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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22570: Variant p.Arg386Trp

NADPH:adrenodoxin oxidoreductase, mitochondrial
Gene: FDXR
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Variant information Variant position: help 386 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 Arginine (R) to Tryptophan (W) at position 386 (R386W, p.Arg386Trp). 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 large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 MMDS9B; likely pathogenic; decreased NADPH-adrenodoxin reductase activity. Any additional useful information about the variant.


Sequence information Variant position: help 386 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 491 The length of the canonical sequence.
Location on the sequence: help PVDPSVPFDSKLGVIPNVEG R VMDVPGLYCSGWVKRGPTGV 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                         PV----DPSVPFDSKLGVIPNVEGRVMD-------VPGLYCSGWVKRGPTGV

Mouse                         PI----DPSVPFDPKLGVIPNTEGRVVN-------VPGLYC

Rat                           PI----DPSVPFDPKLGIIPNTEGRVVN-------APGLYC

Bovine                        PI----DPSVPFDPKLGVVPNMEGRVVD-------VPGLYC

Drosophila                    CV----DTGINFDTRRGRVHNINGRILKDDATGEVDPGLYV

Slime mold                    KQ----FPSVPFDFNSVSIPNKYGKVLEEPNSDKFINGLYV

Baker's yeast                 PMPEFSKLSIGFDKDH--IANKQGRVLT--SSGEIFPHLYA

Fission yeast                 PLPGMKDVGVPFDDAKGIVKNVNGFVR---------PGIYT
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 33 – 491 NADPH:adrenodoxin oxidoreductase, mitochondrial
Binding site 398 – 398
Binding site 405 – 405



Literature citations
Biallelic mutations in the ferredoxin reductase gene cause novel mitochondriopathy with optic atrophy.
Peng Y.; Shinde D.N.; Valencia C.A.; Mo J.S.; Rosenfeld J.; Truitt Cho M.; Chamberlin A.; Li Z.; Liu J.; Gui B.; Brockhage R.; Basinger A.; Alvarez-Leon B.; Heydemann P.; Magoulas P.L.; Lewis A.M.; Scaglia F.; Gril S.; Chong S.C.; Bower M.; Monaghan K.G.; Willaert R.; Plona M.R.; Dineen R.; Milan F.; Hoganson G.; Powis Z.; Helbig K.L.; Keller-Ramey J.; Harris B.; Anderson L.C.; Green T.; Sukoff Rizzo S.J.; Kaylor J.; Chen J.; Guan M.X.; Sellars E.; Sparagana S.P.; Gibson J.B.; Reinholdt L.G.; Tang S.; Huang T.;
Hum. Mol. Genet. 26:4937-4950(2017)
Cited for: SUBCELLULAR LOCATION; VARIANTS MMDS9B LEU-51; LEU-74; PHE-143; MET-158; ALA-205; PHE-207; 274-LYS--HIS-491 DEL; TYR-353; ASN-368; TRP-386; SER-437 AND CYS-437; CHARACTERIZATION OF VARIANT MMDS9B TRP-386; INVOLVEMENT IN MMDS9B; Expanding the clinical and genetic spectrum of FDXR deficiency by functional validation of variants of uncertain significance.
Stenton S.L.; Piekutowska-Abramczuk D.; Kulterer L.; Kopajtich R.; Claeys K.G.; Ciara E.; Eisen J.; Ploski R.; Pronicka E.; Malczyk K.; Wagner M.; Wortmann S.B.; Prokisch H.;
Hum. Mutat. 42:310-319(2021)
Cited for: VARIANTS MMDS9B TRP-12; SER-109; ALA-111; 189-LEU--ALA-192 DEL; VAL-211; LEU-228; TYR-353; TRP-386 AND GLN-448; INVOLVEMENT IN MMDS9B;
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.