STS_HUMAN
ID STS_HUMAN Reviewed; 583 AA.
AC P08842; B2RA47;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Steryl-sulfatase;
DE EC=3.1.6.2 {ECO:0000269|PubMed:10844566, ECO:0000269|PubMed:23466819, ECO:0000269|PubMed:9252398};
DE AltName: Full=Arylsulfatase C;
DE Short=ASC;
DE AltName: Full=Estrone sulfatase {ECO:0000303|PubMed:12657638};
DE AltName: Full=Steroid sulfatase;
DE AltName: Full=Steryl-sulfate sulfohydrolase;
DE Flags: Precursor;
GN Name=STS; Synonyms=ARSC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT
RP ASN-47 AND ASN-259, LACK OF GLYCOSYLATION AT ASN-333 AND ASN-459,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=2668275; DOI=10.1016/s0021-9258(18)80080-1;
RA Stein C., Hille A., Seidel J., Rijnbout S., Waheed A., Schmidt B.,
RA Geuze H., von Figura K.;
RT "Cloning and expression of human steroid-sulfatase. Membrane topology,
RT glycosylation, and subcellular distribution in BHK-21 cells.";
RL J. Biol. Chem. 264:13865-13872(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3032454; DOI=10.1016/0092-8674(87)90447-8;
RA Yen P.H., Allen E., Marsh B., Mohandas T., Wang N., Taggart R.T.,
RA Shapiro L.J.;
RT "Cloning and expression of steroid sulfatase cDNA and the frequent
RT occurrence of deletions in STS deficiency: implications for X-Y
RT interchange.";
RL Cell 49:443-454(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-174 AND 461-583.
RX PubMed=3203382; DOI=10.1016/0092-8674(88)90257-7;
RA Yen P.H., Marsh B., Allen E., Tsai S.P., Ellison J., Connolly L.,
RA Neiswanger K., Shapiro L.J.;
RT "The human X-linked steroid sulfatase gene and a Y-encoded pseudogene:
RT evidence for an inversion of the Y chromosome during primate evolution.";
RL Cell 55:1123-1135(1988).
RN [6]
RP PROTEIN SEQUENCE OF 22-45.
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
RP COFACTOR, OXOALANINE AT CYS-75, TRANSMEMBRANE TOPOLOGY, ACTIVE SITE, AND
RP GLYCOSYLATION AT ASN-47 AND ASN-259.
RX PubMed=12657638; DOI=10.1074/jbc.m211497200;
RA Hernandez-Guzman F.G., Higashiyama T., Pangborn W., Osawa Y., Ghosh D.;
RT "Structure of human estrone sulfatase suggests functional roles of membrane
RT association.";
RL J. Biol. Chem. 278:22989-22997(2003).
RN [8]
RP VARIANTS IXL LEU-341; ARG-372 AND TYR-446.
RX PubMed=1539590;
RA Basler E., Grompe M., Parenti G., Yates J., Ballabio A.;
RT "Identification of point mutations in the steroid sulfatase gene of three
RT patients with X-linked ichthyosis.";
RL Am. J. Hum. Genet. 50:483-491(1992).
RN [9]
RP VARIANTS IXL LEU-341; ARG-372; SER-372; ARG-444 AND TYR-446, CATALYTIC
RP ACTIVITY, AND CHARACTERIZATION OF VARIANTS IXL LEU-341; ARG-372; SER-372;
RP ARG-444 AND TYR-446.
RX PubMed=9252398; DOI=10.1074/jbc.272.33.20756;
RA Alperin E.S., Shapiro L.J.;
RT "Characterization of point mutations in patients with X-linked ichthyosis.
RT Effects on the structure and function of the steroid sulfatase protein.";
RL J. Biol. Chem. 272:20756-20763(1997).
RN [10]
RP VARIANT IXL PRO-560.
RX PubMed=10679952;
RX DOI=10.1002/(sici)1098-1004(200003)15:3<296::aid-humu17>3.0.co;2-#;
RA Sugawara T., Shimizu H., Hoshi N., Fujimoto Y., Nakajima A., Fujimoto S.;
RT "PCR diagnosis of X-linked ichthyosis: identification of a novel mutation
RT (E560P) of the steroid sulfatase gene.";
RL Hum. Mutat. 15:296-296(2000).
RN [11]
RP VARIANT IXL ARG-380, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT.
RX PubMed=10844566; DOI=10.1046/j.1523-1747.2000.00004.x;
RA Oyama N., Satoh M., Iwatsuki K., Kaneko F.;
RT "Novel point mutations in the steroid sulfatase gene in patients with X-
RT linked ichthyosis: transfection analysis using the mutated genes.";
RL J. Invest. Dermatol. 114:1195-1199(2000).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, VARIANT MET-476, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=23466819; DOI=10.1038/jhg.2013.12;
RA Matsumoto J., Ariyoshi N., Ishii I., Kitada M.;
RT "Functional characterization of seven single-nucleotide polymorphisms of
RT the steroid sulfatase gene found in a Japanese population.";
RL J. Hum. Genet. 58:267-272(2013).
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:0000269|PubMed:10844566,
CC ECO:0000269|PubMed:23466819, ECO:0000269|PubMed:9252398}.
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:0000269|PubMed:10844566, ECO:0000269|PubMed:23466819};
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:0000269|PubMed:9252398};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12657638};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12657638};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24.8 uM for 3beta-sulfooxy-androst-5-en-17-one (DHEA-S)
CC {ECO:0000269|PubMed:23466819};
CC Vmax=354.4 umol/min/mg enzyme with 3beta-sulfooxy-androst-5-en-17-one
CC (DHEA-S) {ECO:0000269|PubMed:23466819};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12657638}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, microneme
CC membrane {ECO:0000269|PubMed:2668275}; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:2668275}; Multi-pass
CC membrane protein.
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:0000269|PubMed:12657638}.
CC -!- DISEASE: Ichthyosis, X-linked (IXL) [MIM:308100]: A keratinization
CC disorder manifesting with mild erythroderma and generalized exfoliation
CC of the skin within a few weeks after birth. Affected boys later develop
CC large, polygonal, dark brown scales, especially on the neck,
CC extremities, trunk, and buttocks. {ECO:0000269|PubMed:10679952,
CC ECO:0000269|PubMed:10844566, ECO:0000269|PubMed:1539590,
CC ECO:0000269|PubMed:9252398}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Steroid sulfatase entry;
CC URL="https://en.wikipedia.org/wiki/Steroid_sulfatase";
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DR EMBL; J04964; AAA60597.1; -; mRNA.
DR EMBL; M16505; AAA60596.1; -; mRNA.
DR EMBL; AK314034; BAG36744.1; -; mRNA.
DR EMBL; BC075030; AAH75030.1; -; mRNA.
DR EMBL; M23945; AAA60598.1; -; Genomic_DNA.
DR EMBL; M23556; AAA60599.1; -; Genomic_DNA.
DR PIR; A32641; KJHUAC.
DR RefSeq; NP_000342.2; NM_000351.5.
DR RefSeq; NP_001307679.1; NM_001320750.1.
DR RefSeq; NP_001307680.1; NM_001320751.1.
DR RefSeq; NP_001307681.1; NM_001320752.1.
DR RefSeq; NP_001307682.1; NM_001320753.1.
DR RefSeq; NP_001307683.1; NM_001320754.1.
DR PDB; 1P49; X-ray; 2.60 A; A=22-583.
DR PDBsum; 1P49; -.
DR AlphaFoldDB; P08842; -.
DR SMR; P08842; -.
DR BioGRID; 106905; 36.
DR IntAct; P08842; 22.
DR MINT; P08842; -.
DR STRING; 9606.ENSP00000217961; -.
DR BindingDB; P08842; -.
DR ChEMBL; CHEMBL3559; -.
DR DrugBank; DB02735; 2-Amino-3-Oxo-4-Sulfo-Butyric Acid.
DR DrugBank; DB02292; Irosustat.
DR DrugBank; DB06713; Norelgestromin.
DR DrugBank; DB09070; Tibolone.
DR DrugCentral; P08842; -.
DR SwissLipids; SLP:000001236; -.
DR GlyConnect; 1770; 2 N-Linked glycans (1 site).
DR GlyGen; P08842; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P08842; -.
DR PhosphoSitePlus; P08842; -.
DR SwissPalm; P08842; -.
DR BioMuta; STS; -.
DR DMDM; 135006; -.
DR EPD; P08842; -.
DR jPOST; P08842; -.
DR MassIVE; P08842; -.
DR MaxQB; P08842; -.
DR PaxDb; P08842; -.
DR PeptideAtlas; P08842; -.
DR PRIDE; P08842; -.
DR ProteomicsDB; 52168; -.
DR Antibodypedia; 363; 262 antibodies from 32 providers.
DR DNASU; 412; -.
DR GeneID; 412; -.
DR KEGG; hsa:412; -.
DR UCSC; uc004cry.5; human.
DR CTD; 412; -.
DR DisGeNET; 412; -.
DR GeneCards; STS; -.
DR HGNC; HGNC:11425; STS.
DR HPA; ENSG00000101846; Tissue enhanced (placenta).
DR MalaCards; STS; -.
DR MIM; 300747; gene.
DR MIM; 308100; phenotype.
DR neXtProt; NX_P08842; -.
DR Orphanet; 461; Recessive X-linked ichthyosis.
DR Orphanet; 281090; Syndromic recessive X-linked ichthyosis.
DR PharmGKB; PA36225; -.
DR VEuPathDB; HostDB:ENSG00000101846; -.
DR eggNOG; KOG3867; Eukaryota.
DR HOGENOM; CLU_006332_13_4_1; -.
DR InParanoid; P08842; -.
DR OMA; VFQIHKY; -.
DR OrthoDB; 873694at2759; -.
DR PhylomeDB; P08842; -.
DR TreeFam; TF314186; -.
DR BRENDA; 3.1.6.2; 2681.
DR PathwayCommons; P08842; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-1663150; The activation of arylsulfatases.
DR SignaLink; P08842; -.
DR BioGRID-ORCS; 412; 8 hits in 703 CRISPR screens.
DR ChiTaRS; STS; human.
DR EvolutionaryTrace; P08842; -.
DR GeneWiki; Steroid_sulfatase; -.
DR GenomeRNAi; 412; -.
DR Pharos; P08842; Tchem.
DR PRO; PR:P08842; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P08842; protein.
DR Bgee; ENSG00000101846; Expressed in placenta and 178 other tissues.
DR ExpressionAtlas; P08842; baseline and differential.
DR Genevisible; P08842; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005768; C:endosome; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
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; TAS:ProtInc.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IDA:MGI.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR GO; GO:0006706; P:steroid catabolic process; TAS:ProtInc.
