Detail Information for IndEnz0002018627
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;