Q32KH2 · Q32KH2_CANLF

Function

function

Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin.

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site51Ca2+ (UniProtKB | ChEBI)
Binding site52Ca2+ (UniProtKB | ChEBI)
Active site87Nucleophile
Binding site87Ca2+ (UniProtKB | ChEBI); via 3-oxoalanine
Binding site316Ca2+ (UniProtKB | ChEBI)
Binding site317Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell surface
Cellular Componentendoplasmic reticulum
Cellular Componentextracellular space
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi stack
Cellular Componentmembrane raft
Molecular Functionarylsulfatase activity
Molecular Functioncalcium ion binding
Molecular FunctionN-acetylglucosamine-6-sulfatase activity
Biological Processbone development
Biological Processcartilage condensation
Biological Processcartilage development
Biological Processcell adhesion
Biological Processchondrocyte development
Biological Processembryonic skeletal system development
Biological Processesophagus smooth muscle contraction
Biological Processglial cell-derived neurotrophic factor receptor signaling pathway
Biological Processheparan sulfate proteoglycan metabolic process
Biological Processinnervation
Biological Processkidney development
Biological Processlimb joint morphogenesis
Biological Processnegative regulation of angiogenesis
Biological Processnegative regulation of cell migration
Biological Processnegative regulation of endothelial cell proliferation
Biological Processnegative regulation of fibroblast growth factor receptor signaling pathway
Biological Processnegative regulation of prostatic bud formation
Biological Processpositive regulation of BMP signaling pathway
Biological Processpositive regulation of smooth muscle cell proliferation
Biological Processpositive regulation of Wnt signaling pathway
Biological Processvascular endothelial growth factor receptor signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Extracellular sulfatase
  • EC number

Gene names

    • Name
      SULF1
    • Synonyms
      sulf1

Organism names

Accessions

  • Primary accession
    Q32KH2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue.

Type
IDPosition(s)Description
Signal1-22
ChainPRO_501410441823-869Extracellular sulfatase
Modified residue873-oxoalanine (Cys)

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.

Proteomic databases

Expression

Gene expression databases

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region, coiled coil.

Type
IDPosition(s)Description
Domain43-373Sulfatase N-terminal
Compositional bias495-510Basic and acidic residues
Region495-524Disordered
Domain536-678Extracellular sulfatase C-terminal
Coiled coil642-669
Domain681-739Extracellular sulfatase C-terminal

Sequence similarities

Belongs to the sulfatase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    869
  • Mass (Da)
    100,584
  • Last updated
    2005-12-06 v1
  • MD5 Checksum
    E026C5CD1C0E7F29309990C752B6486F
MKYSCCALVLAVLATELLGGHCSTVRSQRFRGRIQQERKNIRPNIILVLTDDQDVELGSLQVMNKTRKIMEHGGATFTNAFVTTPMCCPSRSSMLTGKYVHNHNVYTNNENCSSPSWQAMHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWLGLIKNSRFYNYTVCRNGIKEKHGFDYAKDYFTDLITNESINYFKMSKRMYPHRPIMMVISHAAPHGPEDSAPQFSKLYPNASQHITPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNVLHRKRLQTLMSVDDSVERLYNMLVETGELDNTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSIVPQIVLNIDLAPTILDIAGLDTPPDVDGKSVLKLLDLEKPGNRFRTNKKARIWRDTFLVERGKFLRKKEESSKNIQQSNHLPKYERVKELCQQARYQTACEQPGQKWQCIEDTSGKLRIHKCKGSSDLLTVRPSARNLYPRGFHDKDKDKDCSCGEPGYRAGRGQRKGQRQFLRNQGTPKYKPRFVHTRQTRSLSVEFEGEIYDINLEEEELQVLRPRNIVKRHDEGHRGPGGHQAPGDGDVMLADRDNALGLPTTVRVTHKCFILPNDTIHCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPEECACSKQSYYNKEKGVKKQEKVKSHLHPFKEAAQEVDSKLQLFKENRRRKKERKEKKRQRKGEECSLPGLTCFTHDNNHWQTAPFWNLGSFCACTSSNNNTYWCLRTVNETHNFLFCEFATGFLEYFDMNTDPYQLTNAVHTVERGILNQLHVQLMELRSCQGYKQCNPRPKGLEVGNKDGGSYDLHRGQLWDGWEG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias495-510Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BN000765
EMBL· GenBank· DDBJ
CAI85011.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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