UniProt functional annotation for Q8NBK3



	UniProt functional annotation for Q8NBK3

UniProt code: Q8NBK3.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Oxidase that catalyzes the conversion of cysteine to 3- oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756, PubMed:21224894). 3- oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756). Known substrates include GALNS, ARSA, STS and ARSE (PubMed:12757706, PubMed:15907468, PubMed:15657036). {ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:15907468, ECO:0000269|PubMed:16368756, ECO:0000269|PubMed:21224894, ECO:0000269|PubMed:25931126}.

Catalytic activity: Reaction=2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl- [sulfatase] + an organic disulfide + H(+) + H2O + hydrogen sulfide; Xref=Rhea:RHEA:51152, Rhea:RHEA-COMP:12900, Rhea:RHEA-COMP:12901, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29256, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:35489, ChEBI:CHEBI:85621; EC=1.8.3.7; Evidence={ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:25931126};

Cofactor: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:25931126}; Note=The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000269|PubMed:25931126};

Biophysicochemical properties: Kinetic parameters: KM=0.34 uM for [sulfatase]-L-cysteine {ECO:0000269|PubMed:25931126}; Note=Kcat is 6.06 min(-1) with [sulfatase]-L-cysteine as substrate. {ECO:0000269|PubMed:25931126};

Pathway: Protein modification; sulfatase oxidation. {ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:15907468, ECO:0000269|PubMed:25931126}.

Subunit: Monomer, homodimer and heterodimer with SUMF2. {ECO:0000269|PubMed:15907468, ECO:0000269|PubMed:15962010, ECO:0000269|PubMed:16368756}.

Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:15962010, ECO:0000269|PubMed:18266766, ECO:0000269|PubMed:21224894}.

Tissue specificity: Ubiquitous. Highly expressed in kidney, pancreas and liver. Detected at lower levels in leukocytes, lung, placenta, small intestine, skeletal muscle and heart. {ECO:0000269|PubMed:15962010}.

Ptm: N-glycosylated. Contains high-mannose-type oligosaccharides. {ECO:0000269|PubMed:15657036, ECO:0000269|PubMed:15907468, ECO:0000269|PubMed:19159218}.

Disease: Multiple sulfatase deficiency (MSD) [MIM:272200]: A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. {ECO:0000269|PubMed:12757705, ECO:0000269|PubMed:12757706, ECO:0000269|PubMed:15146462, ECO:0000269|PubMed:18157819, ECO:0000269|PubMed:21224894}. Note=The disease is caused by variants affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases. {ECO:0000269|PubMed:12757706}.

Miscellaneous: The resulting 3-oxoalanine in the substrate protein is called C(alpha)-formylglycine by many authors. It should not be confused with N-formylglycine.

Similarity: Belongs to the sulfatase-modifying factor family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Oxidase that catalyzes the conversion of cysteine to 3- oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756, PubMed:21224894). 3- oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756). Known substrates include GALNS, ARSA, STS and ARSE (PubMed:12757706, PubMed:15907468, PubMed:15657036). {ECO:0000269\|PubMed:12757706, ECO:0000269\|PubMed:15657036, ECO:0000269\|PubMed:15907468, ECO:0000269\|PubMed:16368756, ECO:0000269\|PubMed:21224894, ECO:0000269\|PubMed:25931126}.


Catalytic activity:		Reaction=2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl- [sulfatase] + an organic disulfide + H(+) + H2O + hydrogen sulfide; Xref=Rhea:RHEA:51152, Rhea:RHEA-COMP:12900, Rhea:RHEA-COMP:12901, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29256, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:35489, ChEBI:CHEBI:85621; EC=1.8.3.7; Evidence={ECO:0000269\|PubMed:15657036, ECO:0000269\|PubMed:25931126};
Cofactor:		Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269\|PubMed:25931126}; Note=The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000269\|PubMed:25931126};
Biophysicochemical properties:		Kinetic parameters: KM=0.34 uM for [sulfatase]-L-cysteine {ECO:0000269\|PubMed:25931126}; Note=Kcat is 6.06 min(-1) with [sulfatase]-L-cysteine as substrate. {ECO:0000269\|PubMed:25931126};
Pathway:		Protein modification; sulfatase oxidation. {ECO:0000269\|PubMed:12757706, ECO:0000269\|PubMed:15657036, ECO:0000269\|PubMed:15907468, ECO:0000269\|PubMed:25931126}.
Subunit:		Monomer, homodimer and heterodimer with SUMF2. {ECO:0000269\|PubMed:15907468, ECO:0000269\|PubMed:15962010, ECO:0000269\|PubMed:16368756}.
Subcellular location:		Endoplasmic reticulum lumen {ECO:0000269\|PubMed:15657036, ECO:0000269\|PubMed:15962010, ECO:0000269\|PubMed:18266766, ECO:0000269\|PubMed:21224894}.
Tissue specificity:		Ubiquitous. Highly expressed in kidney, pancreas and liver. Detected at lower levels in leukocytes, lung, placenta, small intestine, skeletal muscle and heart. {ECO:0000269\|PubMed:15962010}.
Ptm:		N-glycosylated. Contains high-mannose-type oligosaccharides. {ECO:0000269\|PubMed:15657036, ECO:0000269\|PubMed:15907468, ECO:0000269\|PubMed:19159218}.
Disease:		Multiple sulfatase deficiency (MSD) [MIM:272200]: A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. {ECO:0000269\|PubMed:12757705, ECO:0000269\|PubMed:12757706, ECO:0000269\|PubMed:15146462, ECO:0000269\|PubMed:18157819, ECO:0000269\|PubMed:21224894}. Note=The disease is caused by variants affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases. {ECO:0000269\|PubMed:12757706}.
Miscellaneous:		The resulting 3-oxoalanine in the substrate protein is called C(alpha)-formylglycine by many authors. It should not be confused with N-formylglycine.
Similarity:		Belongs to the sulfatase-modifying factor family. {ECO:0000305}.