Detail Information for IndEnz0002012433
IED ID IndEnz0002012433
Enzyme Type ID protease012433
Protein Name Ubiquitin carboxyl-terminal hydrolase 47
EC 3.4.19.12
Ubiquitin thioesterase 47
Ubiquitin-specific-processing protease 47
Gene Name Usp47 Ubp64E CG5486
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 MTDKESEQCTVSVFDQTPGSEQKKINVVVRSHFTVKRVIDLIGTQFSYEKFELLLQPHDNKDLVNLNALESQLMYEVAGFEPQLKNHLILLPSGSWDGDVTKRFELPIKRVVVKKVMKSDGEKAKSPATGEKKKRVVGEKTKKKPASGSSSPSKAKTTSEDSLAKTSISSESSPEKTSKIKTTAAKISKPGSEKAPRASPEECPELSTEINSKNTSSESPVAKKTAKVTSKPTLELLSPIKPSSPIKELDCEPVDTLSKQQLSEQLQLYPQGRNLISPVDDAPSDLFISDAEQLSDDDLALGASASPTMLGPGYDYGAPTGDSDVEGVTGVTDPSTIGTDDGTYPALSNFYRRKYGGDELRAWQRVNTTGADFVSSATTETEAEARQASLGPRGYVGLVNQAMTCYLNSLLQALFMTPEFRNALYRWEFDNDNEAKNIPYQLQKLFLNLQTSPKAAVETTDLTRSFGWDSTEAWQQHDIQELCRVMFDALEHKFKNTKQANLISNLYEGKMNDYVKCLECNTEKTREDTFLDIPLPVRPFGSSSAYGSIEEALRAFVQPETLDGNNQYLCEKCKKKCDAHKGLHFKSFPYILTLHLKRFDFDYQTMHRIKLNDRVTFPQTLNLNTFINRSGNSGEQNSQLNGTVDDCSTADSGSAMEDDNLSSGVVTTASSSQHENDLNDEDEGIDMSSSTSKSAKQGSGPYLYELFAIMIHSGSASGGHYYAYIKDFDNNEWFCFNDQNVTSITQEDIQRSFGGPNGSYYSSAYTSSTNAYMLMYRQVDAKRNELVAKVADFPEHIKTLLPKLHSEEETRVSRLGRHITVTDLALPDLYKPRVYFYNPSLKKMKITRVYVSQSFNINLVLMSAYEMLNVEQFAPLSRCRLVAYNSSMDTIIQSLESCTDPALTELRAAQNYSLDFLLEYRAEDQEFEVYPPNGITWYVFKVDLSTMAMDGPFLVYSAAREREASDVLRRSIALRLHISEQQFLLATVRATVPKAFVSYDPHPTPEALQHLQNMANTQFKSITYFYLNVPNTDAATLEMLGVPTVESVECASGGDVVDAAMMNGVAPGHMSSSNDYDWRRYKRDLVEPMSQPSPSHGHESNSEDSSLSDGDRTLVETDNMAHRGGGDSQVSSTSHSPQLSSPEDEAASHDAMMRVHAYCNGNGSYAAADVVDPLLLPTSTNHFFYATKVECVDVVGTGSSSGHQSDEEAQLRKPTRAYKLLVGTHMRMGAFKKHIEQLIQVPAAHFKLQRKHDNNLSNNQNNSLVHLIEGETLTVELGKTLEPDEFKAKIHFLRLADIDNETSKLPCVCEWVYNANTTAEQAKKELVAKLHRIDAKYATLSVQNCRIWLKGGRIPIKILSDDETLYCDMRSSIAAEFIVQECEEEVDPQPKDDSLTLFVRRWCPAKLEFGKFQEITLDQDSEIRLSLSQISDIPIDKLSYMKLNSNFPCTSISALSVNESSSWYSVPTTLDKYPLNSTQTGNIYLYKDRTVPARELTLEERRLMNAREKARLDRVGCVSTTRYAQRRERALKIYLDSPEKSSNVTASAPMDVHVNN
Enzyme Length 1556
Uniprot Accession Number Q24574
Absorption
Active Site ACT_SITE 405; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000305|PubMed:10949024, ECO:0000305|PubMed:26169834"; ACT_SITE 720; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:10949024, ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834};
DNA Binding
EC Number 3.4.19.12
Enzyme Function FUNCTION: Ubiquitin-specific protease that deubiquitinates target proteins to regulate different cellular and developmental pathways (PubMed:10949024, PubMed:18160715, PubMed:26169834, PubMed:27552662). Functions downstream of Dsor1/MEK to positively regulate the Ras/MAPK signaling pathway (PubMed:27552662). Likely to modulate the pathway during various cellular and developmental processes including rl/MAPK activation by the receptors InR, Egfr and sevenless/sev (PubMed:27552662). Functions in the post-translational stabilization of rl/MAPK levels in a mechanism that is independent of rl activity and opposes the activity of the E2 enzyme Unc6 and the putative E3 ligases poe, Ufd4 and Kcmf1, which mediate the ubiquitination and proteasomal degradation of rl (PubMed:27552662). During eye development it may also act downstream of rl/MAPK to negatively regulate the Ras/MAPK signaling pathway by stabilizing the transcriptional repressor ttk and consequently inhibiting photoreceptor cell development (PubMed:18160715). This suggests that at least during eye development, it may act in both the positive and negative regulation of the Ras/MAPK signaling pathway to mediate the development of different cell types (PubMed:18160715, PubMed:27552662). Positively regulates border follicle cell migration during oogenesis by mediating the deubiquitination and stabilization of slbo (PubMed:10949024). In the wing disks it positively regulates wg signaling by stabilizing arm (PubMed:26169834). Has an effect on position-effect variegation (PubMed:8816485). {ECO:0000269|PubMed:10949024, ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834, ECO:0000269|PubMed:27552662, ECO:0000269|PubMed:8816485}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Chain (1); Compositional bias (6); Domain (1); Erroneous initiation (2); Frameshift (1); Modified residue (10); Mutagenesis (2); Region (3); Sequence conflict (7)
Keywords Alternative splicing;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
Modified Residue MOD_RES 172; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 173; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 238; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 1131; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 1132; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 1140; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 1141; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 1199; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 1201; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897; MOD_RES 1205; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 173,794
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda