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P08842 (STS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Steryl-sulfatase

EC=3.1.6.2
Alternative name(s):
Arylsulfatase C
Short name=ASC
Steroid sulfatase
Steryl-sulfate sulfohydrolase
Gene names
Name:STS
Synonyms:ARSC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conversion of sulfated steroid precursors to estrogens during pregnancy.

Catalytic activity

3-beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3-beta-hydroxyandrost-5-en-17-one + sulfate.

Cofactor

Binds 1 calcium ion per subunit. Ref.7

Subunit structure

Homodimer.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Post-translational modification

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity By similarity.

Involvement in disease

Ichthyosis, X-linked (IXL) [MIM:308100]: A keratinization disorder manifesting with mild erythroderma and generalized exfoliation of the skin within a few weeks after birth. Affected boys later develop large, polygonal, dark brown scales, especially on the neck, extremities, trunk, and buttocks.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the sulfatase family.

Ontologies

Keywords
   Biological processLipid metabolism
Pregnancy
Steroid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DiseaseDisease mutation
Ichthyosis
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

epidermis development

Traceable author statement Ref.9. Source: ProtInc

female pregnancy

Inferred from electronic annotation. Source: UniProtKB-KW

glycosphingolipid metabolic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

steroid catabolic process

Traceable author statement PubMed 6957717. Source: ProtInc

   Cellular_componentGolgi apparatus

Traceable author statement Ref.1. Source: ProtInc

endoplasmic reticulum

Traceable author statement Ref.1. Source: ProtInc

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

endosome

Traceable author statement Ref.1. Source: ProtInc

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Traceable author statement PubMed 6957717. Source: ProtInc

lysosome

Traceable author statement Ref.1. Source: ProtInc

membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

steryl-sulfatase activity

Traceable author statement. Source: Reactome

sulfuric ester hydrolase activity

Inferred from direct assay PubMed 15962010. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.6
Chain22 – 583562Steryl-sulfatase
PRO_0000033414

Regions

Topological domain22 – 184163Lumenal Ref.7
Transmembrane185 – 20824Helical
Topological domain209 – 2124Cytoplasmic Ref.7
Transmembrane213 – 23422Helical
Topological domain235 – 583349Lumenal Ref.7

Sites

Active site1361 Ref.7
Metal binding351Calcium
Metal binding361Calcium
Metal binding751Calcium; via 3-oxoalanine
Metal binding3421Calcium
Metal binding3431Calcium
Site3331Not glycosylated
Site4591Not glycosylated

Amino acid modifications

Modified residue7513-oxoalanine (Cys)
Glycosylation471N-linked (GlcNAc...) Ref.1 Ref.7
Glycosylation2591N-linked (GlcNAc...) Ref.1 Ref.7
Disulfide bond141 ↔ 148
Disulfide bond170 ↔ 242
Disulfide bond446 ↔ 489
Disulfide bond481 ↔ 487
Disulfide bond562 ↔ 570
Disulfide bond563 ↔ 572

Natural variations

Natural variant3411S → L in IXL; loss of activity. Ref.8 Ref.9
VAR_007240
Natural variant3721W → R in IXL; loss of activity. Ref.8 Ref.9
VAR_007241
Natural variant3721W → S in IXL; loss of activity. Ref.9
VAR_014020
Natural variant3801G → R in IXL. Ref.11
VAR_014021
Natural variant4441H → R in IXL; loss of activity. Ref.9
VAR_014022
Natural variant4461C → Y in IXL; loss of activity. Ref.8 Ref.9
VAR_007242
Natural variant5601Q → P in IXL. Ref.10
VAR_014023

Experimental info

Sequence conflict231A → E in AAA60596. Ref.2

Secondary structure

............................................................................................... 583
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08842 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 74746AFA9D21A0A6

FASTA58365,492
        10         20         30         40         50         60 
MPLRKMKIPF LLLFFLWEAE SHAASRPNII LVMADDLGIG DPGCYGNKTI RTPNIDRLAS 

        70         80         90        100        110        120 
GGVKLTQHLA ASPLCTPSRA AFMTGRYPVR SGMASWSRTG VFLFTASSGG LPTDEITFAK 

       130        140        150        160        170        180 
LLKDQGYSTA LIGKWHLGMS CHSKTDFCHH PLHHGFNYFY GISLTNLRDC KPGEGSVFTT 

       190        200        210        220        230        240 
GFKRLVFLPL QIVGVTLLTL AALNCLGLLH VPLGVFFSLL FLAALILTLF LGFLHYFRPL 

       250        260        270        280        290        300 
NCFMMRNYEI IQQPMSYDNL TQRLTVEAAQ FIQRNTETPF LLVLSYLHVH TALFSSKDFA 

       310        320        330        340        350        360 
GKSQHGVYGD AVEEMDWSVG QILNLLDELR LANDTLIYFT SDQGAHVEEV SSKGEIHGGS 

       370        380        390        400        410        420 
NGIYKGGKAN NWEGGIRVPG ILRWPRVIQA GQKIDEPTSN MDIFPTVAKL AGAPLPEDRI 

