Variant position: 226 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:
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 I--------IPYNDLPALERALQDP---NVA AFMVEPIQGEAGVVVPDPGYL
Mouse T--------IPYNDLPALERALQDP---NVA AFMVEPIQGE
Rat T--------IPYNDLPALERALQDP---NVA AFMVEPIQGE
Bovine I--------IPYNDLPALERALQDP---NVA AFMVEPIQGE
Caenorhabditis elegans T--------VPYNNLKAVEDAIKDK---NVA AFMVEPIQGE
Drosophila L--------IEYDNVSALEESLKDP---NVC AFMVEPIQGE
Slime mold K--------IDYNSTQQLEEVLSQH-ADRVC GFIVEPIQGE
Baker's yeast S--GHSVHKIRYGHAEDFVPILESPEGKNVA AIILEPIQGE
Fission yeast PKISGADRVLRYNNIEDLKYYLDTF-GPKVA AFLVEPIQGE
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.
Type Positions Description
26 – 439 Ornithine aminotransferase, hepatic form
36 – 439 Ornithine aminotransferase, renal form
224 – 229
Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V.
Michaud J.; Thompson G.N.; Brody L.C.; Steel G.; Obie C.; Fontaine G.; Schappert K.; Keith C.G.; Valle D.; Mitchell G.A.;
Am. J. Hum. Genet. 56:616-622(1995)
Cited for: VARIANT HOGA VAL-226;
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;
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.