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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04181: Variant p.Val332Met

Ornithine aminotransferase, mitochondrial
Gene: OAT
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Variant information Variant position: help 332 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 Valine (V) to Methionine (M) at position 332 (V332M, p.Val332Met). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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
Variant description: help In HOGA; loss of protein stability; loss of ornithine aminotransferase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 332 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 439 The length of the canonical sequence.
Location on the sequence: help LTIKPGEHGSTYGGNPLGCR V AIAALEVLEEENLAENADKL 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                         LTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKL

Mouse                         LTIKPGEHGSTYGGNPLGCRIAIAALEVLEEENLAENADKM

Rat                           LTIKPGEHGSTYGGNPLGCRIAIAALEVLEEEHLAENADKM

Bovine                        LTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENAEKM

Caenorhabditis elegans        MNIKPGEHGSTYGGNPLACKVAIAALEILQEEKLVENSAVM

Drosophila                    LCIKPGEHGSTYGGNPLGCRVAMAALEVLQEEKLAENAFKM

Slime mold                    LTIKPGEHGSTYGGSPLASAVAMAALDVLRDENLAENAQKL

Baker's yeast                 SCFTPGSHGSTFGGNPLASRVAIAALEVIRDEKLCQRAAQL

Fission yeast                 LNFEPGTHGSTYGGNPLGAAVSIAALEVVKEEKLTERAAVL
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 26 – 439 Ornithine aminotransferase, hepatic form
Chain 36 – 439 Ornithine aminotransferase, renal form
Helix 327 – 342



Literature citations
Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy.
Ramesh V.; McClatchey A.I.; Ramesh N.; Benoit L.A.; Berson E.L.; Shih V.E.; Gusella J.F.;
Proc. Natl. Acad. Sci. U.S.A. 85:3777-3780(1988)
Cited for: VARIANTS HOGA LYS-54 AND MET-332; 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; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; 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.