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 3D-structure; Calcium; Cytoplasmic vesicle; Direct protein sequencing;
KW Disease variant; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Ichthyosis; Lipid metabolism; Membrane; Metal-binding;
KW Pregnancy; Reference proteome; Signal; Steroid metabolism; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2765556"
FT CHAIN 22..583
FT /note="Steryl-sulfatase"
FT /id="PRO_0000033414"
FT TOPO_DOM 22..184
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:2668275"
FT TRANSMEM 185..208
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:2668275"
FT TOPO_DOM 209..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2668275"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:2668275"
FT TOPO_DOM 235..583
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:2668275"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:12657638"
FT ACT_SITE 136
FT /evidence="ECO:0000269|PubMed:12657638"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12657638"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12657638"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000269|PubMed:12657638"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12657638"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12657638"
FT SITE 333
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:2668275"
FT SITE 459
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:2668275"
FT MOD_RES 75
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000269|PubMed:12657638"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12657638,
FT ECO:0000269|PubMed:2668275"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12657638,
FT ECO:0000269|PubMed:2668275"
FT DISULFID 141..148
FT DISULFID 170..242
FT DISULFID 446..489
FT DISULFID 481..487
FT DISULFID 562..570
FT DISULFID 563..572
FT VARIANT 341
FT /note="S -> L (in IXL; loss of steryl-sulfatase activity;
FT dbSNP:rs137853167)"
FT /evidence="ECO:0000269|PubMed:1539590,
FT ECO:0000269|PubMed:9252398"
FT /id="VAR_007240"
FT VARIANT 372
FT /note="W -> R (in IXL; loss of steryl-sulfatase activity;
FT dbSNP:rs137853165)"
FT /evidence="ECO:0000269|PubMed:1539590,
FT ECO:0000269|PubMed:9252398"
FT /id="VAR_007241"
FT VARIANT 372
FT /note="W -> S (in IXL; loss of steryl-sulfatase activity;
FT dbSNP:rs137853168)"
FT /evidence="ECO:0000269|PubMed:9252398"
FT /id="VAR_014020"
FT VARIANT 380
FT /note="G -> R (in IXL; strong decreases of steryl-sulfatase
FT activity)"
FT /evidence="ECO:0000269|PubMed:10844566"
FT /id="VAR_014021"
FT VARIANT 444
FT /note="H -> R (in IXL; loss of steryl-sulfatase activity;
FT dbSNP:rs137853169)"
FT /evidence="ECO:0000269|PubMed:9252398"
FT /id="VAR_014022"
FT VARIANT 446
FT /note="C -> Y (in IXL; loss of steryl-sulfatase activity;
FT dbSNP:rs137853166)"
FT /evidence="ECO:0000269|PubMed:1539590,
FT ECO:0000269|PubMed:9252398"
FT /id="VAR_007242"
FT VARIANT 476
FT /note="V -> M (does not affect steryl-sulfatase activity;
FT dbSNP:rs183370963)"
FT /evidence="ECO:0000269|PubMed:23466819"
FT /id="VAR_081729"
FT VARIANT 560
FT /note="Q -> P (in IXL)"
FT /evidence="ECO:0000269|PubMed:10679952"
FT /id="VAR_014023"
FT CONFLICT 23
FT /note="A -> E (in Ref. 2; AAA60596)"
FT /evidence="ECO:0000305"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 187..205
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 213..241
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 307..328
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 335..343
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:1P49"
FT TURN 518..521
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 523..537
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:1P49"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1P49"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:1P49"
SQ SEQUENCE 583 AA; 65492 MW; 74746AFA9D21A0A6 CRC64;
MPLRKMKIPF LLLFFLWEAE SHAASRPNII LVMADDLGIG DPGCYGNKTI RTPNIDRLAS
GGVKLTQHLA ASPLCTPSRA AFMTGRYPVR SGMASWSRTG VFLFTASSGG LPTDEITFAK
LLKDQGYSTA LIGKWHLGMS CHSKTDFCHH PLHHGFNYFY GISLTNLRDC KPGEGSVFTT
GFKRLVFLPL QIVGVTLLTL AALNCLGLLH VPLGVFFSLL FLAALILTLF LGFLHYFRPL
NCFMMRNYEI IQQPMSYDNL TQRLTVEAAQ FIQRNTETPF LLVLSYLHVH TALFSSKDFA
GKSQHGVYGD AVEEMDWSVG QILNLLDELR LANDTLIYFT SDQGAHVEEV SSKGEIHGGS
NGIYKGGKAN NWEGGIRVPG ILRWPRVIQA GQKIDEPTSN MDIFPTVAKL AGAPLPEDRI
IDGRDLMPLL EGKSQRSDHE FLFHYCNAYL NAVRWHPQNS TSIWKAFFFT PNFNPVGSNG
CFATHVCFCF GSYVTHHDPP LLFDISKDPR ERNPLTPASE PRFYEILKVM QEAADRHTQT
LPEVPDQFSW NNFLWKPWLQ LCCPSTGLSC QCDREKQDKR LSR
