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UniProtKB/Swiss-Prot O60313: Variant p.Gly300Glu

Dynamin-like 120 kDa protein, mitochondrial
Gene: OPA1
Variant information

Variant position:  300
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 Glutamate (E) at position 300 (G300E, p.Gly300Glu).
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 medium size and acidic (E)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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 OPA1; loss of GTPase activity; loss of function in promoting mitochondrial fusion.
Any additional useful information about the variant.

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



Sequence information

Variant position:  300
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  960
The length of the canonical sequence.

Location on the sequence:   ASYNTQDHLPRVVVVGDQSA  G KTSVLEMIAQARIFPRGSGE
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                         ASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGE

Mouse                         ASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGE

Rat                           ASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGE

Chicken                       ASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGE

Zebrafish                     SNYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGE

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 88 – 960 Dynamin-like 120 kDa protein, mitochondrial
Chain 195 – 960 Dynamin-like 120 kDa protein, form S1
Topological domain 114 – 960 Mitochondrial intermembrane
Domain 285 – 561 Dynamin-type G
Nucleotide binding 295 – 302 GTP
Region 295 – 302 G1 motif


Literature citations

Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy.
Delettre C.; Lenaers G.; Griffoin J.-M.; Gigarel N.; Lorenzo C.; Belenguer P.; Pelloquin L.; Grosgeorge J.; Turc-Carel C.; Perret E.; Astarie-Dequeker C.; Lasquellec L.; Arnaud B.; Ducommun B.; Kaplan J.; Hamel C.P.;
Nat. Genet. 26:207-210(2000)
Cited for: SUBCELLULAR LOCATION; TISSUE SPECIFICITY; VARIANT OPA1 GLU-300;

OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation.
Ban T.; Heymann J.A.; Song Z.; Hinshaw J.E.; Chan D.C.;
Hum. Mol. Genet. 19:2113-2122(2010)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBUNIT; CHARACTERIZATION OF VARIANTS OPA1 GLU-300; VAL-439; HIS-445; ARG-545; LYS-728; ARG-785 AND PRO-939; CHARACTERIZATION OF VARIANTS VARIANT DOA+ THR-357; VAL-439; HIS-445; ARG-545 AND ASP-910;

Spectrum, frequency and penetrance of OPA1 mutations in dominant optic atrophy.
Toomes C.; Marchbank N.J.; Mackey D.A.; Craig J.E.; Newbury-Ecob R.A.; Bennett C.P.; Vize C.J.; Desai S.P.; Black G.C.M.; Patel N.; Teimory M.; Markham A.F.; Inglehearn C.F.; Churchill A.J.;
Hum. Mol. Genet. 10:1369-1378(2001)
Cited for: VARIANTS OPA1 GLN-290; GLU-300; PHE-384; LYS-503 AND ASN-505; VARIANTS ASN-158 AND GLY-907;

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.