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Protein

Steryl-sulfatase

Gene

Sts

Organism
Rattus norvegicus (Rat)
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+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341CalciumBy similarity
Metal bindingi35 – 351CalciumBy similarity
Metal bindingi74 – 741Calcium; via 3-oxoalanineBy similarity
Active sitei135 – 1351By similarity
Metal bindingi341 – 3411CalciumBy similarity
Metal bindingi342 – 3421CalciumBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • steryl-sulfatase activity Source: RGD

GO - Biological processi

  • female pregnancy Source: UniProtKB-KW
  • learning or memory Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • response to estrogen Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to pH Source: RGD
  • skin development Source: RGD
  • steroid metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism, Pregnancy, Steroid metabolism

Keywords - Ligandi

Calcium, Metal-binding

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3783. Sts.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 183163LumenalBy similarityAdd
BLAST
Transmembranei184 – 20724HelicalBy similarityAdd
BLAST
Topological domaini208 – 2114CytoplasmicBy similarity
Transmembranei212 – 23322HelicalBy similarityAdd
BLAST
Topological domaini234 – 577344LumenalBy similarityAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: RGD
  • integral component of membrane Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
  • nuclear envelope Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3531.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 577558Steryl-sulfatasePRO_0000033416Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Modified residuei74 – 7413-oxoalanine (Cys)By similarity
Disulfide bondi140 ↔ 147By similarity
Disulfide bondi169 ↔ 241By similarity
Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence analysis
Disulfide bondi445 ↔ 488By similarity
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence analysis
Disulfide bondi480 ↔ 486By similarity
Disulfide bondi561 ↔ 571By similarity

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15589.
PRIDEiP15589.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

MINTiMINT-4568201.
STRINGi10116.ENSRNOP00000043915.

Chemistry

BindingDBiP15589.

Structurei

3D structure databases

ProteinModelPortaliP15589.
SMRiP15589. Positions 26-573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP15589.
KOiK01131.
PhylomeDBiP15589.

Family and domain databases

Gene3Di3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWPCLLALL LSQLNFLCAA RPGPGPNFLL IMADDLGIGD LGCYGNRTLR
60 70 80 90 100
TPHIDRLALE GVKLTQHLAA APLCTPSRAA FLTGRYPVRS GMASHGRLGV
110 120 130 140 150
FLFSASSGGL PPNEVTFAKL LKGQGYTTGL VGKWHLGLSC QAASDFCHHP
160 170 180 190 200
GRHGFDRFLG TPTTNLRDCK PGGGTVFGSA QQVFVVLPMN ILGAVLLAMA
210 220 230 240 250
LARWAGLARP PGWVFGVTVA AMAAVGGAYV AFLYHFRPAN CFLMADFTIT
260 270 280 290 300
QQPTDYKGLT QRLASEAGDF LRRNRDTPFL LFLSFMHVHT AHFANPEFAG
310 320 330 340 350
QSLHGAYGDA VEEMDWAVGQ VLATLDKLGL ANNTLVYLTS DHGAHVEELG
360 370 380 390 400
PNGERHGGSN GIYRGGKANT WEGGIRVPGL VRWPGVIVPG QEVEEPTSNM
410 420 430 440 450
DVFPTVARLA GAELPTDRVI DGRDLMPLLL GHVQHSEHEF LFHYCNAYLS
460 470 480 490 500
AVAWRPHNSS SVWKAFYFTP NFDPPGSNGC FSTHVCMCHG HHVTHHDPPL
510 520 530 540 550
LFDIARDPRE RHPLTPETEP RHGEILRNMD AAARAHVATL EEAPNQLSMS
560 570
NVAWKPWLQL CLPSKPHPLA CRCAGDG
Length:577
Mass (Da):62,679
Last modified:October 1, 1996 - v2
Checksum:i07562EADEDCDB716
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37138 mRNA. Translation: AAC53097.1.
PIRiS05414.
RefSeqiNP_036793.1. NM_012661.1.
UniGeneiRn.6312.

Genome annotation databases

GeneIDi24800.
KEGGirno:24800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37138 mRNA. Translation: AAC53097.1.
PIRiS05414.
RefSeqiNP_036793.1. NM_012661.1.
UniGeneiRn.6312.

3D structure databases

ProteinModelPortaliP15589.
SMRiP15589. Positions 26-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4568201.
STRINGi10116.ENSRNOP00000043915.

Chemistry

BindingDBiP15589.
ChEMBLiCHEMBL3531.

Proteomic databases

PaxDbiP15589.
PRIDEiP15589.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24800.
KEGGirno:24800.

Organism-specific databases

CTDi412.
RGDi3783. Sts.

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP15589.
KOiK01131.
PhylomeDBiP15589.

Miscellaneous databases

PROiP15589.

Family and domain databases

Gene3Di3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Li X.M., Salido E.C., Gong Y., Yen P.H., Kitada Y., Serikawa T., Shapiro L.J.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. Cited for: PROTEIN SEQUENCE OF 20-45.
    Tissue: Liver.

Entry informationi

Entry nameiSTS_RAT
AccessioniPrimary (citable) accession number: P15589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.