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Database: UniProt
Entry: F7I2I0_CALJA
LinkDB: F7I2I0_CALJA
Original site: F7I2I0_CALJA 
ID   F7I2I0_CALJA            Unreviewed;       294 AA.
AC   F7I2I0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
GN   Name=SULT1E1 {ECO:0000313|Ensembl:ENSCJAP00000026189.3};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000026189.3, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000026189.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000026189.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC         hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567;
CC         Evidence={ECO:0000256|ARBA:ARBA00043800};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC         Evidence={ECO:0000256|ARBA:ARBA00043800};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-
CC         estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582;
CC         Evidence={ECO:0000256|ARBA:ARBA00043684};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC         Evidence={ECO:0000256|ARBA:ARBA00043684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC         = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC         H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC         ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC         Evidence={ECO:0000256|ARBA:ARBA00043689};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl
CC         sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:133681;
CC         Evidence={ECO:0000256|ARBA:ARBA00033673};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC         Evidence={ECO:0000256|ARBA:ARBA00033673};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-
CC         bisphosphate + estrone 3-sulfate + H(+); Xref=Rhea:RHEA:15973,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17263, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:60050; EC=2.8.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00043703};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15974;
CC         Evidence={ECO:0000256|ARBA:ARBA00043703};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC       {ECO:0000256|ARBA:ARBA00005771, ECO:0000256|RuleBase:RU361155}.
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DR   AlphaFoldDB; F7I2I0; -.
DR   STRING; 9483.ENSCJAP00000026189; -.
DR   Ensembl; ENSCJAT00000027675.5; ENSCJAP00000026189.3; ENSCJAG00000014226.5.
DR   eggNOG; KOG1584; Eukaryota.
DR   GeneTree; ENSGT00940000162261; -.
DR   HOGENOM; CLU_027239_1_2_1; -.
DR   InParanoid; F7I2I0; -.
DR   OMA; VIKVIQF; -.
DR   OrthoDB; 3083090at2759; -.
DR   TreeFam; TF321745; -.
DR   Proteomes; UP000008225; Chromosome 3.
DR   Bgee; ENSCJAG00000014226; Expressed in liver and 2 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR   GO; GO:0047894; F:flavonol 3-sulfotransferase activity; IEA:Ensembl.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0050294; F:steroid sulfotransferase activity; IEA:Ensembl.
DR   GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IEA:Ensembl.
DR   GO; GO:0006711; P:estrogen catabolic process; IEA:Ensembl.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:Ensembl.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0051923; P:sulfation; IEA:Ensembl.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR11783:SF53; SULFOTRANSFERASE 1E1; 1.
DR   PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00022665};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Steroid-binding {ECO:0000256|ARBA:ARBA00022665};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361155}.
FT   DOMAIN          37..286
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
SQ   SEQUENCE   294 AA;  35052 MW;  505DFB0C56EC25CE CRC64;
     MNSELDYYEK FEEVHGILMY KDFAKYWDNV EAFQARPDDV VIATYPKSGT TWVCEIVYMI
     YKEGDVEKCK EDVIFNRIPF LECRNENVMN GVKQLEEMNS PRIVKTHLPP ELLPASFWEK
     NCKMIYLCRN AKDVAVSFYY FFLMVAGHPN PGSFPEFVEK FMQGQVPYGS WYKHVKSWWE
     KGKSPRVLFL FYEDLKENTR KEVIKLIHFL ERKPSEELVD KIIHHTSFQE MKNNPSTNYT
     TLPDEIMNQK VSPFMRKGII GDWKNHFTVA LNEKFEKNYE EQMKESTLKF RTEI
//
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