Sequence information
Variant position: 182 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:
DFGVFLGWNINNDTWVITEQ
L KPLTVNLDFQRNNKTVFKAS
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 DFGVFLGWNINNDTWVITEQL KPLTVNLDFQRNNKTVFKAS
Chimpanzee DFGVFLGWNINNDTWVITEQL KPLTVNLDFQRNNKTVFKAS
Mouse DFGIFLGWNINNNTWVVTEEL KPLTVNLDFQRNNKTVFKAT
Rat DFGIFLGWNINNNTWVVTEEL KPLTVNLDFQRNNKTVFKAT
Bovine DFGVFLGWNINNDTWVITEEL KPLTVNLDFQRNNKTLFKAT
Caenorhabditis elegans DFGLFMGWDPVLHDWQISQKL RKMIINVNWLKDGKLLYKSN
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
Chain
143 – 395
Acid ceramidase subunit beta
Site
162 – 162
Important for catalytic activity
Glycosylation
173 – 173
N-linked (GlcNAc...) asparagine
Glycosylation
195 – 195
N-linked (GlcNAc...) asparagine
Disulfide bond
31 – 340
Interchain (between alpha and beta subunits)
Mutagenesis
162 – 162
D -> N. Strongly decreased autocatalytic processing. Strongly decreased ceramidase activity.
Mutagenesis
173 – 173
N -> Q. Loss of ceramide catabolic process.
Mutagenesis
176 – 176
W -> Q. Moderately decreased autocatalytic processing, but loss of ceramidase activity, when associated with 169-Q--Q-171.
Mutagenesis
195 – 195
N -> Q. No effect on ceramide catabolic process.
Helix
177 – 182
Literature citations
Farber lipogranulomatosis: clinical and molecular genetic analysis reveals a novel mutation in an Indian family.
Devi A.R.R.; Gopikrishna M.; Ratheesh R.; Savithri G.; Swarnalata G.; Bashyam M.;
J. Hum. Genet. 51:811-814(2006)
Cited for: VARIANT FRBRL VAL-182;
Disclaimer:
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.