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UniProtKB - P08842 (STS_HUMAN)

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Protein

Steryl-sulfatase

Gene

STS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of sulfated steroid precursors to estrogens during pregnancy.

Catalytic activityi

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

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi35Calcium1 Publication1
Metal bindingi36Calcium1 Publication1
Metal bindingi75Calcium; via 3-oxoalanine1 Publication1
Active sitei1361 Publication1
Metal bindingi342Calcium1 Publication1
Metal bindingi343Calcium1 Publication1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • steryl-sulfatase activity Source: Reactome
  • sulfuric ester hydrolase activity Source: MGI
Complete GO annotation...

GO - Biological processi

  • epidermis development Source: ProtInc
  • female pregnancy Source: UniProtKB-KW
  • glycosphingolipid metabolic process Source: Reactome
  • post-translational protein modification Source: Reactome
  • steroid catabolic process Source: ProtInc
Complete GO annotation...

Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism, Pregnancy, Steroid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.6.2. 2681.
ReactomeiR-HSA-1660662. Glycosphingolipid metabolism.
R-HSA-1663150. The activation of arylsulfatases.

Chemistry databases

SwissLipidsiSLP:000001236.

Names & Taxonomyi

Protein namesi
Recommended name:
Steryl-sulfatase (EC:3.1.6.2)
Alternative name(s):
Arylsulfatase C
Short name:
ASC
Steroid sulfatase
Steryl-sulfate sulfohydrolase
Gene namesi
Name:STS
Synonyms:ARSC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11425. STS.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 184LumenalAdd BLAST163
Transmembranei185 – 208HelicalAdd BLAST24
Topological domaini209 – 212Cytoplasmic4
Transmembranei213 – 234HelicalAdd BLAST22
Topological domaini235 – 583LumenalAdd BLAST349

GO - Cellular componenti

  • endoplasmic reticulum Source: ProtInc
  • endoplasmic reticulum lumen Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • endosome Source: ProtInc
  • Golgi apparatus Source: ProtInc
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: ProtInc
  • lysosome Source: ProtInc
  • membrane Source: ProtInc
  • plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Ichthyosis, X-linked (IXL)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:308100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007240341S → L in IXL; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137853167Ensembl.1
Natural variantiVAR_007241372W → R in IXL; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137853165Ensembl.1
Natural variantiVAR_014020372W → S in IXL; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs137853168Ensembl.1
Natural variantiVAR_014021380G → R in IXL. 1 Publication1
Natural variantiVAR_014022444H → R in IXL; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs137853169Ensembl.1
Natural variantiVAR_007242446C → Y in IXL; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137853166Ensembl.1
Natural variantiVAR_014023560Q → P in IXL. 1 Publication1

Keywords - Diseasei

Disease mutation, Ichthyosis

Organism-specific databases

DisGeNETi412.
MalaCardsiSTS.
MIMi308100. phenotype.
OpenTargetsiENSG00000101846.
Orphaneti461. Recessive X-linked ichthyosis.
281090. Syndromic X-linked ichthyosis.
PharmGKBiPA36225.

Chemistry databases

ChEMBLiCHEMBL3559.
DrugBankiDB02735. 2-Amino-3-Oxo-4-Sulfo-Butyric Acid.
DB06713. Norelgestromin.

Polymorphism and mutation databases

BioMutaiSTS.
DMDMi135006.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000003341422 – 583Steryl-sulfataseAdd BLAST562

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi47N-linked (GlcNAc...) asparagine2 Publications1
Modified residuei753-oxoalanine (Cys)1 Publication1
Disulfide bondi141 ↔ 148
Disulfide bondi170 ↔ 242
Glycosylationi259N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi446 ↔ 489
Disulfide bondi481 ↔ 487
Disulfide bondi562 ↔ 570
Disulfide bondi563 ↔ 572

Post-translational modificationi

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei333Not glycosylated1 Publication1
Sitei459Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP08842.
MaxQBiP08842.
PaxDbiP08842.
PeptideAtlasiP08842.
PRIDEiP08842.

PTM databases

iPTMnetiP08842.
PhosphoSitePlusiP08842.
SwissPalmiP08842.

Expressioni

Gene expression databases

BgeeiENSG00000101846.
CleanExiHS_STS.
GenevisibleiP08842. HS.

Organism-specific databases

HPAiHPA002904.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi106905. 21 interactors.
IntActiP08842. 1 interactor.
MINTiMINT-1177440.
STRINGi9606.ENSP00000217961.

Chemistry databases

BindingDBiP08842.

