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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O43933: Variant p.Leu664Pro

Peroxisomal ATPase PEX1
Gene: PEX1
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Variant information Variant position: help 664 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 664 (L664P, p.Leu664Pro). 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 PBD1A and PBD1B; decreased binding to PEX6; impaired protein import into peroxisomes. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 664 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1283 The length of the canonical sequence.
Location on the sequence: help LEVAFSEAVWMQPSVVLLDD L DLIAGLPAVPEHEHSPDAVQ 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                         LEVAFSEAVWMQ---------------PSVVLLDDLDLIAGLPAVPEHEHSPDA---VQ

Mouse                         LEVAFSEAAWRQ---------------PSVILLDDLDLIAG

Slime mold                    FNKLFYKSCKESGNTLSATTSTNTTPPPIIIILESLDLILG

Baker's yeast                 IMEWCSFCYWYG---------------PSLIVLDNVEALFG

Fission yeast                 WNNVFIQAERYE---------------PSIIYLDDVHCLIS
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 – 1283 Peroxisomal ATPase PEX1
Mutagenesis 662 – 662 D -> N. In B1 mutant; abolished ATP hydrolysis; decreased interaction with PEX6; decreased localization to peroxisomal membranes.



Literature citations
Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I.
Tamura S.; Okumoto K.; Toyama R.; Shimozawa N.; Tsukamoto T.; Suzuki Y.; Osumi T.; Kondo N.; Fujiki Y.;
Proc. Natl. Acad. Sci. U.S.A. 95:4350-4355(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS PBD1A 634-GLY--HIS-690 DEL; PRO-664 AND ASP-843; VARIANTS PBD1B 634-GLY--HIS-690 DEL; PRO-664 AND ASP-843; Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p.
Tamura S.; Yasutake S.; Matsumoto N.; Fujiki Y.;
J. Biol. Chem. 281:27693-27704(2006)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; INTERACTION WITH PEX6; MUTAGENESIS OF LYS-605; ASP-662; LYS-887 AND ASP-940; CHARACTERIZATION OF VARIANT PBD1A PRO-664;
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.