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UniProtKB/Swiss-Prot P04181: Variant p.Glu318Lys

Ornithine aminotransferase, mitochondrial
Gene: OAT
Chromosomal location: 10q26
Variant information

Variant position:  318
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glutamate (E) to Lysine (K) at position 318 (E318K, p.Glu318Lys).
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 medium size and acidic (E) to large size and basic (K)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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

Involvement in disease:  Hyperornithinemia with gyrate atrophy of choroid and retina (HOGA) [MIM:258870]: A disorder clinically characterized by a triad of progressive chorioretinal degeneration, early cataract formation, and type II muscle fiber atrophy. Characteristic chorioretinal atrophy with progressive constriction of the visual fields leads to blindness at the latest during the sixth decade of life. Patients generally have normal intelligence. {ECO:0000269|PubMed:1612597, ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989, ECO:0000269|PubMed:2793865, ECO:0000269|PubMed:3375240, ECO:0000269|PubMed:7668253, ECO:0000269|PubMed:7887415}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In HOGA; loss of activity and protein stability.
Any additional useful information about the variant.

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



Sequence information

Variant position:  318
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  439
The length of the canonical sequence.

Location on the sequence:   LYPVSAVLCDDDIMLTIKPG  E HGSTYGGNPLGCRVAIAALE
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                         LYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALE

Mouse                         LYPVSAVLCDDEIMLTIKPGEHGSTYGGNPLGCRIAIAALE

Rat                           LYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRIAIAALE

Bovine                        LYPVSAVLCDDEIMLTIKPGEHGSTYGGNPLGCRVAIAALE

Caenorhabditis elegans        FYPVSAVLCDDNVMMNIKPGEHGSTYGGNPLACKVAIAALE

Drosophila                    MYPVSAVLCNDQVMLCIKPGEHGSTYGGNPLGCRVAMAALE

Slime mold                    LLPISAVLGGKDVMLTIKPGEHGSTYGGSPLASAVAMAALD

Baker's yeast                 VLPVSCVLSSHDIMSCFTPGSHGSTFGGNPLASRVAIAALE

Fission yeast                 VYPVSAVLSSREIMLNFEPGTHGSTYGGNPLGAAVSIAALE

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 26 – 439 Ornithine aminotransferase, hepatic form
Chain 36 – 439 Ornithine aminotransferase, renal form


Literature citations

Functional analysis of missense mutations of OAT, causing gyrate atrophy of choroid and retina.
Doimo M.; Desbats M.A.; Baldoin M.C.; Lenzini E.; Basso G.; Murphy E.; Graziano C.; Seri M.; Burlina A.; Sartori G.; Trevisson E.; Salviati L.;
Hum. Mutat. 34:229-236(2013)
Cited for: VARIANTS HOGA ASP-51; ARG-104; GLN-199; LYS-318; MET-332; TYR-394; LEU-417; ASN-436 AND PHE-437; CHARACTERIZATION OF ASP-51; ARG-104; GLN-199; VAL-226; LYS-318; MET-332; TYR-394; LEU-402; LEU-417; ASN-436 AND PHE-437; SUBUNIT; SUBCELLULAR LOCATION;

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.