Variant position: 169 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 395 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human EDKKGHLIHGRNMDFGVFLG WNINNDTWVITEQLKPLTVNL
Chimpanzee EDKKGHLIHGRNMDFGVFLG WNINNDTWVITEQLKPLTVNL
Mouse EDEKGHLLHGRNMDFGIFLG WNINNNTWVVTEELKPLTVNL
Rat EDGKGHLLHGRNMDFGIFLG WNINNNTWVVTEELKPLTVNL
Bovine EDKEGHLLHGRNLDFGVFLG WNINNDTWVITEELKPLTVNL
Caenorhabditis elegans QDKDGHVFHARNLDFGLFMG WDPVLHDWQISQKLRKMIINV
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
143 – 395 Acid ceramidase subunit beta
162 – 162 Important for catalytic activity
173 – 173 N-linked (GlcNAc...) asparagine
31 – 340 Interchain (between alpha and beta subunits)
159 – 159 R -> Q. Strongly decreased autocatalytic processing. Moderately decreased ceramidase activity.
162 – 162 D -> N. Strongly decreased autocatalytic processing. Strongly decreased ceramidase activity.
169 – 171 WNI -> QNQ. Moderately decreased autocatalytic processing, but loss of ceramidase activity, when associated with Q-176.
173 – 173 N -> Q. Loss of ceramide catabolic process.
176 – 176 W -> Q. Moderately decreased autocatalytic processing, but loss of ceramidase activity, when associated with 169-Q--Q-171.
Brief Report: Peripheral Osteolysis in Adults Linked to ASAH1 (Acid Ceramidase) Mutations: A New Presentation of Farber's Disease.
Bonafe L.; Kariminejad A.; Li J.; Royer-Bertrand B.; Garcia V.; Mahdavi S.; Bozorgmehr B.; Lachman R.L.; Mittaz-Crettol L.; Campos-Xavier B.; Nampoothiri S.; Unger S.; Rivolta C.; Levade T.; Superti-Furga A.;
Arthritis Rheum. 68:2323-2327(2016)
Cited for: VARIANTS FRBRL ARG-169 AND GLY-254;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.