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UniProtKB/Swiss-Prot P51659: Variant p.Gly16Ser

Peroxisomal multifunctional enzyme type 2
Gene: HSD17B4
Variant information

Variant position:  16
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Glycine (G) to Serine (S) at position 16 (G16S, p.Gly16Ser).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from glycine (G) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In DBPD; no dehydrogenase activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

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:   MGSPLRFDGRVVLVT  G AGAGLGRAYALAFAERGALV
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                         MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALV

Mouse                         MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALV

Rat                           MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALV

Drosophila                    SDGKLRYDGRVAVVTGAGAGLGREYALLFAERGAKV

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.

TypePositionsDescription
Chain 1 – 736 Peroxisomal multifunctional enzyme type 2
Chain 1 – 311 (3R)-hydroxyacyl-CoA dehydrogenase
Nucleotide binding 13 – 37 NAD
Region 1 – 305 (3R)-hydroxyacyl-CoA dehydrogenase
Binding site 21 – 21 NAD; via amide nitrogen
Alternative sequence 1 – 38 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVV -> MVILEAPHLLRRKEPETPGLSSRIGPSLCPGFCRKRSVSCCFQNLCNNPMEKIISQCRFFVSM. In isoform 2.
Turn 15 – 18


Literature citations

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;

Disclaimer: 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.