IED ID | IndEnz0002018446 |
Enzyme Type ID | protease018446 |
Protein Name |
Calpain-A EC 3.4.22.- Calcium-activated neutral proteinase A CANP A Cleaved into: Calpain-A catalytic subunit |
Gene Name | CalpA CG7563 |
Organism | Drosophila melanogaster (Fruit fly) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
Enzyme Sequence | MDDLRGFLRQAGQEFLNAAGEAAMGAAKDVVGSVINEIFIKKEADTKRVLPSIKNMRVLGEKSSSLGPYSEVQDYETILNSCLASGSLFEDPLFPASNESLQFSRRPDRHIEWLRPHEIAENPQFFVEGYSRFDVQQGELGDCWLLAATANLTQESNLFFRVIPAEQSFEENYAGIFHFRFWQYGKWVDVIIDDRLPTYNGELMYMHSTEKNEFWSALLEKAYAKLHGSYEALKGGSTCEAMEDFTGGVSEWYDLKEAPGNLFTILQKAAERNSMMGCSIEPDPNVTEAETPQGLIRGHAYSITKVCLIDIVTPNRQGKIPMIRMRNPWGNEAEWNGPWSDSSPEWRYIPEEQKAEIGLTFDRDGEFWMSFQDFLNHFDRVEICNLSPDSLTEDQQNSGKRKWEMSMYEGEWTPGVTAGGCRNFLDTFWHNPQYIITLVDPDEEDEEGQCTVIVALMQKNRRSKRNMGMECLTIGFAIYSLNDRELENRPQGLNFFRYKSSVGRSPHFINTREVCARFKLPPGHYLIVPSTFDPNEEGEFIIRVFSETQNNMEENDDHVGYGGKADTITPGFPTPKPIDPQKEGLRRLFDSIAGKDMEVDWMELKRILDHSMRDDLPKPVVFNRFSNNMAFETQAAGPGDDGAGACGLLSLICGPFLKGTPFEEQLGMNDQSNKRLIGDNPADGGPVTANAIVDETHGFSKDVCRSMVAMLDADKSGKLGFEEFETLLSEIAKWKAIFKVYDVENTGRVSGFQLREALNSAGYHLNNRVLNVLGHRYGSRDGKIAFDDFIMCAVKIKTYIDIFKERDTEKNETATFTLEEWIERTIYS |
Enzyme Length | 828 |
Uniprot Accession Number | Q11002 |
Absorption | |
Active Site | ACT_SITE 143; /evidence=ECO:0000250; ACT_SITE 299; /evidence=ECO:0000250; ACT_SITE 327; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Activated by millimolar concentrations of calcium, and by phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol and phosphatidic acid. {ECO:0000269|PubMed:10446155}. |
Binding Site | |
Calcium Binding | CA_BIND 712..723; /note=1; /evidence=ECO:0000305; CA_BIND 742..753; /note=2; /evidence=ECO:0000305 |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Involved in the organization of the actin-related cytoskeleton during embryogenesis. {ECO:0000269|PubMed:10446155, ECO:0000269|PubMed:7929201}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (2); Calcium binding (2); Chain (2); Domain (6); Erroneous initiation (1); Region (3); Sequence conflict (6); Site (1) |
Keywords | Alternative splicing;Autocatalytic cleavage;Calcium;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7823949}. |
Modified Residue | |
Post Translational Modification | PTM: Undergoes calcium-dependent autolytic cleavage between Lys-54 and Asn-55, which is necessary for activation of the protein. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10585440; 11438678; 11861563; 12586708; 12646209; 15250825; 15382138; 15451413; 15525665; 16336044; 1648232; 17998402; 18690061; 19380483; 19442719; 20220848; 20371351; 20670829; 20813047; 21074052; 21264297; 21858230; 22366109; 22701808; 22743648; 22827336; 22848598; 23000359; 23071443; 23722427; 23864715; 24739137; 25257175; 25848931; 26138338; 26912791; 27264536; 27582081; 27794539; 27837663; 29230001; 29476013; 29995573; 30242153; 30617798; 30705102; 31068592; 31722958; 32143742; 32678085; 32848200; 32973097; 33305734; 33563832; 34462500; 8908516; 9396712; 9571143; |
Motif | |
Gene Encoded By | |
Mass | 93,963 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.B36; |