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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
Type of variant: help LP/P [Disclaimer]
Residue change: help From Valine (V) to Methionine (M) at position 332 (V332M, p.Val332Met).
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and hydrophobic.
BLOSUM score: help 1
Variant description: help In HOGA; loss of protein stability; loss of ornithine aminotransferase activity.
Other resources: help


Sequence information Variant position: help 332
Protein sequence length: help 439
Location on the sequence: help LTIKPGEHGSTYGGNPLGCR V AIAALEVLEEENLAENADKL
Residue conservation: help
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
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.