRSEI
