Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q5JRX3: Variant p.Phe169Ser

Presequence protease, mitochondrial
Gene: PITRM1
Feedback?
Variant information Variant position: help 169 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Phenylalanine (F) to Serine (S) at position 169 (F169S, p.Phe169Ser). 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 Change from large size and aromatic (F) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 169 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1037 The length of the canonical sequence.
Location on the sequence: help STQNPKDFQNLLSVYLDATF F PCLRELDFWQEGWRLEHENP 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                         STQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENP

Mouse                         STQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENP

Xenopus laevis                STQNAKDFQNLLSVYLDAVFFPCLRELDFWQEGWRLEHENP

Xenopus tropicalis            STQNAKDFQNLLSVYLDAVFFPCLRELDFWQEGWRLEHENP

Zebrafish                     STQNAKDFQNLLSVYLDAVFFPCLRELDFWQEGWRLEHENP

Drosophila                    STMNEIDFRNLQHIYLDAVFRPNLAYFDFLQEGWRLENKDI

Baker's yeast                 STTNPQDFANLRGVYLDSTLNPLLKQEDFDQEGWRLEHKNI

Fission yeast                 ATVNTTDYKNLRDVYLDATLFPKLRKLDFLQEGWRFEHADV

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 29 – 1037 Presequence protease, mitochondrial
Active site 180 – 180
Disulfide bond 119 – 556
Mutagenesis 183 – 183 R -> AKN. Decreased metalloendopeptidase activity towards an amyloid-beta peptide derivative.
Mutagenesis 183 – 183 R -> DE. Loss of metalloendopeptidase activity towards an amyloid-beta peptide derivative.
Mutagenesis 185 – 185 E -> A. Loss of metalloendopeptidase activity towards an amyloid-beta peptide derivative.
Mutagenesis 185 – 185 E -> DQ. No effect on metalloendopeptidase activity towards an amyloid-beta peptide derivative.
Mutagenesis 185 – 185 E -> RKN. Decreased metalloendopeptidase activity towards an amyloid-beta peptide derivative.



Literature citations
Cloning, expression, and characterization of human metalloprotease 1: a novel member of the pitrilysin family of metalloendoproteases.
Mzhavia N.; Berman Y.L.; Qian Y.; Yan L.; Devi L.A.;
DNA Cell Biol. 18:369-380(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2); FUNCTION; CATALYTIC ACTIVITY; ACTIVITY REGULATION; BIOPHYSICOCHEMICAL PROPERTIES; TISSUE SPECIFICITY; VARIANTS SER-169; VAL-328; VAL-397; ILE-621 AND ARG-1037;
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.