       430        440        450        460        470        480 
IDGRDLMPLL EGKSQRSDHE FLFHYCNAYL NAVRWHPQNS TSIWKAFFFT PNFNPVGSNG 

       490        500        510        520        530        540 
CFATHVCFCF GSYVTHHDPP LLFDISKDPR ERNPLTPASE PRFYEILKVM QEAADRHTQT 

       550        560        570        580 
LPEVPDQFSW NNFLWKPWLQ LCCPSTGLSC QCDREKQDKR LSR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells."
Stein C., Hille A., Seidel J., Rijnbout S., Waheed A., Schmidt B., Geuze H., von Figura K.
J. Biol. Chem. 264:13865-13872(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-47 AND ASN-259, LACK OF GLYCOSYLATION AT ASN-333 AND ASN-459.
[2]"Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange."
Yen P.H., Allen E., Marsh B., Mohandas T., Wang N., Taggart R.T., Shapiro L.J.
Cell 49:443-454(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution."
Yen P.H., Marsh B., Allen E., Tsai S.P., Ellison J., Connolly L., Neiswanger K., Shapiro L.J.
Cell 55:1123-1135(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-174 AND 461-583.
[6]"Characterization of rat and human steroid sulfatases."
Kawano J., Kotani T., Ohtaki S., Minamino N., Matsuo H., Oinuma T., Aikawa E.
Biochim. Biophys. Acta 997:199-205(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-45.
Tissue: Liver.
[7]"Structure of human estrone sulfatase suggests functional roles of membrane association."
Hernandez-Guzman F.G., Higashiyama T., Pangborn W., Osawa Y., Ghosh D.
J. Biol. Chem. 278:22989-22997(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, COFACTOR, TRANSMEMBRANE TOPOLOGY, ACTIVE SITE, GLYCOSYLATION AT ASN-47 AND ASN-259.
[8]"Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis."
Basler E., Grompe M., Parenti G., Yates J., Ballabio A.
Am. J. Hum. Genet. 50:483-491(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IXL LEU-341; ARG-372 AND TYR-446.
[9]"Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein."
Alperin E.S., Shapiro L.J.
J. Biol. Chem. 272:20756-20763(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IXL LEU-341; ARG-372; SER-372; ARG-444 AND TYR-446.
[10]"PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene."
Sugawara T., Shimizu H., Hoshi N., Fujimoto Y., Nakajima A., Fujimoto S.
Hum. Mutat. 15:296-296(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IXL PRO-560.
[11]"Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes."
Oyama N., Satoh M., Iwatsuki K., Kaneko F.
J. Invest. Dermatol. 114:1195-1199(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IXL ARG-380.
+Additional computationally mapped references.

Web resources

Wikipedia

Steroid sulfatase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04964 mRNA. Translation: AAA60597.1.
M16505 mRNA. Translation: AAA60596.1.
AK314034 mRNA. Translation: BAG36744.1.
BC075030 mRNA. Translation: AAH75030.1.
M23945 Genomic DNA. Translation: AAA60598.1.
M23556 Genomic DNA. Translation: AAA60599.1.
CCDSCCDS14127.1.
PIRKJHUAC. A32641.
RefSeqNP_000342.2. NM_000351.4.
UniGeneHs.522578.
Hs.700558.
Hs.700559.
Hs.740067.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P49X-ray2.60A22-583[»]
ProteinModelPortalP08842.
SMRP08842. Positions 23-575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08842. 1 interaction.
MINTMINT-1177440.
STRING9606.ENSP00000217961.

Chemistry

BindingDBP08842.
ChEMBLCHEMBL3559.
DrugBankDB00655. Estrone.

PTM databases

PhosphoSiteP08842.

Polymorphism databases

DMDM135006.

Proteomic databases

MaxQBP08842.
PaxDbP08842.
PRIDEP08842.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217961; ENSP00000217961; ENSG00000101846.
GeneID412.
KEGGhsa:412.
UCSCuc004cry.4. human.

Organism-specific databases

CTD412.
GeneCardsGC0XP007147.
HGNCHGNC:11425. STS.
HPAHPA002904.
MIM300747. gene.
308100. phenotype.
neXtProtNX_P08842.
Orphanet461. Recessive X-linked ichthyosis.
281090. Syndromic X-linked ichthyosis.
PharmGKBPA36225.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000135352.
HOVERGENHBG004283.
InParanoidP08842.
KOK01131.
OMAGLSCQCD.
OrthoDBEOG7QZG9J.
PhylomeDBP08842.
TreeFamTF314186.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.

Gene expression databases

BgeeP08842.
CleanExHS_STS.
GenevestigatorP08842.

Family and domain databases

Gene3D3.40.720.10. 2 hits.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08842.
GeneWikiSteroid_sulfatase.
GenomeRNAi412.
NextBio1743.
PROP08842.
SOURCESearch...

Entry information

Entry nameSTS_HUMAN
AccessionPrimary (citable) accession number: P08842
Secondary accession number(s): B2RA47
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM