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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50336: Variant p.Leu295Pro

Protoporphyrinogen oxidase
Gene: PPOX
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Variant information Variant position: help 295 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 Leucine (L) to Proline (P) at position 295 (L295P, p.Leu295Pro). 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 -3 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 VP; strongly decreases enzyme activity; impairs protein folding and/or stability. Any additional useful information about the variant.


Sequence information Variant position: help 295 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 477 The length of the canonical sequence.
Location on the sequence: help SSLEADHVISAIPASVLSEL L PAEAAPLARALSAITAVSVA 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                         SSL------EADHVISAIPASVLSELL--PAEAAPLARALSAITAVSVA

Mouse                         SSL------EADHIISAIPASELSKLL--PAEAAPLARILS

Bovine                        SSL------EADHIISAIPASVLSKLL--PAEATPLARALS

Slime mold                    QY-------QYDQLISTIPLNQLAPMF--KKSDSKLYQLLQ

Baker's yeast                 QYE------TFDHLRLTITPPKIAKLL--PKDQNSLSKLLD

Fission yeast                 QSLVDVNGQAYEYVVFANSSRNLENLISCPKMETPTS----

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 1 – 477 Protoporphyrinogen oxidase
Mutagenesis 284 – 284 S -> I. Decreases enzyme activity by 87%. Impairs protein folding and/or stability.
Mutagenesis 290 – 290 V -> L. No effect on enzyme activity.



Literature citations
Structural insight into human variegate porphyria disease.
Qin X.; Tan Y.; Wang L.; Wang Z.; Wang B.; Wen X.; Yang G.; Xi Z.; Shen Y.;
FASEB J. 25:653-664(2011)
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453; MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368; Variegate porphyria in Western Europe: identification of PPOX gene mutations in 104 families, extent of allelic heterogeneity, and absence of correlation between phenotype and type of mutation.
Whatley S.D.; Puy H.; Morgan R.R.; Robreau A.M.; Roberts A.G.; Nordmann Y.; Elder G.H.; Deybach J.C.;
Am. J. Hum. Genet. 65:984-994(1999)
Cited for: VARIANTS ARG-256 AND HIS-304; VARIANTS VP PRO-38; GLU-40; PRO-73; GLY-84; PRO-85; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-172; ARG-232; HIS-281 DEL; ASP-282; PRO-295; GLY-335; PRO-350; PRO-444; ARG-453 AND VAL-453;
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.