ID   ST3A1_RABIT             Reviewed;         301 AA.
AC   O46640;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Amine sulfotransferase;
DE            EC=2.8.2.3;
DE   AltName: Full=AST-RB1;
DE   AltName: Full=Sulfotransferase 3A1;
DE            Short=ST3A1;
GN   Name=SULT3A1; Synonyms=ST3A1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-66; 160-176; 200-206;
RP   254-260 AND 286-301, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=9538231; DOI=10.1093/oxfordjournals.jbchem.a021961;
RA   Yoshinari K., Nagata K., Ogino M., Fujita K., Shiraga T., Iwasaki K.,
RA   Hata T., Yamazoe Y.;
RT   "Molecular cloning and expression of an amine sulfotransferase cDNA: a new
RT   gene family of cytosolic sulfotransferases in mammals.";
RL   J. Biochem. 123:479-486(1998).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the N-sulfonation of amines
CC       (PTHP, aniline, 4-chloroaniline, 2-naphthylamine).
CC       {ECO:0000269|PubMed:9538231}.
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:0000269|PubMed:9538231}.
CC   -!- TISSUE SPECIFICITY: Expressed in male liver.
CC       {ECO:0000269|PubMed:9538231}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; D86219; BAA24994.1; -; mRNA.
DR   PIR; JW0078; JW0078.
DR   RefSeq; NP_001075679.1; NM_001082210.2.
DR   AlphaFoldDB; O46640; -.
DR   SMR; O46640; -.
DR   STRING; 9986.ENSOCUP00000022723; -.
DR   GeneID; 100009006; -.
DR   KEGG; ocu:100009006; -.
DR   CTD; 57430; -.
DR   eggNOG; KOG1584; Eukaryota.
DR   InParanoid; O46640; -.
DR   OrthoDB; 780670at2759; -.
DR   BRENDA; 2.8.2.3; 1749.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047685; F:amine sulfotransferase activity; IEA:UniProtKB-EC.
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; Direct protein sequencing; Reference proteome; Transferase.
FT   CHAIN           1..301
FT                   /note="Amine sulfotransferase"
FT                   /id="PRO_0000085166"
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         186
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   301 AA;  35943 MW;  A28EE738D54C3C97 CRC64;
     MDNSRKYLLN FKGCNFERTL VDMKILEKLD DFEIRDDDVF VITYPKSGTV WTQQILSLIY
     FEGHRNRTEK WDTLDRVPFL EYNIRKVDIE NRPSPRLFAS HLPYYLAPKS LKNNKAKIIY
     VYRNPKDVLI SFFHFSNMVV KLEASNTLEN FMEKFLDGKV VGSIWFDHIR GWYEHKNDFN
     ILFMMYEDMK KDLRSSILKI SSFLEKDLSE EEVDAIVRQA TFENMKFIPQ ANYNNILSNE
     IGRRHNEGAF LRKGAVGDWK HHMTVEQSER FDRIFQEEMK DFPLKFIWDL NDEANSNHSA
     K