Variant position: 33 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 267 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 PTTSTLDWCEENYSVTWYIA EFWNTVSNLIMIIPPMFGAVQ
Mouse PTTSTLDWCEENYVVTLFVA EFWNTVSNLIMIIPPIFGAIQ
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
1 – 267 Alkaline ceramidase 3
1 – 33 Cytoplasmic
19 – 19 Calcium
20 – 20 Calcium; via carbonyl oxygen
22 – 22 Calcium; via carbonyl oxygen
24 – 24 Calcium
33 – 33 Calcium
1 – 133 Missing. In isoform 2.
19 – 19 D -> G. Mildly decreased enzyme activity.
22 – 22 E -> G. Strongly decreased enzyme activity.
24 – 24 N -> G. Strongly decreased enzyme activity.
29 – 33
Deficiency of the alkaline ceramidase ACER3 manifests in early childhood by progressive leukodystrophy.
Edvardson S.; Yi J.K.; Jalas C.; Xu R.; Webb B.D.; Snider J.; Fedick A.; Kleinman E.; Treff N.R.; Mao C.; Elpeleg O.;
J. Med. Genet. 53:389-396(2016)
Cited for: FUNCTION; CATALYTIC ACTIVITY; INVOLVEMENT IN PLDECO; VARIANT PLDECO GLY-33; CHARACTERIZATION OF VARIANT PLDECO GLY-33;
Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy.
Vasiliauskaite-Brooks I.; Healey R.D.; Rochaix P.; Saint-Paul J.; Sounier R.; Grison C.; Waltrich-Augusto T.; Fortier M.; Hoh F.; Saied E.M.; Arenz C.; Basu S.; Leyrat C.; Granier S.;
Nat. Commun. 9:5437-5437(2018)
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2-244 IN COMPLEX WITH CALCIUM AND ZINC IONS; FUNCTION; CATALYTIC ACTIVITY; COFACTOR; PATHWAY; CHARACTERIZATION OF VARIANT PLDECO GLY-33; SUBCELLULAR LOCATION; TOPOLOGY; MUTAGENESIS OF ASP-19; GLU-22; ASN-24; SER-99; TYR-149 AND SER-228;
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.