Detail Information for IndEnz0002004459
IED ID IndEnz0002004459
Enzyme Type ID protease004459
Protein Name COP9 signalosome complex subunit 5
Dch5
Signalosome subunit 5
EC 3.4.-.-
JAB1 homolog
Gene Name CSN5 quo CG14884
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 MDSDAAQKTWELENNIQTLPSCDEIFRYDAEQQRQIIDAKPWEKDPHFFKDIKISALALLKMVMHARSGGTLEVMGLMLGKVEDNTMIVMDAFALPVEGTETRVNAQAQAYEYMTAYMEAAKEVGRMEHAVGWYHSHPGYGCWLSGIDVSTQMLNQTYQEPFVAIVVDPVRTVSAGKVCLGAFRTYPKGYKPPNEEPSEYQTIPLNKIEDFGVHCKQYYPLEISYFKSALDRRLLDSLWNKYWVNTLGSSGLLTNTEYTTGQIMDLSEKLEQSENFLGRGTDVNEKRSEDKLSKATRDCSRSTIELIHGLMAQIVKDKLFNKVGLGK
Enzyme Length 327
Uniprot Accession Number Q9XZ58
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.-.-
Enzyme Function FUNCTION: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. The CSN complex plays an essential role in oogenesis and embryogenesis and is required for proper photoreceptor R cell differentiation and promote lamina glial cell migration or axon targeting. It also promotes Ubl-dependent degradation of cyclin E (CycE) during early oogenesis. Also involved in regulation of axis formation by checkpoint-dependent, translational control of Gurken. {ECO:0000269|PubMed:11779478, ECO:0000269|PubMed:12183637, ECO:0000269|PubMed:12223399, ECO:0000269|PubMed:12397113, ECO:0000269|PubMed:12737805}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Erroneous initiation (1); Metal binding (3); Modified residue (3); Motif (1); Mutagenesis (6); Sequence conflict (3)
Keywords Cytoplasm;Developmental protein;Differentiation;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Oogenesis;Phosphoprotein;Protease;Reference proteome;Signalosome;Zinc
Interact With Q9VCY3; Q7KRW1
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus {ECO:0000305|PubMed:10531038}.
Modified Residue MOD_RES 300; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 302; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 303; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18327897
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10471706; 10782111; 12415283; 12593986; 12850443; 14570571; 14578910; 14605208; 15037551; 15474165; 15571808; 15575970; 15857915; 15922834; 15927177; 16127432; 16216235; 16496002; 17041588; 17251548; 17295838; 17486136; 18298797; 18493598; 18782863; 18926707; 19064709; 19176824; 19363474; 19855832; 19859546; 20068067; 20691177; 20800474; 21145488; 21205937; 21548953; 21576393; 21849035; 22036573; 22050674; 22589731; 22935612; 22937016; 23071443; 23275879; 23583758; 23637332; 23899565; 24362437; 24576427; 25106867; 25119050; 25312911; 25329560; 25393278; 25459658; 25992709; 26672093; 26870755; 26912791; 28619822; 29029226; 29764959; 32653676; 33382409; 33535499; 33561251; 33988679;
Motif MOTIF 135..148; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Gene Encoded By
Mass 37,083
Kinetics
Metal Binding METAL 135; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 137; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 148; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Rhea ID
Cross Reference Brenda