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UniProtKB/Swiss-Prot P53634: Variant p.Tyr347Cys

Dipeptidyl peptidase 1
Gene: CTSC
Variant information

Variant position:  347
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Tyrosine (Y) to Cysteine (C) at position 347 (Y347C, p.Tyr347Cys).
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:  Change from large size and aromatic (Y) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Variant description:  In PLS and AP1.
Any additional useful information about the variant.

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

Sequence information

Variant position:  347
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  463
The length of the canonical 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.





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.

Chain 231 – 394 Dipeptidyl peptidase 1 heavy chain
Binding site 347 – 347 Chloride
Alternative sequence 138 – 463 Missing. In isoform 2.
Alternative sequence 142 – 463 Missing. In isoform 3.
Beta strand 342 – 347

Literature citations

Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis.
Toomes C.; James J.; Wood A.J.; Wu C.L.; McCormick D.; Lench N.; Hewitt C.; Moynihan L.; Roberts E.; Woods C.G.; Markham A.; Wong M.; Widmer R.; Ghaffar K.A.; Pemberton M.; Hussein I.R.; Temtamy S.A.; Davies R.; Read A.P.; Sloan P.; Dixon M.J.; Thakker N.S.;
Nat. Genet. 23:421-424(1999)
Cited for: VARIANTS PLS PHE-249; LEU-252; PRO-272; SER-301; CYS-339 AND CYS-347;

Localisation of a gene for prepubertal periodontitis to chromosome 11q14 and identification of a cathepsin C gene mutation.
Hart T.C.; Hart P.S.; Michalec M.D.; Zhang Y.; Marazita M.L.; Cooper M.; Yassin O.M.; Nusier M.; Walker S.;
J. Med. Genet. 37:95-101(2000)

The role of cathepsin C in Papillon-Lefevre syndrome, prepubertal periodontitis, and aggressive periodontitis.
Hewitt C.; McCormick D.; Linden G.; Turk D.; Stern I.; Wallace I.; Southern L.; Zhang L.; Howard R.; Bullon P.; Wong M.; Widmer R.; Gaffar K.A.; Awawdeh L.; Briggs J.; Yaghmai R.; Jabs E.W.; Hoeger P.; Bleck O.; Rudiger S.G.; Petersilka G.; Battino M.; Brett P.; Hattab F.; Al-Hamed M.; Sloan P.; Toomes C.; Dixon M.J.; James J.; Read A.P.; Thakker N.S.;
Hum. Mutat. 23:222-228(2004)
Cited for: VARIANTS PLS GLU-129; ARG-139; TYR-236; PHE-249; LEU-252; HIS-272; SER-301; ARG-312; CYS-339; CYS-347 AND GLY-447; VARIANTS AP1 HIS-272 AND CYS-412; VARIANT THR-153;

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.