Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60313: Variant p.Gly300Glu

Dynamin-like GTPase OPA1, mitochondrial
Gene: OPA1
Feedback?
Variant information Variant position: help 300 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help 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: help 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: help -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: help In OPA1; loss of GTPase activity; loss of function in promoting mitochondrial fusion. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 300 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 960 The length of the canonical sequence.
Location on the sequence: help 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: help 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: help 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 GTPase OPA1, long form
Chain 195 – 960 Dynamin-like GTPase OPA1, short form
Topological domain 114 – 770 Mitochondrial intermembrane
Domain 285 – 561 Dynamin-type G
Region 295 – 302 G1 motif
Binding site 298 – 298
Binding site 300 – 300
Binding site 301 – 301
Binding site 302 – 302
Binding site 302 – 302
Binding site 303 – 303
Binding site 317 – 317
Mutagenesis 297 – 297 Q -> E. Abolished GTPase activity without affecting the ability to bind membranes.
Mutagenesis 298 – 298 S -> A. Abolished GTPase activity without affecting the ability to bind membranes.
Mutagenesis 300 – 300 G -> E. Abolished GTPase activity without affecting the ability to bind membranes.
Mutagenesis 301 – 301 K -> A. Abolished GTPase activity.
Mutagenesis 302 – 302 T -> A. Abolished GTPase activity.
Mutagenesis 302 – 302 T -> N. Abolished GTPase activity without affecting the ability to bind membranes.
Mutagenesis 316 – 316 R -> A. Strongly decreased GTPase activity.
Mutagenesis 320 – 320 E -> A. Decreased GTPase activity.



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; DOMAIN; 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.