IED ID | IndEnz0002018627 |
Enzyme Type ID | protease018627 |
Protein Name |
Calpain-B EC 3.4.22.- Calcium-activated neutral proteinase B CANP B Cleaved into: Calpain-B catalytic subunit 1; Calpain-B catalytic subunit 2 |
Gene Name | CalpB CG8107 |
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 | MYGIDNYPKNYHASGIGLVNLAALGYSKNEVSGGNEGGGAPKPKAGLYPSLPYPSSESVGGMPYVVKQTSHAQNASYAGPTMGMGMPVPEAPSAPAPYPSATPYPGSGLYPSLPSANVSSLPYPTAPMAPYPTGMPYPTGMPQPNLPYPAAPLAPYPSAMPGLPGMPMPYAPMPTSPAPQHNIGFPALPYPTAPPPESAPTQEEEPSVGVAELSFTSVKVPENQNMFWMGRKATSARQNSVSKGDFQSLRDSCLANGTMFEDPDFPATNASLMYSRRPDRYYEWLRPGDIADDPQFFVEGYSRFDVQQGELGDCWLLAAAANLTQDSTLFFRVIPPDQDFQENYAGIFHFKFWQYGKWVEVVIDDRLPTYNGELIYMHSTEKNEFWSALLEKAYAKLHGSYEALKGGTTCEAMEDFTGGVTEWYDIKEAPPNLFSIMMKAAERGSMMGCSLEPDPHVLEAETPQGLIRGHAYSITKVCLMDISTPNRQGKLPMIRMRNPWGNDAEWSGPWSDSSPEWRFIPEHTKEEIGLNFDRDGEFWMSFQDFLNHFDRVEICNLSPDSLTEDQQHSSRRKWEMSMFEGEWTSGVTAGGCRNFLETFWHNPQYIISLEDPDDEDDDGKCTAIVALMQKNRRSKRNVGIDCLTIGFAIYHLTDRDMQVKPQGLNFFKYRASVARSPHFINTREVCARFKLPPGHYLIVPSTFDPNEEGEFIIRVFSETRNNMEENDDEVGFGETDDRIAPSLPPPTPKEEDDPQRIALRRLFDSVAGSDEEVDWQELKRILDHSMRDVMVGSDGFSKDAVRSMVAMLDKDRSGRLGFEEFEALLTDIAKWRAVFKLYDTRRTGSIDGFHLRGALNSAGYHLNNRLLNALAHRYGSREGQIPFDDFLMCAIKVRTFIEMFRERDTDNSDTAFFNLDDWLERTIYS |
Enzyme Length | 925 |
Uniprot Accession Number | Q9VT65 |
Absorption | |
Active Site | ACT_SITE 314; /evidence=ECO:0000250|UniProtKB:Q07009; ACT_SITE 470; /evidence=ECO:0000250|UniProtKB:Q07009; ACT_SITE 498; /evidence=ECO:0000250|UniProtKB:Q07009 |
Activity Regulation | ACTIVITY REGULATION: Activated by millimolar concentrations of calcium. {ECO:0000269|PubMed:10446155}. |
Binding Site | |
Calcium Binding | CA_BIND 809..820; /note=1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; CA_BIND 839..850; /note=2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Calcium-regulated non-lysosomal thiol-protease. {ECO:0000269|PubMed:10446155}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Calcium binding (2); Chain (3); Domain (3); Mutagenesis (2); Region (4); Sequence conflict (6); Site (2) |
Keywords | Autocatalytic cleavage;Calcium;Cytoplasm;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease |
Interact With | P12370 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14614768}. Membrane {ECO:0000269|PubMed:14614768}. Note=Translocates to intracellular membranes when calcium levels are increased. |
Modified Residue | |
Post Translational Modification | PTM: Undergoes calcium-dependent autolytic cleavage between Asn-74 and Ala-75 and between Gln-224 and Asn-225 to produce two major products, calpain B catalytic subunit 1 and calpain B catalytic subunit 2. This autolysis is necessary for activation of the protein. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11162675; 11985896; 12646209; 14605208; 14976200; 14988399; 15250825; 15382138; 15451413; 15575970; 15640802; 15710747; 16212942; 18032413; 19442719; 19581587; 19694808; 20041201; 20214937; 20220848; 20371351; 21074052; 21356551; 21669932; 21858230; 22496853; 22701808; 22827336; 23071443; 23722427; 23864715; 23944235; 24705267; 25449646; 26138338; 26370122; 26512413; 26870755; 27153400; 27264536; 27894253; 27960592; 28231245; 29230001; 29476013; 29995573; 30298734; 30705102; 31068592; 31412687; 31722958; 32678085; 32848200; 33305734; |
Motif | |
Gene Encoded By | |
Mass | 103,814 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.B37; |