Variant position: 182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 296 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 ESLFPEVANGKLMILTVTQK TKNDMTVWSEEVEIEREVLLE
Mouse ESLFPEVANSKLMILTVTQK TENDMTVWSEEVEVEREVLLE
Rat ESLFPEVANSKLMILTVTQK TEHDMTVWSEEVEVEREALLE
Chicken ESMFPEVNANHLTVLTVTQK TKNDMTVWSQEVEDEREMLLE
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
39 – 296 Methylmalonic aciduria and homocystinuria type D protein, mitochondrial
165 – 165 F -> A. Mildly decreases methylcobalamin levels and strongly increases adenosylcobalamin levels.
186 – 186 M -> A. Decreases methylcobalamin levels. No effect on interaction with MMACHC.
189 – 189 W -> A. Decreases methylcobalamin levels. Impairs interaction with MMACHC.
197 – 197 R -> A. Decreases methylcobalamin levels, but increases adenosylcobalamin levels.
Gene identification for the cblD defect of vitamin B12 metabolism.
Coelho D.; Suormala T.; Stucki M.; Lerner-Ellis J.P.; Rosenblatt D.S.; Newbold R.F.; Baumgartner M.R.; Fowler B.;
N. Engl. J. Med. 358:1454-1464(2008)
Cited for: FUNCTION; TISSUE SPECIFICITY; VARIANTS MAHCD LEU-ALA-GLU-PRO-LEU-SER-108 INS; ASN-182; 204-PHE--ALA-232 DEL; CYS-249 AND PRO-259;
Structural insights into the MMACHC-MMADHC protein complex involved in vitamin B12 trafficking.
Froese D.S.; Kopec J.; Fitzpatrick F.; Schuller M.; McCorvie T.J.; Chalk R.; Plessl T.; Fettelschoss V.; Fowler B.; Baumgartner M.R.; Yue W.W.;
J. Biol. Chem. 290:29167-29177(2015)
Cited for: INTERACTION WITH MMACHC; CHARACTERIZATION OF VARIANTS MAHCD ASN-182 AND PRO-259; MUTAGENESIS OF TRP-189 AND ASP-226;
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.