Structurei

Secondary structure

1583
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 36Combined sources9
Helixi43 – 45Combined sources3
Beta strandi48 – 50Combined sources3
Helixi53 – 56Combined sources4
Turni57 – 61Combined sources5
Beta strandi62 – 69Combined sources8
Helixi75 – 84Combined sources10
Helixi88 – 91Combined sources4
Beta strandi96 – 98Combined sources3
Helixi118 – 124Combined sources7
Beta strandi128 – 134Combined sources7
Beta strandi141 – 143Combined sources3
Turni144 – 146Combined sources3
Helixi151 – 153Combined sources3
Beta strandi157 – 164Combined sources8
Helixi168 – 170Combined sources3
Helixi179 – 185Combined sources7
Helixi187 – 205Combined sources19
Helixi213 – 241Combined sources29
Beta strandi244 – 246Combined sources3
Beta strandi249 – 254Combined sources6
Helixi260 – 273Combined sources14
Turni274 – 277Combined sources4
Beta strandi280 – 285Combined sources6
Beta strandi290 – 292Combined sources3
Turni297 – 299Combined sources3
Beta strandi304 – 306Combined sources3
Helixi307 – 328Combined sources22
Helixi332 – 334Combined sources3
Beta strandi335 – 343Combined sources9
Beta strandi352 – 354Combined sources3
Beta strandi370 – 372Combined sources3
Helixi373 – 376Combined sources4
Beta strandi380 – 383Combined sources4
Turni385 – 387Combined sources3
Helixi400 – 402Combined sources3
Helixi403 – 411Combined sources9
Beta strandi417 – 419Combined sources3
Helixi427 – 430Combined sources4
Beta strandi440 – 446Combined sources7
Beta strandi449 – 455Combined sources7
Beta strandi464 – 468Combined sources5
Turni482 – 484Combined sources3
Beta strandi489 – 491Combined sources3
Beta strandi501 – 503Combined sources3
Turni505 – 507Combined sources3
Turni518 – 521Combined sources4
Helixi523 – 537Combined sources15
Helixi550 – 553Combined sources4
Helixi557 – 559Combined sources3
Beta strandi563 – 568Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P49X-ray2.60A22-583[»]
ProteinModelPortaliP08842.
SMRiP08842.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08842.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP08842.
KOiK01131.
OMAiFATHVCF.
OrthoDBiEOG091G07AL.
PhylomeDBiP08842.
TreeFamiTF314186.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiView protein in InterPro
IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
PfamiView protein in Pfam
PF00884. Sulfatase. 1 hit.
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiView protein in PROSITE
PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08842-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLRKMKIPF LLLFFLWEAE SHAASRPNII LVMADDLGIG DPGCYGNKTI 
        60         70         80         90        100
RTPNIDRLAS GGVKLTQHLA ASPLCTPSRA AFMTGRYPVR SGMASWSRTG 
       110        120        130        140        150
VFLFTASSGG LPTDEITFAK LLKDQGYSTA LIGKWHLGMS CHSKTDFCHH 
       160        170        180        190        200
PLHHGFNYFY GISLTNLRDC KPGEGSVFTT GFKRLVFLPL QIVGVTLLTL 
       210        220        230        240        250
AALNCLGLLH VPLGVFFSLL FLAALILTLF LGFLHYFRPL NCFMMRNYEI 
       260        270        280        290        300
IQQPMSYDNL TQRLTVEAAQ FIQRNTETPF LLVLSYLHVH TALFSSKDFA 
       310        320        330        340        350
GKSQHGVYGD AVEEMDWSVG QILNLLDELR LANDTLIYFT SDQGAHVEEV 
       360        370        380        390        400
SSKGEIHGGS NGIYKGGKAN NWEGGIRVPG ILRWPRVIQA GQKIDEPTSN 
       410        420        430        440        450
MDIFPTVAKL AGAPLPEDRI IDGRDLMPLL EGKSQRSDHE FLFHYCNAYL 
       460        470        480        490        500
NAVRWHPQNS TSIWKAFFFT PNFNPVGSNG CFATHVCFCF GSYVTHHDPP 
       510        520        530        540        550
LLFDISKDPR ERNPLTPASE PRFYEILKVM QEAADRHTQT LPEVPDQFSW 
       560        570        580 
NNFLWKPWLQ LCCPSTGLSC QCDREKQDKR LSR
Length:583
Mass (Da):65,492
Last modified:April 1, 1990 - v2
Checksum:i74746AFA9D21A0A6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23A → E in AAA60596 (PubMed:3032454).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007240341S → L in IXL; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137853167Ensembl.1
Natural variantiVAR_007241372W → R in IXL; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137853165Ensembl.1
Natural variantiVAR_014020372W → S in IXL; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs137853168Ensembl.1
Natural variantiVAR_014021380G → R in IXL. 1 Publication1
Natural variantiVAR_014022444H → R in IXL; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs137853169Ensembl.1
Natural variantiVAR_007242446C → Y in IXL; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs137853166Ensembl.1
Natural variantiVAR_014023560Q → P in IXL. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14127.1.
PIRiA32641. KJHUAC.
RefSeqiNP_000342.2. NM_000351.5.
NP_001307679.1. NM_001320750.1.
NP_001307680.1. NM_001320751.1.
NP_001307681.1. NM_001320752.1.
NP_001307682.1. NM_001320753.1.
NP_001307683.1. NM_001320754.1.
UniGeneiHs.522578.
Hs.700558.
Hs.700559.
Hs.740067.

Genome annotation databases

EnsembliENST00000217961; ENSP00000217961; ENSG00000101846.
GeneIDi412.
KEGGihsa:412.
UCSCiuc004cry.5. human.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiSTS_HUMAN
AccessioniPrimary (citable) accession number: P08842
Secondary accession number(s): B2RA47
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 1, 1990
Last modified: June 7, 2017
This is version 180 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families