Q32KJ3 · Q32KJ3_RAT
- ProteinExtracellular sulfatase
- GeneSulf2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids866 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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
- an aryl sulfate + H2O = a phenol + H+ + sulfate
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 52 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 53 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 88 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 88 | Ca2+ (UniProtKB | ChEBI); via 3-oxoalanine | ||||
Sequence: C | ||||||
Binding site | 317 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 318 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameExtracellular sulfatase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ32KJ3
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MAPPGLPLWLLSTALFSLLAGSSA | ||||||
Chain | PRO_5004220808 | 25-866 | Extracellular sulfatase | |||
Sequence: FLSYPRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGMKEKHGSDYSTDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPSVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERPVNRFHLKKKLRVWRDSFLVERGKLLHKREGDKVNAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDASGALKLHKCKGPVRFGGGGDRALSNLVPKYDGQSSEACSCDGGGGGGDYKLGLAGRRKLFKKKYKTSYARNRSIRSVAIEVDGEVYHVGLDNMPLPRNLTKRHWPGAPEDQDDKDGGSFSGTGGLPDYSAPNPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHKVSYHSQHKGRLKHKGSSLHPFRKGLQEKDKVWLLREQKRKKKLRKLLKRLQNNDTCSMPGLTCFTHDNHHWQTAPLWTLGPFCACTSANNNTYWCLRTINETHNFLFCEFATGFIEYFDLSTDPYQLMNAVNTLDRDVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLRDGGSYEQYRQFQRRKWPEMKRPSSKSL | ||||||
Modified residue | 88 | 3-oxoalanine (Cys) | ||||
Sequence: C |
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
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 44-374 | Sulfatase N-terminal | ||||
Sequence: PNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGMKEKHGSDYSTDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYIVYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPSVEAGSLNPHIVLNIDLAPTILDIAG | ||||||
Domain | 533-669 | Extracellular sulfatase C-terminal | ||||
Sequence: KTSYARNRSIRSVAIEVDGEVYHVGLDNMPLPRNLTKRHWPGAPEDQDDKDGGSFSGTGGLPDYSAPNPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHK | ||||||
Region | 568-596 | Disordered | ||||
Sequence: TKRHWPGAPEDQDDKDGGSFSGTGGLPDY | ||||||
Coiled coil | 633-660 | |||||
Sequence: KLHIDHEIETLQNKIKNLREVRGHLKKK |
Sequence similarities
Belongs to the sulfatase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length866
- Mass (Da)99,488
- Last updated2005-12-06 v1
- ChecksumE35E8E515B290818