Q32KJ3 · Q32KJ3_RAT

  • Protein
    Extracellular sulfatase
  • Gene
    Sulf2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

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.

TypeIDPosition(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 region
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 Processcartilage 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 Processglomerular filtration
Biological Processheparan sulfate proteoglycan metabolic process
Biological Processinnervation
Biological Processkidney development
Biological Processliver regeneration
Biological Processnegative regulation of fibroblast growth factor receptor signaling pathway
Biological Processpositive regulation of canonical Wnt signaling pathway
Biological Processpositive regulation of endothelin production
Biological Processpositive regulation of vascular endothelial growth factor production
Biological Processpositive regulation of Wnt signaling pathway
Biological Processregulation of hepatocyte proliferation
Biological Processresponse to wounding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Extracellular sulfatase
  • EC number

Gene names

    • Name
      Sulf2

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q32KJ3

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_500422080825-866Extracellular 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.

Keywords

Family & Domains

Features

Showing features for domain, region, coiled coil.

TypeIDPosition(s)Description
Domain44-374Sulfatase N-terminal
Domain533-669Extracellular sulfatase C-terminal
Region568-596Disordered
Coiled coil633-660

Sequence similarities

Belongs to the sulfatase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    866
  • Mass (Da)
    99,488
  • Last updated
    2005-12-06 v1
  • Checksum
    E35E8E515B290818
MAPPGLPLWLLSTALFSLLAGSSAFLSYPRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGMKEKHGSDYSTDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPSVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERPVNRFHLKKKLRVWRDSFLVERGKLLHKREGDKVNAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDASGALKLHKCKGPVRFGGGGDRALSNLVPKYDGQSSEACSCDGGGGGGDYKLGLAGRRKLFKKKYKTSYARNRSIRSVAIEVDGEVYHVGLDNMPLPRNLTKRHWPGAPEDQDDKDGGSFSGTGGLPDYSAPNPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHKVSYHSQHKGRLKHKGSSLHPFRKGLQEKDKVWLLREQKRKKKLRKLLKRLQNNDTCSMPGLTCFTHDNHHWQTAPLWTLGPFCACTSANNNTYWCLRTINETHNFLFCEFATGFIEYFDLSTDPYQLMNAVNTLDRDVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLRDGGSYEQYRQFQRRKWPEMKRPSSKSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BN000744
EMBL· GenBank· DDBJ
CAI84990.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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