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UniProtKB/Swiss-Prot P08294: Variant p.Arg231Gly

Extracellular superoxide dismutase [Cu-Zn]
Gene: SOD3
Variant information

Variant position:  231
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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 Glycine (G) at position 231 (R231G, p.Arg231Gly).
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 glycine (G)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Polymorphism:  The variant Gly-231 which is found in about 2.2% of individual displays a 10-fold increased plasma EC-SOD content due to reduced heparin-binding affinity and thus the impairment of its binding ability to endothelial cell surface.
Additional information on the polymorphism described.

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



Sequence information

Variant position:  231
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  240
The length of the canonical sequence.

Location on the sequence:   GVCGPGLWERQAREHSERKK  R RRESECKAA
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                         GVCGPGLWERQAREHSERKKRRRESECKAA------------------

Mouse                         GTSSSAAWESQTKE---RKKRRRESECKTT

Rat                           GTSNSEAWESQTKE---RKKRRRESECKTT

Rabbit                        GASGPAPWARQAQEHAERKKRRRESECKAA

Caenorhabditis elegans        GTVEERILETTTASLPPVTQSQPIGSSSYY

Drosophila                    GIK---------------------------

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 19 – 240 Extracellular superoxide dismutase [Cu-Zn]
Site 238 – 238 Not glycated
Glycosylation 229 – 229 N-linked (Glc) (glycation) lysine; in vitro
Glycosylation 230 – 230 N-linked (Glc) (glycation) lysine; in vitro


Literature citations

Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS THR-58; THR-91 AND GLY-231;

10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain.
Sandstrom J.; Nilsson P.; Karlsson K.; Marklund S.L.;
J. Biol. Chem. 269:19163-19166(1994)
Cited for: VARIANT GLY-231;

Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum.
Yamada H.; Yamada Y.; Adachi T.; Goto H.; Ogasawara N.; Futenma A.; Kitano M.; Hirano K.; Kato K.;
Jpn. J. Hum. Genet. 40:177-184(1995)
Cited for: VARIANT GLY-231;

Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface.
Adachi T.; Yamada H.; Yamada Y.; Morihara N.; Yamazaki N.; Murakami T.; Futenma A.; Kato K.; Hirano K.;
Biochem. J. 313:235-239(1996)
Cited for: VARIANT GLY-231;

An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases.
Adachi T.; Morihara N.; Yamazaki N.; Yamada H.; Futenma A.; Kato K.; Hirano K.;
J. Biochem. 120:184-188(1996)
Cited for: VARIANT GLY-231;

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.