| IED ID | IndEnz0002003192 |
| Enzyme Type ID | protease003192 |
| Protein Name |
Probable ubiquitin carboxyl-terminal hydrolase FAF EC 3.4.19.12 Protein fat facets Ubiquitin thioesterase FAF Ubiquitin-specific-processing protease FAF Deubiquitinating enzyme FAF |
| Gene Name | faf CG1945 |
| 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 | MTFDTRRHTTGQPGSTAPSSSSSTTSTTTTTTSPAQSAGSGSGIGTGTGTVANSSLPGGGSGSLDGNQDQQPATDSQSSDDVAASLSANSVDSTITIVPPEKLISSFPTTKLRSLTQKISNPRWVVPVLPEQELEVLLNAAIELTQAGVDHDCEPCVEFYRNGLSTSFAKILTDEAVNSWKNNIHHCILVSCGKLLHLIAIHMQRDNPYLLDLLAIVFDPENKFNTFNAGRQPECFAAPDYIWGQLDSNKMYARPPPEPKNARGWLVDLINRFGQLGGFDNLLERFNIGLELLKRNQNKCTGKNISVEGRVENGAQDNRLTLALIHSLLRPFGQCYELLMPATIAKYFMPTWNVVLDLLDSFTDEELKREVKPEGRNDYINGIVKSARLLASRLTGQEELIRDLEMFRLKMILRLLQVSSFNGKMNALNEINKVLSSVAYFSHRSQPLPHCMPEDEMDWLTADRMAQWIKSSDVLGVVLKDSLHQPQYVEKLEKIIRFLIKEQALTLDDLDAVWRAQAGKHEAIVKNVHDLLAKLAWDFTPEQLDHLFEAFQASMTTANKRQRERLLELIRRLAEDDKNGVMAQKVLKLFWTLAHSQEVPPEVLDQALGAHVKILDYSCSQERDAQKTIWLDKCVDELKSGDGWVLPALRLIRDICCLYDTTTNHAQRTQTSTNRQQVIERLQNDYSLVILVTNSLTAYMEKVRQMVTDSPGLDATRILIDGRFPHHVQIAERLEFLKFLLKDGQLWLCADQAKQIWHCLAVNAVFPADREECFRWFGKLMGEEPDLDPGINKDFFENNILQLDPHLLTESGIKCFERFFKAVNSKEDKLKAIHRGYMLDNEDLIGKDYLWRVITTGGEEIASKAIDLLKEVSTALGPRLQENIAEFHEMFIGECCSRLRTHYGNIVILGKTQLQEELDAPDQSDNTNDESKDSKMRFIEAEKMCRILKVLQEYVKECDRSFSGDRVHLPLSRVTRGKNTILYIRFQNPGRSIDDMEIVTHSNETMAAFKRNLLKRIKGTSTANIKVDLFYANDEMIGVSDEINPLYQYTIRDKMNLTAKLTPVGTGLASSPDSSSDSSTGSPPRPCPDMQRVESESTLPGVIISQNYQYTEFFLKLYQLGSDLEHGRLRDSAKVLLHLLPCDRQTIRQLKIMCKVPKAAVTVAVTGDKIAKDEEEKLYPTEQAGIEDEEEHCTPEQMFLHPTPAQVLYNLSVLHGLLIPALDPLGESALLVQSAWMHSGCAHFVLELLTKNNFLPSADMHTKRASFQCVLRLAKLFLYIVGSVLSRVGDEPMICDLDNGSRSQVDILKQNFSTMPSSSQGTLRAISAKLAVILAREMLSASPEGDRCRTLFSSTLQWSCPDISTIKAVVQLAWASSCGNLQALGNSSGDFEDEVIVPDGQDFSMCKEALEVLTISFILNPSANEALTSDPNWPKFITSIVLKNPLRHVRQVASEQLFLASTYCAGDRRPFVYMVNLLVGALKTLVPQYESTCAEFFSVLCRTLSYGCIYNWPLQISEGLLGDEIKWLQRIRENVHATGDTQVHEELLEGHLCLAKELMFFLGADSKAQLNELIHELIDDFLFTASREFLHLRRHGSLRQDTVPPPVCRSPHTIAAACDLLIALCQLCVPNMKLLTNTLIDFVCTDTDPLREWDYLPPVGARPTKGFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATTDGEDFSGDSDLTGGGLGSALFSGPASALVSLPSSSSTIEDGLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEVGDNCQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNPANGKCQWYKFDDGEVTECKMHEDEEMKAECFGGEYMGETYDNNLKRMQYRRQKRWWNAYMLFYTRCDQTPVQYEPSVEQLSLAESRNMVLPLPKPIERSVRHQNIRFLHSRSIFSVEFFNFIKKLVSCNLLSARSNKITPAAEELSLLGVQLASQFLFHTGFRTKKSLRGPVMEWYDALSHHIRSSALVRKWFANHALLSPPSRLGEYILMAPSPDVRTVFVKLVVFFCHFAINDEPLTGYDGANLCEQVLISVLRLLKSEAADYGKHLPHYFSLFSMYVGLGTREKQQLLRLNVPLQFIQVALDDGPGPAIKYQYPEFSKLHQVVSHLIRCSDVSEKCQSSNQNARPLSNPFKDPNVAHEELTPLSTECMDLLFNRTGYIKKVIEDTNVGDEGLKLLQYCSWENPHFSRAVLTELLWQCGFAYCHDMRHHTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTQLFHKSPIALQMLHTNSNITRHWSIAVEWLQGELDRQRGIGCQYNSYSWSPPAQSNDNTNGYMLERSQSAKNTWSMAFELCPDEVSEKTDENNEPNLETNMDENKSEPVAQPGGVLEGSTGGTEQLPENKTPTTSSPSTAAWPARGDSNAIPRLSRQLFGAYTSTGSGSTSGGSAPTSALTTTAGSGANSETESSAQETTGETTINGLTNSLDQMEITAKKKCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATAATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ |
| Enzyme Length | 2778 |
| Uniprot Accession Number | P55824 |
| Absorption | |
