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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P57727: Variant p.Asp103Gly

Transmembrane protease serine 3
Gene: TMPRSS3
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Variant information Variant position: help 103 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 Aspartate (D) to Glycine (G) at position 103 (D103G, p.Asp103Gly). 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 medium size and acidic (D) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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 DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 103 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 454 The length of the canonical sequence.
Location on the sequence: help FKCIELIARCDGVSDCKDGE D EYRCVRVGGQNAVLQVFTAA 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                         FKCIELIARCDGVSDCKDGEDEYRCVRVGGQNAVLQVFTAA

Mouse                         FKCIELTARCDGVSDCKNAEDEYRCVRVSGQRAALQVFTAA
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 – 454 Transmembrane protease serine 3
Topological domain 70 – 454 Extracellular
Domain 72 – 108 LDL-receptor class A
Disulfide bond 92 – 107
Alternative sequence 1 – 127 Missing. In isoform B.



Literature citations
The transmembrane serine protease (TMPRSS3) mutated in deafness DFNB8/10 activates the epithelial sodium channel (ENaC) in vitro.
Guipponi M.; Vuagniaux G.; Wattenhofer M.; Shibuya K.; Vazquez M.; Dougherty L.; Scamuffa N.; Guida E.; Okui M.; Rossier C.; Hancock M.; Buchet K.; Reymond A.; Hummler E.; Marzella P.L.; Kudoh J.; Shimizu N.; Scott H.S.; Antonarakis S.E.; Rossier B.C.;
Hum. Mol. Genet. 11:2829-2836(2002)
Cited for: SUBCELLULAR LOCATION; AUTOCATALYTIC CLEAVAGE; MUTAGENESIS OF SER-401; CHARACTERIZATION OF VARIANTS DFNB8 GLY-103; TRP-109; PHE-194; CYS-251; LEU-404 AND ARG-407; FUNCTION IN ENAC CLEAVAGE; Mutations in the TMPRSS3 gene are a rare cause of childhood nonsyndromic deafness in Caucasian patients.
Wattenhofer M.; Di Iorio V.; Rabionet R.; Dougherty L.; Pampanos A.; Schwede T.; Montserrat-Sentis B.; Arbones L.; Iliades T.; Pasquadibisceglie A.; D'Amelio M.; Alwan S.; Rossier C.; Dahl H.-H.M.; Petersen M.B.; Estivill X.; Gasparini P.; Scott H.S.; Antonarakis S.E.;
J. Mol. Med. 80:124-131(2002)
Cited for: VARIANTS DFNB8 GLY-103 AND THR-426; VARIANT ASN-173;
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.