A0A452RZK0 · A0A452RZK0_URSAM

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 site52Ca2+ (UniProtKB | ChEBI)
Binding site53Ca2+ (UniProtKB | ChEBI)
Active site88Nucleophile
Binding site88Ca2+ (UniProtKB | ChEBI); via 3-oxoalanine
Binding site317Ca2+ (UniProtKB | ChEBI)
Binding site318Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell surface
Cellular Componentendoplasmic reticulum
Cellular Componentextracellular space
Cellular ComponentGolgi stack
Cellular Componentplasma membrane
Molecular Functionarylsulfatase activity
Molecular Functioncalcium ion binding
Molecular Functionglycosaminoglycan binding
Molecular FunctionN-acetylglucosamine-6-sulfatase activity
Biological Processbone development
Biological Processchondrocyte development
Biological Processembryonic skeletal system development
Biological Processesophagus smooth muscle contraction
Biological Processglial cell-derived neurotrophic factor receptor signaling pathway
Biological Processglomerular basement membrane development
Biological Processheparan sulfate proteoglycan metabolic process
Biological Processinnervation
Biological Processnegative regulation of fibroblast growth factor receptor signaling pathway
Biological Processpositive regulation of vascular endothelial growth factor production
Biological Processpositive regulation of Wnt signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Extracellular sulfatase
  • EC number

Gene names

    • Name
      SULF2

Organism names

Accessions

  • Primary accession
    A0A452RZK0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue.

Type
IDPosition(s)Description
Signal1-24
ChainPRO_501882531125-870Extracellular sulfatase
Modified residue883-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.

Interaction

Protein-protein interaction databases

Family & Domains

Features

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

Type
IDPosition(s)Description
Domain44-374Sulfatase N-terminal
Domain528-664Extracellular sulfatase C-terminal
Region548-591Disordered
Compositional bias566-580Basic and acidic residues
Coiled coil628-655

Sequence similarities

Belongs to the sulfatase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    870
  • Mass (Da)
    100,236
  • Last updated
    2019-05-08 v1
  • Checksum
    34B420EA6D4D8D3D
MAPPSLLFCLLSATVFSLLGGSSAFLSHHRLKARFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRSFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHGFDYSKDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSSLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYNMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPSDMDGKSILKLLDTERPVNRFHLKKKMRVWRDSFLVERGKLLHKRDSDKVDAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDASGKLKLHKCKGPARLGGRALSNLVPKYYAPGGGEACACDGGDYKLGLAGRRKKFFKKKYKTSYARNRSIRSVAIEVGGGVHHTGLDDAPQPRNLTKRHWPGAPEDPDDKDGGDFSGTGGLPDYSAPNPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHKISYHTQHQGRLKHKGSSLHPFRKGLREKDKVWLLREQKRKKKLRKLLRRLQNNDTCSMPGLTCFTHDNRHWQTAPLWTLGPFCACTSANNNTYWCMRTINETHNFLFCEFATGFLEYFDLNTDPYQLMNAVNTLDREVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLKDGGSYEQYRQFQRRKWPEMKRPSSKSLGQLWEGWEG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias566-580Basic and acidic residues

Keywords

Genome annotation databases

Similar Proteins

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