Variant position: 16 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 736 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 MGSPLRFDGRVVLVT GAGAGLGRAYALAFAERGALV
Mouse MASPLRFDGRVVLVT GAGGGLGRAYALAFAERGALV
Rat MASPLRFDGRVVLVT GAGGGLGRAYALAFAERGALV
Drosophila SDGKLRYDGRVAVVT GAGAGLGREYALLFAERGAKV
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 – 736 Peroxisomal multifunctional enzyme type 2
1 – 311 (3R)-hydroxyacyl-CoA dehydrogenase
13 – 37 NAD
1 – 305 (3R)-hydroxyacyl-CoA dehydrogenase
21 – 21 NAD; via amide nitrogen
1 – 38 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVV -> MVILEAPHLLRRKEPETPGLSSRIGPSLCPGFCRKRSVSCCFQNLCNNPMEKIISQCRFFVSM. In isoform 2.
15 – 18
Human peroxisomal multifunctional enzyme type 2. Site-directed mutagenesis studies show the importance of two protic residues for 2-enoyl-CoA hydratase 2 activity.
Qin Y.M.; Haapalainen A.M.; Kilpelainen S.H.; Marttila M.S.; Koski M.K.; Glumoff T.; Novikov D.K.; Hiltunen J.K.;
J. Biol. Chem. 275:4965-4972(2000)
Cited for: MUTAGENESIS OF TYR-347; GLU-366; ASP-370; HIS-406; GLU-408; TYR-410; ASP-490; TYR-505; ASP-510; HIS-515; ASP-517 AND HIS-532; CHARACTERIZATION OF VARIANT DBPD SER-16; CATALYTIC ACTIVITY;
Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency.
van Grunsven E.G.; van Berkel E.; Ijlst L.; Vreken P.; de Klerk J.B.C.; Adamski J.; Lemonde H.; Clayton P.T.; Cuebas D.A.; Wanders R.J.A.;
Proc. Natl. Acad. Sci. U.S.A. 95:2128-2133(1998)
Cited for: VARIANT DBPD SER-16; CATALYTIC ACTIVITY; FUNCTION;
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