STS_MOUSE
ID STS_MOUSE Reviewed; 624 AA.
AC P50427;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 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].
RC STRAIN=BALB/cJ;
RX PubMed=8673109; DOI=10.1038/ng0596-83;
RA Salido E.C., Li X.M., Yen P.H., Martin N., Mohandas T.K., Shapiro L.J.;
RT "Cloning and expression of the mouse pseudoautosomal steroid sulphatase
RT gene (Sts).";
RL Nat. Genet. 13:83-86(1996).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; U37545; AAB09308.1; -; mRNA.
DR RefSeq; NP_033319.1; NM_009293.1.
DR AlphaFoldDB; P50427; -.
DR SMR; P50427; -.
DR BioGRID; 203559; 3.
DR IntAct; P50427; 1.
DR GlyGen; P50427; 2 sites.
DR iPTMnet; P50427; -.
DR PhosphoSitePlus; P50427; -.
DR SwissPalm; P50427; -.
DR EPD; P50427; -.
DR jPOST; P50427; -.
DR MaxQB; P50427; -.
DR PeptideAtlas; P50427; -.
DR PRIDE; P50427; -.
DR ProteomicsDB; 257094; -.
DR DNASU; 20905; -.
DR GeneID; 20905; -.
DR KEGG; mmu:20905; -.
DR CTD; 412; -.
DR MGI; MGI:98438; Sts.
DR InParanoid; P50427; -.
DR PhylomeDB; P50427; -.
DR BioGRID-ORCS; 20905; 0 hits in 2 CRISPR screens.
DR PRO; PR:P50427; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P50427; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; ISO:MGI.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR GO; GO:0009268; P:response to pH; ISO:MGI.
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; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Metal-binding; Microsome; Pregnancy;
KW Reference proteome; Signal; Steroid metabolism; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..624
FT /note="Steryl-sulfatase"
FT /id="PRO_0000033415"
FT TOPO_DOM 24..192
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TRANSMEM 193..216
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TOPO_DOM 217..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT TOPO_DOM 243..624
FT /note="Lumenal"
FT /evidence="ECO:0000250, ECO:0000250|UniProtKB:P08842"
FT REGION 572..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT ACT_SITE 144
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT MOD_RES 83
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P08842"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 149..156
FT /evidence="ECO:0000250"
FT DISULFID 178..250
FT /evidence="ECO:0000250"
FT DISULFID 454..495
FT /evidence="ECO:0000250"
FT DISULFID 487..493
FT /evidence="ECO:0000250"
SQ SEQUENCE 624 AA; 66591 MW; 025C0CF8659D0A9E CRC64;
MPRPRPLLLA VMAATLADII LAADPAPAGP APRPPNFLLI MADDLGIGDL GCYGNKTLRT
PHLDRLAREG VKLTQHLAAA PLCTPSRAAF LTGRYPPRSG MAAHGRVGVY LFTASSGGLP
PSEVTMARLL KGRGYATALI GKWHLGLSCR GATDFCHHPL RHGFDRFLGV PTTNLRDCRP
GAGTVFGPAL RVFAAGPLAA LGASLAAMAA ARWAGLARVP GWALAGTAAA MLAVGGPRSA
SCLGFRPANC FLMDDLAVAQ RPTDYGGLTR RLADEAALFL RRNRARPFLL FLSFLHVHTA
HFADPGFAGR SLHGAYGDSV EEMDWGVGRV LAALDELGLA RETLVYFTSD HGAHVEELGP
RGERMGGSNG VFRGGKGNNW EGGVRVPCLV RWPRELSPGR VVAEPTSLMD VFPTVARLAG
AELPGDRVID GRDLMPLLRG DAQRSEHEFL FHYCNAYLQA VRWHNGSAVW KAFYFTPNFA
PAGANGCFST HVCLCAGPAH VTAHDPPLLF DLTRDPGERR PLTPEAEPRH REVLDAIDAA
ARAHRARLRP APDQLAPRHL MWKPWLQLWG GGGAGGGAGA QDDSGHAHGD GSHAHDDPGH
AQDRGDDDAH YGGHATTRTQ ATPR