| Active Site | ACT_SITE 1677; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000305|PubMed:23919485"; ACT_SITE 1986; /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:23919485}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Ubiquitin C-terminal hydrolase involved in development and the imd/NF-kappa-B (IMD) signaling cascade (PubMed:23919485, PubMed:1295747). Required for eye and embryo development, and plays a role in compound eye assembly and oogenesis respectively (PubMed:1295747). In the larval eye disks, cells outside the assembling facets require this protein for short-range cell interactions that prevent the mystery cells from becoming photoreceptors (PubMed:1295747). Also required for nuclear migration and cellularization in early embryogenesis and could play a role in pole cell determination, development or function (PubMed:1295747). Regulates the IMD signaling cascade at later stages of infection (around 6 hours post-infection) by inhibiting the expression of the antimicrobial peptides Dpt and Dro (PubMed:23919485). Acts by modulating the state of imd polyubiquitination and/or stability; a function which appears to be independent of its enzymatic activity (PubMed:23919485). In turn, imd enhances the polyubiquitination and stability of faf suggesting that they may form a regulatory feedback mechanism within the Imd pathway (PubMed:23919485). {ECO:0000269|PubMed:1295747, ECO:0000269|PubMed:23919485}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Chain (1); Compositional bias (3); Domain (1); Frameshift (1); Modified residue (1); Mutagenesis (1); Region (4); Sequence conflict (3) |
| Keywords | Alternative splicing;Developmental protein;Differentiation;Hydrolase;Oogenesis;Phosphoprotein;Protease;Reference proteome;Sensory transduction;Thiol protease;Ubl conjugation;Ubl conjugation pathway;Vision |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 924; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897 |
| Post Translational Modification | PTM: Ubiquitinated. Ubiquitination is enhanced by the expression of imd. {ECO:0000269|PubMed:23919485}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10570463; 10603300; 10725248; 10766017; 10835395; 10898994; 10949024; 11102374; 11102377; 11151297; 11182084; 11222152; 11301252; 11406394; 11473321; 11697879; 11782945; 11825870; 11861167; 11901120; 11911874; 12021769; 12021772; 12242239; 12367500; 12367627; 12408836; 12461563; 12814944; 12818174; 12850443; 12900457; 14588248; 14691551; 14704174; 14760701; 15013811; 15046717; 15308208; 15331236; 15454263; 15469967; 15620635; 15790962; 15927177; 16243437; 16702236; 16815332; 16905559; 16957085; 16980395; 17409080; 17500595; 17603113; 17658258; 18245346; 18716220; 18959482; 19401399; 19520911; 20100334; 20146544; 20220848; 20371351; 21074052; 21350007; 22253573; 22745309; 22918439; 22937016; 22939627; 23071443; 23271647; 23275879; 23487316; 23899565; 24114784; 24881051; 24948796; 25027767; 25242144; 25294943; 25312911; 25540427; 25644700; 25672900; 25763846; 25776889; 25848931; 25882370; 26120032; 26801178; 26870755; 27346357; 27794539; 28036067; 28515050; 29050293; 29084807; 29109678; 29391183; 29472843; 30333215; 30635270; 31076285; 32169355; 32573431; 32820799; 32972998; 33211537; 33988679; 7833286; 7835340; 7867504; 7972125; 8173320; 8224855; 8331338; 8525378; 8640222; 8793288; 8816485; 8898233; 9053303; 9162472; 9310325; 9332974; 9356481; 9374412; 9431804; 9435287; 9502724; |
| Motif | |
| Gene Encoded By | |
| Mass | 311,143 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |