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MGP006548

UniProt Annotations

Entry Information

Gene Name	heparan-alpha-glucosaminide N-acetyltransferase
Protein Entry	HGNAT_HUMAN
UniProt ID	Q68CP4
Species	Human

Comments

Comment type	Description
Alternative Products	Event=Alternative initiation; Named isoforms=2; Comment=Isoform 1 and isoform 2 are correctly targeted to the lysosomal compartment and are functional enzymes.; Name=1; IsoId=Q68CP4-1; Sequence=Displayed; Note=Intralysosomal proteolytic cleavage is faster and enzymatic activity higher than isoform 2.; Name=2; IsoId=Q68CP4-2; Sequence=VSP_040504;
Catalytic Activity	Acetyl-CoA + heparan sulfate alpha-D- glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D- glucosaminide. {ECO:0000269\|PubMed:16960811}.
Disease	Mucopolysaccharidosis 3C (MPS3C) [MIM:252930]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. {ECO:0000269\|PubMed:16960811, ECO:0000269\|PubMed:17033958, ECO:0000269\|PubMed:17397050, ECO:0000269\|PubMed:18024218, ECO:0000269\|PubMed:19479962}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Function	Lysosomal acetyltransferase that acetylates the non- reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase. {ECO:0000269\|PubMed:16960811, ECO:0000269\|PubMed:17033958, ECO:0000269\|PubMed:19823584, ECO:0000269\|PubMed:20650889}.
Miscellaneous	A signal sequence is predicted but has been shown not to be cleaved in the reticulum endoplasmic.
Ptm	Glycosylated. {ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19823584}.
Ptm	Undergoes intralysosomal proteolytic cleavage; occurs within the end of the first and/or the beginning of the second luminal domain and is essential for the activation of the enzyme.
Subcellular Location	Lysosome membrane {ECO:0000269\|PubMed:16960811, ECO:0000269\|PubMed:17033958, ECO:0000269\|PubMed:17897319}; Multi-pass membrane protein {ECO:0000269\|PubMed:16960811, ECO:0000269\|PubMed:17033958, ECO:0000269\|PubMed:17897319}. Note=Colocalizes with the lysosomal marker LAMP2. The signal peptide is not cleaved upon translocation into the endoplasmic reticulum; the precursor is probably targeted to the lysosomes via the adapter protein complex-mediated pathway that involves tyrosine- and/or dileucine-based conserved amino acid motifs in the last C-terminus 16-amino acid domain.
Subunit	Homooligomer. Homooligomerization is necessary for enzyme activity. {ECO:0000269\|PubMed:20650889}.
Tissue Specificity	Widely expressed, with highest level in leukocytes, heart, liver, skeletal muscle, lung, placenta and liver. {ECO:0000269\|PubMed:16960811, ECO:0000269\|PubMed:17033958}.