P55824 · FAF_DROME
- ProteinProbable ubiquitin carboxyl-terminal hydrolase FAF
- Genefaf
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2778 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ubiquitin C-terminal hydrolase involved in development and the imd/NF-kappa-B (IMD) signaling cascade (PubMed:1295747, PubMed:23919485).
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).
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).
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1677 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 1986 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | cysteine-type deubiquitinase activity | |
Biological Process | cell migration | |
Biological Process | cellularization | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | dorsal/ventral axis specification | |
Biological Process | germ cell migration | |
Biological Process | mystery cell differentiation | |
Biological Process | negative regulation of innate immune response | |
Biological Process | nuclear cortical migration | |
Biological Process | oogenesis | |
Biological Process | positive regulation of BMP signaling pathway | |
Biological Process | protein deubiquitination | |
Biological Process | proteolysis | |
Biological Process | visual perception |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProbable ubiquitin carboxyl-terminal hydrolase FAF
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP55824
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1677 | Loss of enzymatic activity. Increased susceptibility to infections by E.cloacae. No effect on binding and polyubiquitination of imd. | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080688 | 1-2778 | Probable ubiquitin carboxyl-terminal hydrolase FAF | |||
Sequence: MTFDTRRHTTGQPGSTAPSSSSSTTSTTTTTTSPAQSAGSGSGIGTGTGTVANSSLPGGGSGSLDGNQDQQPATDSQSSDDVAASLSANSVDSTITIVPPEKLISSFPTTKLRSLTQKISNPRWVVPVLPEQELEVLLNAAIELTQAGVDHDCEPCVEFYRNGLSTSFAKILTDEAVNSWKNNIHHCILVSCGKLLHLIAIHMQRDNPYLLDLLAIVFDPENKFNTFNAGRQPECFAAPDYIWGQLDSNKMYARPPPEPKNARGWLVDLINRFGQLGGFDNLLERFNIGLELLKRNQNKCTGKNISVEGRVENGAQDNRLTLALIHSLLRPFGQCYELLMPATIAKYFMPTWNVVLDLLDSFTDEELKREVKPEGRNDYINGIVKSARLLASRLTGQEELIRDLEMFRLKMILRLLQVSSFNGKMNALNEINKVLSSVAYFSHRSQPLPHCMPEDEMDWLTADRMAQWIKSSDVLGVVLKDSLHQPQYVEKLEKIIRFLIKEQALTLDDLDAVWRAQAGKHEAIVKNVHDLLAKLAWDFTPEQLDHLFEAFQASMTTANKRQRERLLELIRRLAEDDKNGVMAQKVLKLFWTLAHSQEVPPEVLDQALGAHVKILDYSCSQERDAQKTIWLDKCVDELKSGDGWVLPALRLIRDICCLYDTTTNHAQRTQTSTNRQQVIERLQNDYSLVILVTNSLTAYMEKVRQMVTDSPGLDATRILIDGRFPHHVQIAERLEFLKFLLKDGQLWLCADQAKQIWHCLAVNAVFPADREECFRWFGKLMGEEPDLDPGINKDFFENNILQLDPHLLTESGIKCFERFFKAVNSKEDKLKAIHRGYMLDNEDLIGKDYLWRVITTGGEEIASKAIDLLKEVSTALGPRLQENIAEFHEMFIGECCSRLRTHYGNIVILGKTQLQEELDAPDQSDNTNDESKDSKMRFIEAEKMCRILKVLQEYVKECDRSFSGDRVHLPLSRVTRGKNTILYIRFQNPGRSIDDMEIVTHSNETMAAFKRNLLKRIKGTSTANIKVDLFYANDEMIGVSDEINPLYQYTIRDKMNLTAKLTPVGTGLASSPDSSSDSSTGSPPRPCPDMQRVESESTLPGVIISQNYQYTEFFLKLYQLGSDLEHGRLRDSAKVLLHLLPCDRQTIRQLKIMCKVPKAAVTVAVTGDKIAKDEEEKLYPTEQAGIEDEEEHCTPEQMFLHPTPAQVLYNLSVLHGLLIPALDPLGESALLVQSAWMHSGCAHFVLELLTKNNFLPSADMHTKRASFQCVLRLAKLFLYIVGSVLSRVGDEPMICDLDNGSRSQVDILKQNFSTMPSSSQGTLRAISAKLAVILAREMLSASPEGDRCRTLFSSTLQWSCPDISTIKAVVQLAWASSCGNLQALGNSSGDFEDEVIVPDGQDFSMCKEALEVLTISFILNPSANEALTSDPNWPKFITSIVLKNPLRHVRQVASEQLFLASTYCAGDRRPFVYMVNLLVGALKTLVPQYESTCAEFFSVLCRTLSYGCIYNWPLQISEGLLGDEIKWLQRIRENVHATGDTQVHEELLEGHLCLAKELMFFLGADSKAQLNELIHELIDDFLFTASREFLHLRRHGSLRQDTVPPPVCRSPHTIAAACDLLIALCQLCVPNMKLLTNTLIDFVCTDTDPLREWDYLPPVGARPTKGFCGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATTDGEDFSGDSDLTGGGLGSALFSGPASALVSLPSSSSTIEDGLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEVGDNCQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNPANGKCQWYKFDDGEVTECKMHEDEEMKAECFGGEYMGETYDNNLKRMQYRRQKRWWNAYMLFYTRCDQTPVQYEPSVEQLSLAESRNMVLPLPKPIERSVRHQNIRFLHSRSIFSVEFFNFIKKLVSCNLLSARSNKITPAAEELSLLGVQLASQFLFHTGFRTKKSLRGPVMEWYDALSHHIRSSALVRKWFANHALLSPPSRLGEYILMAPSPDVRTVFVKLVVFFCHFAINDEPLTGYDGANLCEQVLISVLRLLKSEAADYGKHLPHYFSLFSMYVGLGTREKQQLLRLNVPLQFIQVALDDGPGPAIKYQYPEFSKLHQVVSHLIRCSDVSEKCQSSNQNARPLSNPFKDPNVAHEELTPLSTECMDLLFNRTGYIKKVIEDTNVGDEGLKLLQYCSWENPHFSRAVLTELLWQCGFAYCHDMRHHTDLLLNILLIDDSWQHHRIHNALNGVAEEREGLLETIQRAKTHYQKRAYQIIKCLTQLFHKSPIALQMLHTNSNITRHWSIAVEWLQGELDRQRGIGCQYNSYSWSPPAQSNDNTNGYMLERSQSAKNTWSMAFELCPDEVSEKTDENNEPNLETNMDENKSEPVAQPGGVLEGSTGGTEQLPENKTPTTSSPSTAAWPARGDSNAIPRLSRQLFGAYTSTGSGSTSGGSAPTSALTTTAGSGANSETESSAQETTGETTINGLTNSLDQMEITAKKKCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATAATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ | ||||||
Modified residue | 924 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated. Ubiquitination is enhanced by the expression of imd.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Developmental stage
Expressed both maternally and zygotically.
