Sequence information
Variant position: 301 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 463 The length of the canonical sequence.
Location on the sequence:
PILSPQEVVSCSQYAQGCEG
G FPYLIAGKYAQDFGLVEEAC
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.
Human PILSPQEVVSCSQYAQGCEGG FPYLIAGKYAQDFGLVEEAC
Mouse PILSPQEVVSCSPYAQGCDGG FPYLIAGKYAQDFGVVEESC
Rat PILSPQEVVSCSPYAQGCDGG FPYLIAGKYAQDFGVVEENC
Bovine PILSPQEVVSCSQYAQGCEGG FPYLIAGKYAQDFGLVEEDC
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.
Type Positions Description
Chain
231 – 394
Dipeptidyl peptidase 1 heavy chain
Binding site
302 – 302
Chloride
Binding site
304 – 304
Chloride; via amide nitrogen
Disulfide bond
291 – 331
Alternative sequence
138 – 463
Missing. In isoform 2.
Alternative sequence
142 – 463
Missing. In isoform 3.
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;
Identification of cathepsin C mutations in ethnically diverse Papillon-Lefevre syndrome patients.
Hart P.S.; Zhang Y.; Firatli E.; Uygur C.; Lotfazar M.; Michalec M.D.; Marks J.J.; Lu X.; Coates B.J.; Seow W.K.; Marshall R.; Williams D.; Reed J.B.; Wright J.T.; Hart T.C.;
J. Med. Genet. 37:927-932(2000)
Cited for: VARIANTS PLS 67-TYR--ALA-74 DEL; PRO-272; SER-300; VAL-301; SER-301; ASN-304; GLY-319; CYS-339; CYS-340 AND GLY-447; VARIANT THR-153;
Papillon-Lefevre syndrome: mutations and polymorphisms in the cathepsin C gene.
Nakano A.; Nomura K.; Nakano H.; Ono Y.; LaForgia S.; Pulkkinen L.; Hashimoto I.; Uitto J.;
J. Invest. Dermatol. 116:339-343(2001)
Cited for: VARIANTS PLS SER-39 AND SER-301; VARIANT VAL-453;
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.