IED ID | IndEnz0002011718 |
Enzyme Type ID | protease011718 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase puf EC 3.4.19.12 Protein puffyeye |
Gene Name | puf Usp34 CG5794 |
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 | MCEVCADFQNLLELYEVRVASSDLKFQLLLKSEIETTFNYIQSWPQRQCMCLYRDTKNYDRFNLVVQSLICLTVQHLKHIDHLIDNYKRLTASAAQVVAQAQQQREQQRDEASAQAEAKESSAPAEEPKKEEPSGSAGEEAQGSGDGPAKKPPVGPCTPPPPQTANPQHKSHLQYTEEPWILPEVEKLLVLVSKVFLLNFPLYIAHKHGMHSRLDDLQAEEAHHLALICDLHDNDLPIYLLRNVSLFCNSGGFGAMSLCFEHPDLPVSTAHSMTAAVSNVKLWLNYHCNTQLFVPLRSRILQYMCKLSDQSLRSAATRAMADFVWSSMRDPLDVAVNFDTEGLALAFKYFTSTTLTMRLAGMAQINAHINLFNEICTTETVNEVELFGQRIANWLTENHIVQHLFGPNLHVEIVKQAHVLLNFLAVENQISEEDIKLIWQATQLKHCSKTIFDILPSLVKNLTPRPAMHLYSLLCRMDPKEHTEQSIYIASALTKQLWTRDTSRSQMNLMQDHLLGSNVTASSSDSGSIEGSNTEDDHVGADDSSIASGGGGGGVGNKSPIDGVTPCKQARHRRHICDPTTEKGKQISPEDMAKVDLVNKRIVNIIDNTSSEEELQSRAALELQLHRSRKKTSNKRRRQKTNKQIILPHELVEIWDGVEDVPSSDEADGEADGDGEGELLADSDECSDGATSQLVPDAVLKHLQGEGPFIRAIETNINELLSGAENDGSYSSPMSNKSEKNLADFDDEDVSPCEEELAQLVSSRANCSDVPPAFAAAAAAMMVAQSAMALQKSGESNVAAAAAAVAAAAAATGTAQQTLVAMNRQASVAAAAAVVAAAKAKSDSDVDLMDVVSGGKQHHSPKASQGSSTSGSTPVQPSFKLNDVCQPGNTLLWDLLQDDKIGQLGESLALEAEKALATLLCFSMDRQLRTKFIEGCLYNVANNRSVIVSLRLLPKLFASFQQFRPSDTHSMTMWAERNHRMMQCFFNNIRHYARRHAEVLITQNGEQQQQQLGGQLYSHKTQVSVRLQFLSSIFSTVGSPKSFRLTLEQLDALWEWLAHDPECADCYFSWLQAQAKGGDQHALGIEALQHLYLKKLPELRPEEFSMVALGLFQQLCSFARIAMAEYDNHSDQISASASAVGMYHLWKIALRAQSNDVSLAAIQYINMYYMGQQLRLEKEFVSQCMENLVQAATALESIDDENALMRVQRGLLLLNTHLDTFRRRYAFHLRRWAIEGKGIGSHSNLKNEGAGPPLRIVLQQAGLSEKSLLQMHACDLIADLKAEVSKWWESLQTGLAAPVLGLLLSDGPLRIITQGQELTSDYDERSLGDAGFKDNQIVYVSLGGRGARRKESNLEHPSMLPPPPKECLPTVLLLQPKYFEKLFCLMQTLGDMQPQASTVNPQHHTKAQLLSRRVWDILAMLPTNPHILDAFKSLVTDLSELEQLDAGGEEEQLATKRKQIKQKFRDLLDPNNLQKFMYSLHIVESLALTSSRRGESNGNVAMGNTPEQVRVKKSSMGRRRNSNEQPPPPPPEVKMSKEQLCELEAPLTPTPSTGLQDVETEASSSSGGDKENQPKQHSKRQKKGETFEQEKERPVGCSTPPSPTPPPPALSVVERGDNKWSEAFVKCGGLRHLYEIFSEGQLQQSAHPKELALNEWRHDCLASLLRILWLLGFEELQSADAHVLMSRPHPFMLQLMEVPQCLTRLSSILNDEVHQQHQASSANPLVFPYQFQHLRTGFWGRAQLIQFAMNILVSFVHASAEARRLLWAPTGTDHCRWLQKFILEDPEPAVRREICAGLYRICLGNAHSYRLLLAPLLHKLIALLPLAEQMSSGNQHTQFLLSEEGKDPYGPACRDYFWLLARLVDTLSPEMVAEEHIDIEMLCESISQSILTREYYELRHGYQDDGLVGLLNLMSNLIKYDTTFKYTPKALSFIEQLIGFLFDMPSPADRQKPKCKSASSRASAYDLLVELCRGCATNYAYLHGRLLAQHKSGPKQPYPWDYWPRDEGRAECGYVGLTNLGATCYMASCVQHLYMMPQARAAVLRVPPNAARKHGPTLLELQRMFAYLLESERKSYNPRSFCRVYQMDHQPLNTGEQKDMAEFFIDLVSKLEDMTPDLKHLVKRLFCGSLSNNVVSLDCGHVSRTAEDFYTVRCQVADMRNLQESLDEVTVKDTLEGDNMYTCSQCGKKVRAEKRACFKKLPQILCFNTMRYTFNMVTMLKEKVNTHFSFPLRLNMCHYVEKTLMPQQYKEERERRQKEKEGADGSGDGNDNEKAEATLDDDIEECYEYELVGVTVHTGTADGGHYYSFIKERTKTSYHTHERWFLFNDAEVKPFDPSQIAAECFGGEMTSKTYDSVTEKYLDFSFEKTNSAYMLFYERRLPEHLQRRHSELLVTPTPSPTVEEKSEAEEPTKMETSSSEIKADVDVEVEVEEKDKEKPAQTDTESKETPAKEEIADDKSKQDEPEEKKIEKQSREGEEKSETDEKPTEMTTVSTEEEKQPTANCDNHQQNNNSNSKASNDQQPSTSKAAQKLQLFRPLLNKELEDWIWQDNRQFLQDRNIFEHTYFNFMWQICGHIPQSLISETDVTCMAAKLSVSFFIETFIHAKEKPTMVPWVELLTKQFNASQEACEWFLSHMSQEPYWPVQVLIQCPNQMVRQMFQRLVIHVIQQLRASHAHLYLEVETDEDDKELIGQASCVTRFIGSLISLLEHGARANLRHLSEYFGLLCEFSRMGDEEAMYLLRIGVLKSLVDFYLGHKQTDSIDISSDNEDNSSEEALSVEKMRPASLDKMIALCASLVERSRGADFRLRLSPKDFSAIAGGKGFPFLYQQIKDGINPHQTKHLIHALCRWDERLATQIIGMLFASVTKHTELCAPFFKLLTLLTETQGGPVGLPCFTQLILPRMWDAAEYCPQSVLDWLSLQATKNKIAHAWILQSAEKWLEQFLLAHDNTRVRNAAAFLLVALVPSQPFRANFRAHSQHKLLALNPHSYRDINSDAQAVLHQVITLLLRLLRPARVYADIGAHGTTKLTAYFNLLSYCMVSKTEKLMASSYMRSLWELFHPRLSEPSVPAHHNKHALLTFWHHSLVDCPENAAQVANCPEITRNIAFNYILADHDDAEIVTYNRSMLPAYYGLLRLCCEQSRALTRQLSQHQNLQWAFKNITPHPTQYAAAVDELFKLMALFATRHPDASEQEKLDVTQFRRAVIVSYTSSLDARVSWSTLISALKILVDNEEDRTMVIFNGGIEMCFEALHTLHSMHHEATACHVAGDLFDLLGEMLLLLATLRTRTDSPAQKKQQQQQQQLEQQLQLQQQQMLQKQQQQSQSQTQTPQSPQQKEKQLQQQMQQHLQLQQLQQMQFQQQHFLRQQHQHSALAKALPDAVKRLATLLNTFNSPEISRMALEVLKELVRNPSLETISILAPILINCHLSVANAPNAIGPLGPYFPRRGAKHTPWPLGAKNSPRPPRPMVQMCIALAELTPRGLDADYDVQVESFYRPYHDFIDVMMRMCVNTGTLNDTLVKLQCLVAIESTPLHFTYFPKFWVGIHNNALTHKYVELLVKNQLLVEYLHNVLRDERSMLKDACVREFLELYYHKVAAQLPVARMIYTINYGMHSKDDIDELCGDLFAIRIIAQATGVPASVRKELRGSLRALQNKSERFRKESERDPFPNKKQKRDSQKIKEKEHPQPESEKETSTENDKPSDVSMESSGNAEQATDSTKPPTPAGSDDEQMDKTSVPSSDDETELEDELQPTPKRNKKASNKKTAQDRVNEEREKRLITLITMESYIQSIFAILKRDASVPSSGATKEPSEEPCGEASTSAAAAVKLSRPKGACTPPEPITDVNDTRCNIDTETEAEADEQSPKTSQTNGSQQNESPPAATSADTAPANPSPAPAAAVASTSQAASPTQI |
Enzyme Length | 3912 |
Uniprot Accession Number | Q9VC56 |
Absorption | |
Active Site | ACT_SITE 2024; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01035, ECO:0000305|PubMed:24173801"; ACT_SITE 2305; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01035, ECO:0000305|PubMed:24173801" |
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:0000250|UniProtKB:Q70CQ2}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Ubiquitin hydrolase that can remove conjugated ubiquitin from target proteins and polyubiquitin chains (PubMed:24173801). Essential for Myc-mediated cell growth and proliferation in developing eyes and wings (PubMed:24173801). In the wing and eye, the deubiquitinating activity acts as an antagonist to the SCF E3 ubiquitin-protein ligase member archipelago (ago) to regulate Myc and CycE stability and thus control cell growth and proliferation (PubMed:24173801). Also appears to regulate ago by modulating its induction by Myc (PubMed:24173801). May also promote cell apoptosis in the wing imaginal disk, acting in an apoptotic pathway that appears to be largely independent of Myc (PubMed:24173801). Required for preventing the activation of the immune deficiency (Imd) and Toll signaling cascades under unchallenged conditions (PubMed:25027767). Also appears to be involved in modulating the differential expression of certain antimicrobial peptides (AMP) in response to infection by either Gram-positive or Gram-negative bacteria (PubMed:25027767). {ECO:0000269|PubMed:24173801, ECO:0000269|PubMed:25027767}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (2); Chain (1); Compositional bias (15); Domain (1); Mutagenesis (3); Region (10) |
Keywords | Alternative splicing;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24173801}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 20220848; 20371351; 20838586; 22937016; 23071443; 23087838; 23275879; 23899565; 24952591; 25294943; 25644700; 25687947; 25848931; 26120032; 26173873; 26370122; 28084990; 28257468; 31625562; 33988679; |
Motif | |
Gene Encoded By | |
Mass | 440,375 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |