Variant position: 193 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 421 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 KTKAEKKGDEYIINGQKMWI TNGGKANWYFLLARSDPDPKA
Chimpanzee KTKAEKKGDEYIINGQKMWI TNGGKANWYFLLARSDPDPKA
Mouse KTKAEKKGDEYVINGQKMWI TNGGKANWYFLLARSNPDPKV
Rat KTKAEKKGDEYVINGQKMWI TNGGKANWYFVLTRSNPDPKV
Pig KTKAEKKGDEYIINGQKMWI TNGGKANWYFLLARSDPDPKA
Bovine KTKAEKKGDEYIINGQKMWI TNGGKANWYFLLARSDPDPKA
Caenorhabditis elegans KTKCEKKGDEYIINGSKAWI TGGGHAKWFFVLARSDPNPKT
Drosophila KTRAEKKGDEWVINGQKMWI TNGGVANWYFVLARTNPDPKC
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
26 – 421 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
191 – 193 FAD
179 – 179 N6-succinyllysine
212 – 212 N6-acetyllysine; alternate
212 – 212 N6-succinyllysine; alternate
191 – 191 W -> A. Loss of electron transfer to ETF.
191 – 191 W -> F. Reduces rate of electron transfer to ETF about six-fold.
182 – 193
The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype?
Andresen B.S.; Bross P.; Udvari S.; Kirk J.; Gray G.; Kmoch S.; Chamoles N.; Knudsen I.; Winter V.; Wilcken B.; Yokota I.; Hart K.; Packman S.; Harpey J.P.; Saudubray J.-M.; Hale D.E.; Bolund L.; Koelvraa S.; Gregersen N.;
Hum. Mol. Genet. 6:695-707(1997)
Cited for: VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352;
Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site.
Kuchler B.; Abdel-Ghany A.G.; Bross P.; Nandy A.; Rasched I.; Ghisla S.;
Biochem. J. 337:225-230(1999)
Cited for: CHARACTERIZATION OF VARIANT ACADMD ALA-193;
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