STS_RAT
ID STS_RAT Reviewed; 577 AA.
AC P15589;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Steryl-sulfatase;
DE EC=3.1.6.2 {ECO:0000250|UniProtKB:P08842};
DE AltName: Full=Arylsulfatase C;
DE Short=ASC;
DE AltName: Full=Steroid sulfatase;
DE AltName: Full=Steryl-sulfate sulfohydrolase;
DE Flags: Precursor;
GN Name=Sts;
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;
RA Li X.M., Salido E.C., Gong Y., Yen P.H., Kitada Y., Serikawa T.,
RA Shapiro L.J.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-45.
RC TISSUE=Liver;
RX PubMed=2765556; DOI=10.1016/0167-4838(89)90187-8;
RA Kawano J., Kotani T., Ohtaki S., Minamino N., Matsuo H., Oinuma T.,
RA Aikawa E.;
RT "Characterization of rat and human steroid sulfatases.";
RL Biochim. Biophys. Acta 997:199-205(1989).
CC -!- FUNCTION: Catalyzes the conversion of sulfated steroid precursors, such
CC as dehydroepiandrosterone sulfate (DHEA-S) and estrone sulfate to the
CC free steroid. {ECO:0000250|UniProtKB:P08842}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehydroepiandrosterone 3-sulfate + H2O = 3beta-hydroxyandrost-
CC 5-en-17-one + H(+) + sulfate; Xref=Rhea:RHEA:19873,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:28689, ChEBI:CHEBI:57905; EC=3.1.6.2;
CC Evidence={ECO:0000250|UniProtKB:P08842};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone 3-sulfate + H2O = estrone + H(+) + sulfate;
CC Xref=Rhea:RHEA:31055, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:17263, ChEBI:CHEBI:60050;
CC Evidence={ECO:0000250|UniProtKB:P08842};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P08842};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P08842};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08842}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P08842}; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08842}; Multi-
CC pass membrane protein {ECO:0000305}. Note=The sequence shows several
CC membrane-spanning domains that could serve to anchor the protein in the
CC microsomal membrane.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250|UniProtKB:P08842}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; U37138; AAC53097.1; -; mRNA.
DR PIR; S05414; S05414.
DR RefSeq; NP_036793.1; NM_012661.1.
DR AlphaFoldDB; P15589; -.
DR SMR; P15589; -.
DR STRING; 10116.ENSRNOP00000043915; -.
DR BindingDB; P15589; -.
DR ChEMBL; CHEMBL3531; -.
DR GlyGen; P15589; 3 sites.
DR PaxDb; P15589; -.
DR PRIDE; P15589; -.
DR GeneID; 24800; -.
DR KEGG; rno:24800; -.
DR CTD; 412; -.
DR RGD; 3783; Sts.
DR eggNOG; KOG3867; Eukaryota.
DR InParanoid; P15589; -.
DR PhylomeDB; P15589; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-1663150; The activation of arylsulfatases.
DR PRO; PR:P15589; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004773; F:steryl-sulfatase activity; IDA:RGD.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR GO; GO:0007611; P:learning or memory; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0043588; P:skin development; IEP:RGD.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Lipid metabolism; Membrane; Metal-binding;
KW Microsome; Pregnancy; Reference proteome; Signal; Steroid metabolism;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2765556"
FT CHAIN 20..577
FT /note="Steryl-sulfatase"
FT /id="PRO_0000033416"
FT TOPO_DOM 21..183
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TRANSMEM 184..207
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TOPO_DOM 208..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TOPO_DOM 234..577
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT ACT_SITE 74
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT ACT_SITE 135
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT MOD_RES 74
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..147
FT /evidence="ECO:0000250"
FT DISULFID 169..241
FT /evidence="ECO:0000250"
FT DISULFID 445..488
FT /evidence="ECO:0000250"
FT DISULFID 480..486
FT /evidence="ECO:0000250"
FT DISULFID 561..571
FT /evidence="ECO:0000250"
SQ SEQUENCE 577 AA; 62679 MW; 07562EADEDCDB716 CRC64;
MLWPCLLALL LSQLNFLCAA RPGPGPNFLL IMADDLGIGD LGCYGNRTLR TPHIDRLALE
GVKLTQHLAA APLCTPSRAA FLTGRYPVRS GMASHGRLGV FLFSASSGGL PPNEVTFAKL
LKGQGYTTGL VGKWHLGLSC QAASDFCHHP GRHGFDRFLG TPTTNLRDCK PGGGTVFGSA
QQVFVVLPMN ILGAVLLAMA LARWAGLARP PGWVFGVTVA AMAAVGGAYV AFLYHFRPAN
CFLMADFTIT QQPTDYKGLT QRLASEAGDF LRRNRDTPFL LFLSFMHVHT AHFANPEFAG
QSLHGAYGDA VEEMDWAVGQ VLATLDKLGL ANNTLVYLTS DHGAHVEELG PNGERHGGSN
GIYRGGKANT WEGGIRVPGL VRWPGVIVPG QEVEEPTSNM DVFPTVARLA GAELPTDRVI
DGRDLMPLLL GHVQHSEHEF LFHYCNAYLS AVAWRPHNSS SVWKAFYFTP NFDPPGSNGC
FSTHVCMCHG HHVTHHDPPL LFDIARDPRE RHPLTPETEP RHGEILRNMD AAARAHVATL
EEAPNQLSMS NVAWKPWLQL CLPSKPHPLA CRCAGDG