Gene expression databases
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-85 | Disordered | ||||
Sequence: MTFDTRRHTTGQPGSTAPSSSSSTTSTTTTTTSPAQSAGSGSGIGTGTGTVANSSLPGGGSGSLDGNQDQQPATDSQSSDDVAAS | ||||||
Compositional bias | 1065-1085 | Polar residues | ||||
Sequence: GTGLASSPDSSSDSSTGSPPR | ||||||
Region | 1065-1094 | Disordered | ||||
Sequence: GTGLASSPDSSSDSSTGSPPRPCPDMQRVE | ||||||
Domain | 1668-2062 | USP | ||||
Sequence: CGLKNAGATCYMNSVLQQLYMVPAVRVGILRAHGAATTDGEDFSGDSDLTGGGLGSALFSGPASALVSLPSSSSTIEDGLHDVRKNYHVVILKHVQAIFAHLGHSALQYYVPRGLWTHFKLLGEPVNLREQQDAVEFFMSLLESLDEGLKALGQPQLMNATLGGSFSDQKICQECPHRYSKEEPFSVFSVDIRNHSSLTESLEQYVKGELLEGADAYHCDKCDKKVVTVKRVCVKKLPPVLAIQLKRFEYDYERVCAIKFNDYFEFPRILDMEPYTVSGLAKLEGEVVEVGDNCQTNVETTKYELTGIVVHSGQASGGHYFSYILSKNPANGKCQWYKFDDGEVTECKMHEDEEMKAECFGGEYMGETYDNNLKRMQYRRQKRWWNAYMLFYTRC | ||||||
Compositional bias | 2568-2584 | Basic and acidic residues | ||||
Sequence: VSEKTDENNEPNLETNM | ||||||
Region | 2568-2632 | Disordered | ||||
Sequence: VSEKTDENNEPNLETNMDENKSEPVAQPGGVLEGSTGGTEQLPENKTPTTSSPSTAAWPARGDSN | ||||||
Compositional bias | 2605-2626 | Polar residues | ||||
Sequence: GTEQLPENKTPTTSSPSTAAWP | ||||||
Region | 2644-2691 | Disordered | ||||
Sequence: AYTSTGSGSTSGGSAPTSALTTTAGSGANSETESSAQETTGETTINGL |
Sequence similarities
Belongs to the peptidase C19 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing. Experimental confirmation may be lacking for some isoforms.
P55824-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length2,778
- Mass (Da)311,143
- Last updated2002-11-28 v2
- ChecksumFFB90438BA53A02B
P55824-3
- Name3
- Differences from canonical
- 2705-2778: KCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATAATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ → VTRANNV
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0B4K6W2 | A0A0B4K6W2_DROME | faf | 2761 | ||
A0A0B4K7S0 | A0A0B4K7S0_DROME | faf | 2773 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 234 | in Ref. 1; AAF01345/AAF01346 | ||||
Sequence: E → D | ||||||
Compositional bias | 1065-1085 | Polar residues | ||||
Sequence: GTGLASSPDSSSDSSTGSPPR | ||||||
Compositional bias | 2568-2584 | Basic and acidic residues | ||||
Sequence: VSEKTDENNEPNLETNM | ||||||
Compositional bias | 2605-2626 | Polar residues | ||||
Sequence: GTEQLPENKTPTTSSPSTAAWP | ||||||
Alternative sequence | VSP_005269 | 2705-2778 | in isoform 3 | |||
Sequence: KCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATAATLEPAGMSELTTMVEKNLIISQENPQAKSSLQ → VTRANNV | ||||||
Sequence conflict | 2725 | in Ref. 1; AAF01345 | ||||
Sequence: T → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L04959 EMBL· GenBank· DDBJ | AAF01345.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
L04958 EMBL· GenBank· DDBJ | AAF01346.1 EMBL· GenBank· DDBJ | mRNA | ||
L04960 EMBL· GenBank· DDBJ | AAF01347.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L04960 EMBL· GenBank· DDBJ | AAF01348.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF57198.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAN14291.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF145677 EMBL· GenBank· DDBJ | AAD38652.1 EMBL· GenBank· DDBJ | mRNA |