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UniProtKB/Swiss-Prot P55789: Variant p.Arg194His

FAD-linked sulfhydryl oxidase ALR
Gene: GFER
Variant information

Variant position:  194
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 Arginine (R) to Histidine (H) at position 194 (R194H, p.Arg194His).
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 large size and basic (R) to medium size and polar (H)
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 MPMCHD; less stable than the wild-type protein within the mitochondria, increased rate of dissociation of FAD by about 45-fold.
Any additional useful information about the variant.

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



Sequence information

Variant position:  194
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  205
The length of the canonical sequence.

Location on the sequence:   HNEVNRKLGKPDFDCSKVDE  R WRDGWKDGSCD
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                         HNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD

Mouse                         HNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD

Rat                           HNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD

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 1 – 205 FAD-linked sulfhydryl oxidase ALR
Domain 95 – 195 ERV/ALR sulfhydryl oxidase
Nucleotide binding 194 – 195 FAD
Disulfide bond 204 – 204 Interchain (with C-95)
Helix 191 – 195


Literature citations

Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy.
Daithankar V.N.; Schaefer S.A.; Dong M.; Bahnson B.J.; Thorpe C.;
Biochemistry 49:6737-6745(2010)
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 81-205; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; DISULFIDE BONDS; FAD-BINDING SITES; CHARACTERIZATION OF VARIANT MPMCHD HIS-194;

The mitochondrial disulfide relay system protein GFER is mutated in autosomal-recessive myopathy with cataract and combined respiratory-chain deficiency.
Di Fonzo A.; Ronchi D.; Lodi T.; Fassone E.; Tigano M.; Lamperti C.; Corti S.; Bordoni A.; Fortunato F.; Nizzardo M.; Napoli L.; Donadoni C.; Salani S.; Saladino F.; Moggio M.; Bresolin N.; Ferrero I.; Comi G.P.;
Am. J. Hum. Genet. 84:594-604(2009)
Cited for: VARIANT MPMCHD HIS-194; CHARACTERIZATION OF VARIANT MPMCHD HIS-194; TISSUE SPECIFICITY;

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.