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Literature summary for 3.4.22.54 extracted from

  • Charton, K.; Sarparanta, J.; Vihola, A.; Milic, A.; Jonson, P.H.; Suel, L.; Luque, H.; Boumela, I.; Richard, I.; Udd, B.
    CAPN3-mediated processing of C-terminal titin replaced by pathological cleavage in titinopathy (2015), Hum. Mol. Genet., 24, 3718-3731.
    View publication on PubMed
Search for more literature for 3.4.22.54

Protein Variants

Protein Variants Comment Organism
C129S inactive Homo sapiens
C129S inactive Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activated by Ca2+ Homo sapiens
Ca2+ activated by Ca2+ Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
titin + H2O Homo sapiens the enzyme binds the C-terminus of titin at recognition motifs [LIMV]X(3,4) [LIMV]X(2)[LIMV][DE] and [LIMV]X(3,4)[LIMVA]X(2)[LIMV][DE] ?
-
 ?
titin + H2O Mus musculus the enzyme binds the C-terminus of titin at recognition motifs [LIMV]X(3,4) [LIMV]X(2)[LIMV][DE] and [LIMV]X(3,4)[LIMVA]X(2)[LIMV][DE] ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P20807
-
-
Mus musculus Q64691
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Homo sapiens
-
skeletal muscle
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
titin + H2O the enzyme binds the C-terminus of titin at recognition motifs [LIMV]X(3,4) [LIMV]X(2)[LIMV][DE] and [LIMV]X(3,4)[LIMVA]X(2)[LIMV][DE] Homo sapiens ?
-
 ?
titin + H2O the enzyme binds the C-terminus of titin at recognition motifs [LIMV]X(3,4) [LIMV]X(2)[LIMV][DE] and [LIMV]X(3,4)[LIMVA]X(2)[LIMV][DE] Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
calpain 3
-
 Homo sapiens
calpain 3
-
 Mus musculus
CAPN3
-
 Homo sapiens
CAPN3
-
 Mus musculus

General Information

General Information Comment Organism
malfunction mutations in calpain 3 underlie limb-girdle muscular dystrophy 2A Homo sapiens
malfunction mutations in calpain 3 underlie limb-girdle muscular dystrophy 2A Mus musculus
physiological function proteolytic processing of C-terminal titin by calpain 3 has an important role in normal muscle Homo sapiens
physiological function proteolytic processing of C-terminal titin by calpain 3 has an important role in normal muscle Mus musculus