ID   SUHB_CAVPO              Reviewed;         287 AA.
AC   P52841;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=3-beta-hydroxysteroid sulfotransferase;
DE            EC=2.8.2.2;
DE   AltName: Full=Alcohol sulfotransferase;
DE   AltName: Full=Hydroxysteroid sulfotransferase 2;
DE            Short=HST2;
DE   AltName: Full=Pregnenolone sulfotransferase;
GN   Name=STD2;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=8672244; DOI=10.1089/dna.1996.15.481;
RA   Dufort I., Tremblay Y., Belanger A., Labrie F., Luu-The V.;
RT   "Isolation and characterization of a stereospecific 3beta-hydroxysteriod
RT   sulfotransferase (pregnenolone sulfotransferase) cDNA.";
RL   DNA Cell Biol. 15:481-487(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=NIH 2; TISSUE=Adrenal gland;
RX   PubMed=8554560; DOI=10.1006/bbrc.1995.2879;
RA   Luu N.X., Driscoll W.J., Martin B.M., Strott C.A.;
RT   "Molecular cloning and expression of a guinea pig 3-hydroxysteroid
RT   sulfotransferase distinct from chiral-specific 3 alpha-hydroxysteroid
RT   sulfotransferase.";
RL   Biochem. Biophys. Res. Commun. 217:1078-1086(1995).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfonation of 3-beta-
CC       hydroxyl groups of neutral steroids. High preference for C21 steroid
CC       (pregnenolone).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-
CC         bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver, intestine and kidney.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; U55944; AAB07868.1; -; mRNA.
DR   EMBL; U35115; AAC52347.1; -; mRNA.
DR   PIR; JC4531; JC4531.
DR   RefSeq; NP_001166297.1; NM_001172826.1.
DR   AlphaFoldDB; P52841; -.
DR   SMR; P52841; -.
DR   GeneID; 100379531; -.
DR   KEGG; cpoc:100379531; -.
DR   CTD; 100379531; -.
DR   InParanoid; P52841; -.
DR   OrthoDB; 780670at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004027; F:alcohol sulfotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
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; Lipid metabolism; Reference proteome;
KW   Steroid metabolism; Transferase.
FT   CHAIN           1..287
FT                   /note="3-beta-hydroxysteroid sulfotransferase"
FT                   /id="PRO_0000085140"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..49
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..223
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         247..249
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        205
FT                   /note="R -> K (in Ref. 2; AAC52347)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  34063 MW;  CCEA3C3623964950 CRC64;
     MSDNTLWFEG IRFPMVGFSP ELLREVRDKF LVKDEDTITV TYPKSGTNWL IEIVCLILSK
     GDPKWVQSVP IWDRSPWIET QHGNELMKSQ KDPRIYTSHL PLHLFPKSFF SSKAKVIYCI
     RNPRDVLVSG YYFTSKMKIA EKPETLQQYM KWFLQGNVIY GSWFEHVRDW LSMREKENFL
     VLSYEELIKD TRSIVEKICQ FLGKRLKPEE IDLVLKYSSF KFMKENEMSN YSLLPNDLTT
     EGFTFLRKGV VGDWKHHFTV AQAEEFDKIY QEKMAGYPPK LFPWEEC