P14217 · ARS_CHLRE

Function

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.

Features

Showing features for binding site, active site.

164750100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site35Ca2+ (UniProtKB | ChEBI)
Binding site36Ca2+ (UniProtKB | ChEBI)
Active site73Nucleophile
Binding site73Ca2+ (UniProtKB | ChEBI); via 3-oxoalanine
Binding site323Ca2+ (UniProtKB | ChEBI)
Binding site324Ca2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionarylsulfatase activity
Molecular Functionmetal ion binding
Biological Processphenol-containing compound metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Arylsulfatase
  • EC number
  • Short names
    AS
  • Alternative names
    • Aryl-sulfate sulphohydrolase

Gene names

    • Name
      AS

Organism names

Accessions

  • Primary accession
    P14217

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000003344422-647Arylsulfatase
Glycosylation42N-linked (GlcNAc...) asparagine
Modified residue733-oxoalanine (Cys)
Glycosylation90N-linked (GlcNAc...) asparagine
Glycosylation279N-linked (GlcNAc...) asparagine
Glycosylation444N-linked (GlcNAc...) asparagine
Glycosylation528N-linked (GlcNAc...) asparagine

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.

Keywords

Proteomic databases

PTM databases

Expression

Induction

By sulfur deprivation.

Family & Domains

Sequence similarities

Belongs to the sulfatase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    647
  • Mass (Da)
    72,106
  • Last updated
    1996-10-01 v2
  • Checksum
    7404EA1BF233F0B1
MGALAVFAVACLAAVASVAHAADTKKPNFVVIFTDDQDAIQNSTHPHYMPSLHKYIRYPGVELSQYFVTTPVCCPSRTNLXRGQFAHNTNFTSVLPPYGGWAKWKGLGIDQSYLPLWLKDQGYNTYYVGKFLVDYSVSNYQQVPRAGTISMPXVTPYTFDYNTRLQRNGATPNIYPGEYSTDVIRDKGVAQIKSAVAAGKPFYAQISPIAPHTSTQISTNPATGVTRSYFFPPIPAPPHWQLFSDANLPGGSXNKNLYEVDVSDKPAWIRALPLAQQNNRTYQEEIYRLRLRSLGPDELIEQVVKTLDEAGVLDNTYIIYSADNGYHVGAHRFGAGKTTGYEEDLRVPFLIRGPGIKASKSDKPQNSKVGLHVDFAPTILSLAGASHLLGDKGLDGTPLGLYANDDGTLPSDYPRPEQHRQQFQGEFWGGWSDELLQNLRSQPNNTWKVVRTYDESSKQGWKLIAQCTNERELYDLRKDPGELYNIYDKAKPAVRSRLEGLLAVLAVCKGESCSNPWKILHPDGTVKNFTQALNSKYDRIYNAIRPFTYKRCLPYLDWDNEDSQFKTQIRGANPAAGVGHHRLLTAASERAIATRRRAQAAVSAELADGPAVFQAKVEEKSVPVPQDILKADVEKWFAFNNAEYYLA

Sequence caution

The sequence CAA34302.1 differs from that shown. Reason: Frameshift
The sequence CAA36545.1 differs from that shown. Reason: Frameshift

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X16180
EMBL· GenBank· DDBJ
CAA34302.1
EMBL· GenBank· DDBJ
mRNA Frameshift
X52304
EMBL· GenBank· DDBJ
CAA36545.1
EMBL· GenBank· DDBJ
mRNA Frameshift
X16179
EMBL· GenBank· DDBJ
CAA34301.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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