Variant position: 171 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 440 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 NLVNNGYVRDETVRAAPYDW RLEPGQQEEYYRKLAGLVEEM
Mouse NLVNNGYVRDETVRAAPYDW RLAPHQQDEYYKKLAGLVEEM
Rat NLVNNGYVRDETVRAAPYDW RLAPRQQDEYYQKLAGLVEEM
Rabbit NLVNNGYVRDETVRAAPYDW RLEPSQQEEYYGKLAGLVEEM
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
25 – 440 Phosphatidylcholine-sterol acyltransferase
173 – 173 Determinant for substrate specificity
173 – 173 E -> A. Increased activity towards PAPC. Increased PAPC/POPC activity ratio.
173 – 173 E -> D. Little change in enzyme specific activity nor in PAPC/POPC activity ratio.
173 – 173 E -> K. Decreased enzyme specific activity. Increased PAPC/POPC activity ratio.
173 – 173 E -> L. Increased activity towards PAPC. Increased PAPC/POPC activity ratio.
173 – 173 E -> Q. Decreased enzyme specific activity. Increased PAPC/POPC activity ratio.
Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele.
Taramelli R.; Pontoglio M.; Candiani G.; Ottolenghi S.; Dieplinger H.; Catapano A.; Albers J.; Vergani C.; McLean J.;
Hum. Genet. 85:195-199(1990)
Cited for: VARIANT LCATD TRP-171;
The molecular basis of lecithin:cholesterol acyltransferase deficiency syndromes: a comprehensive study of molecular and biochemical findings in 13 unrelated Italian families.
Calabresi L.; Pisciotta L.; Costantin A.; Frigerio I.; Eberini I.; Alessandrini P.; Arca M.; Bon G.B.; Boscutti G.; Busnach G.; Frasca G.; Gesualdo L.; Gigante M.; Lupattelli G.; Montali A.; Pizzolitto S.; Rabbone I.; Rolleri M.; Ruotolo G.; Sampietro T.; Sessa A.; Vaudo G.; Cantafora A.; Veglia F.; Calandra S.; Bertolini S.; Franceschini G.;
Arterioscler. Thromb. Vasc. Biol. 25:1972-1978(2005)
Cited for: VARIANTS FED GLU-70 AND ALA-298; VARIANTS LCATD CYS-164; TRP-171; ASN-205; ASN-242; HIS-268; ILE-298 AND MET-333; VARIANTS PRO-115; THR-165 AND ARG-396;
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.