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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O60313: Variant p.Gln310Arg

Dynamin-like GTPase OPA1, mitochondrial
Gene: OPA1
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Variant information Variant position: help 310 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 Glutamine (Q) to Arginine (R) at position 310 (Q310R, p.Gln310Arg). 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 medium size and polar (Q) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 310 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 RVVVVGDQSAGKTSVLEMIA Q ARIFPRGSGEMMTRSPVKVT 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                         RVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVT

Mouse                         RVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVT

Rat                           RVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVT

Chicken                       RVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVT

Zebrafish                     RVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVT
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
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
Binding site 323 – 323
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.
Mutagenesis 321 – 321 M -> A. Strongly decreased GTPase activity.
Mutagenesis 322 – 322 M -> A. Decreased GTPase activity.
Mutagenesis 323 – 323 T -> A. Abolished GTPase activity.
Mutagenesis 324 – 324 R -> A. Strongly decreased GTPase activity.



Literature citations
Molecular screening of 980 cases of suspected hereditary optic neuropathy with a report on 77 novel OPA1 mutations.
Ferre M.; Bonneau D.; Milea D.; Chevrollier A.; Verny C.; Dollfus H.; Ayuso C.; Defoort S.; Vignal C.; Zanlonghi X.; Charlin J.-F.; Kaplan J.; Odent S.; Hamel C.P.; Procaccio V.; Reynier P.; Amati-Bonneau P.;
Hum. Mutat. 30:E692-E705(2009)
Cited for: VARIANTS OPA1 MET-95; CYS-102; 293-VAL-VAL-294 DEL; ARG-310; THR-357; MET-382; PRO-396; 429-PRO-ASN-430 DEL; ASP-430; ARG-449; PHE-ILE-PHE-463 INS; LYS-487; ARG-545; TYR-551; GLN-590; PRO-593; LEU-646; ASP-768; TRP-781; TYR-823; LEU-882; PRO-887; CYS-932 AND PRO-949;
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.