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UniProtKB/Swiss-Prot O60313: Variant p.Ala357Thr

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

Variant position:  357
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 Alanine (A) to Threonine (T) at position 357 (A357T, p.Ala357Thr).
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 small size and hydrophobic (A) to medium size and polar (T)
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 DOA+ and OPA1.
Any additional useful information about the variant.

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



Sequence information

Variant position:  357
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:   HVALFKDSSREFDLTKEEDL  A ALRHEIELRMRKNVKEGCTV
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                         HVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTV

Mouse                         HVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTV

Rat                           HVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTV

Chicken                       HVALFKDSSREFDLTKEEDLAALRNEIEIRMRNSVKEGCTV

Zebrafish                     HVAMFKDSSREFDLGKEEDLAALRHEIELRMRKSVKEGQTV

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
Helix 353 – 370


Literature citations

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;

OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes.
Amati-Bonneau P.; Valentino M.L.; Reynier P.; Gallardo M.E.; Bornstein B.; Boissiere A.; Campos Y.; Rivera H.; de la Aleja J.G.; Carroccia R.; Iommarini L.; Labauge P.; Figarella-Branger D.; Marcorelles P.; Furby A.; Beauvais K.; Letournel F.; Liguori R.; La Morgia C.; Montagna P.; Liguori M.; Zanna C.; Rugolo M.; Cossarizza A.; Wissinger B.; Verny C.; Schwarzenbacher R.; Martin M.A.; Arenas J.; Ayuso C.; Garesse R.; Lenaers G.; Bonneau D.; Carelli V.;
Brain 131:338-351(2008)
Cited for: VARIANTS DOA+ THR-357; VAL-439; HIS-445; ARG-545 AND ASP-910; FUNCTION;

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; 463-ILE-PHE-464 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.