ST3A1_MOUSE
ID ST3A1_MOUSE Reviewed; 293 AA.
AC O35403;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Amine sulfotransferase;
DE EC=2.8.2.3;
DE AltName: Full=SULT-X2;
DE AltName: Full=Sulfotransferase 3A1;
DE Short=ST3A1;
GN Name=Sult3a1; Synonyms=St3a1;
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].
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).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the N-sulfonation of amines.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a primary amine = a sulfamate +
CC adenosine 3',5'-bisphosphate + 2 H(+); Xref=Rhea:RHEA:24136,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:65296, ChEBI:CHEBI:131822; EC=2.8.2.3;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AF026075; AAB82293.1; -; mRNA.
DR CCDS; CCDS23771.1; -.
DR AlphaFoldDB; O35403; -.
DR SMR; O35403; -.
DR STRING; 10090.ENSMUSP00000090259; -.
DR iPTMnet; O35403; -.
DR PhosphoSitePlus; O35403; -.
DR MaxQB; O35403; -.
DR PaxDb; O35403; -.
DR PRIDE; O35403; -.
DR ProteomicsDB; 254572; -.
DR MGI; MGI:1931469; Sult3a1.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; O35403; -.
DR PhylomeDB; O35403; -.
DR BRENDA; 2.8.2.3; 3474.
DR ChiTaRS; Sult3a1; mouse.
DR PRO; PR:O35403; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35403; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047685; F:amine sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008146; F:sulfotransferase activity; 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 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..293
FT /note="Amine sulfotransferase"
FT /id="PRO_0000085165"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 46..51
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 220..225
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 252..254
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 35181 MW; 5BA84040453E0917 CRC64;
MDNKDEYLLN FKGYNFQKTL VKMEVVENIE NYEIRDDDIF IVTYPKSGTI WTQQILSLIY
FEGHRNRTEN IETIDRAPFF EYNIHKLDYA KMPSPRIFSS HIPYYLVPKG LKDKKAKILY
MYRNPKDVLI SYFHFSNLML IFQNPDTVES FMQTFLDGDV VGSLWFDHIR GWYEHRHDFN
IMFMSFEDMK KDFRSSVLKI CSFLEKELSE EDVDAVVRQA TFQKMKADPR ANYEHIIKDE
LGTRNEMGSF LRKGVVGAWK HYLTVDQSER FDKIFHRNMK NIPLKFIWDI NEE
