ST1D1_RAT
ID ST1D1_RAT Reviewed; 295 AA.
AC G3V9R3; Q9Z1G0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Sulfotransferase 1 family member D1;
DE Short=ST1D1;
DE EC=2.8.2.-;
DE AltName: Full=Dopamine sulfotransferase Sult1d1;
DE AltName: Full=Tyrosine-ester sulfotransferase;
GN Name=Sult1d1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RA Herrmann A., Stoffel W.;
RT "Isolation and expression of cDNA encoding tyrosine-ester sulfotransferase
RT from rat kidney.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC99890.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U32372; AAC99890.1; ALT_FRAME; mRNA.
DR EMBL; CH474125; EDL83152.1; -; Genomic_DNA.
DR RefSeq; NP_068537.1; NM_021769.1.
DR AlphaFoldDB; G3V9R3; -.
DR SMR; G3V9R3; -.
DR STRING; 10116.ENSRNOP00000066303; -.
DR PaxDb; G3V9R3; -.
DR Ensembl; ENSRNOT00000072483; ENSRNOP00000066303; ENSRNOG00000001960.
DR GeneID; 60393; -.
DR KEGG; rno:60393; -.
DR UCSC; RGD:620491; rat.
DR CTD; 53315; -.
DR RGD; 620491; Sult1d1.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000162879; -.
DR InParanoid; G3V9R3; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; G3V9R3; -.
DR TreeFam; TF321745; -.
DR PRO; PR:G3V9R3; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Proteomes; UP000234681; Chromosome 14.
DR Bgee; ENSRNOG00000001960; Expressed in esophagus and 10 other tissues.
DR ExpressionAtlas; G3V9R3; baseline and differential.
DR Genevisible; G3V9R3; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Catecholamine metabolism; Cytoplasm; Lipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1 family member D1"
FT /id="PRO_0000416460"
FT ACT_SITE 108
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"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 257..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CONFLICT 97
FT /note="N -> D (in Ref. 1; AAC99890)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="K -> R (in Ref. 1; AAC99890)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="L -> C (in Ref. 1; AAC99890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 35004 MW; D80BD22679C2BA93 CRC64;
MDNKLDVFRR ELVDVQGIPL FWSIAEQWSQ VESFEARPDD ILISTYPKSG TTWISEILDL
IYNNGDAEKC KRDAIYRRVP FMELIIPGIT NGVEMLNNMQ SPRLVKTHLP VQLLPSSFWK
NDCKMIYVAR NAKDVAVSYY YFHQMAKMHP EPGTWEEFLE KFMAGQVSFG PWYDHVKGWW
EKRKEYRILY LFYEDMKEDP KCEIQKVLKF LEKDIPEEVV NKILYHSSFS VMKANPSANY
TTMMKEEMDQ SVSPFMRKGI SGDWKNQFTV AQYEKFEEDY VKKMEESTLK FRSEI
