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P55824

- FAF_DROME

UniProt

P55824 - FAF_DROME

Protein

Probable ubiquitin carboxyl-terminal hydrolase FAF

Gene

faf

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (28 Nov 2002)
      Previous versions | rss
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    Functioni

    Required for eye and embryo development, and plays a role in compound eye assembly and oogenesis respectively. 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. It is also required for nuclear migration and cellularization in early embryogenesis and could play a role in pole cell determination, development or function.

    Catalytic activityi

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1677 – 16771NucleophilePROSITE-ProRule annotation
    Active sitei1986 – 19861Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. ubiquitin-specific protease activity Source: FlyBase

    GO - Biological processi

    1. cellularization Source: FlyBase
    2. compound eye development Source: FlyBase
    3. defense response to Gram-negative bacterium Source: FlyBase
    4. dorsal/ventral axis specification Source: FlyBase
    5. endocytosis Source: FlyBase
    6. germ cell migration Source: FlyBase
    7. mystery cell differentiation Source: FlyBase
    8. negative regulation of innate immune response Source: FlyBase
    9. negative regulation of proteolysis Source: FlyBase
    10. nuclear migration Source: FlyBase
    11. oogenesis Source: UniProtKB-KW
    12. protein deubiquitination Source: FlyBase
    13. ubiquitin-dependent protein catabolic process Source: FlyBase
    14. visual perception Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Differentiation, Oogenesis, Sensory transduction, Ubl conjugation pathway, Vision

    Enzyme and pathway databases

    ReactomeiREACT_181669. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

    Protein family/group databases

    MEROPSiC19.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ubiquitin carboxyl-terminal hydrolase FAF (EC:3.4.19.12)
    Alternative name(s):
    Protein fat facets
    Ubiquitin thioesterase FAF
    Ubiquitin-specific-processing protease FAF
    Short name:
    Deubiquitinating enzyme FAF
    Gene namesi
    Name:faf
    ORF Names:CG1945
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0005632. faf.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27782778Probable ubiquitin carboxyl-terminal hydrolase FAFPRO_0000080688Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei924 – 9241Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP55824.
    PRIDEiP55824.

    Expressioni

    Tissue specificityi

    Eye disks and ovaries.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically.

    Gene expression databases

    BgeeiP55824.

    Interactioni

    Protein-protein interaction databases

    BioGridi68590. 15 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP55824.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1668 – 2062395USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5077.
    GeneTreeiENSGT00740000115055.
    InParanoidiP55824.
    KOiK11840.
    OMAiMAQEQFF.
    OrthoDBiEOG722J7K.
    PhylomeDBiP55824.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 6 hits.
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: P55824-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTFDTRRHTT GQPGSTAPSS SSSTTSTTTT TTSPAQSAGS GSGIGTGTGT     50
    VANSSLPGGG SGSLDGNQDQ QPATDSQSSD DVAASLSANS VDSTITIVPP 100
    EKLISSFPTT KLRSLTQKIS NPRWVVPVLP EQELEVLLNA AIELTQAGVD 150
    HDCEPCVEFY RNGLSTSFAK ILTDEAVNSW KNNIHHCILV SCGKLLHLIA 200
    IHMQRDNPYL LDLLAIVFDP ENKFNTFNAG RQPECFAAPD YIWGQLDSNK 250
    MYARPPPEPK NARGWLVDLI NRFGQLGGFD NLLERFNIGL ELLKRNQNKC 300
    TGKNISVEGR VENGAQDNRL TLALIHSLLR PFGQCYELLM PATIAKYFMP 350
    TWNVVLDLLD SFTDEELKRE VKPEGRNDYI NGIVKSARLL ASRLTGQEEL 400
    IRDLEMFRLK MILRLLQVSS FNGKMNALNE INKVLSSVAY FSHRSQPLPH 450
    CMPEDEMDWL TADRMAQWIK SSDVLGVVLK DSLHQPQYVE KLEKIIRFLI 500
    KEQALTLDDL DAVWRAQAGK HEAIVKNVHD LLAKLAWDFT PEQLDHLFEA 550
    FQASMTTANK RQRERLLELI RRLAEDDKNG VMAQKVLKLF WTLAHSQEVP 600
    PEVLDQALGA HVKILDYSCS QERDAQKTIW LDKCVDELKS GDGWVLPALR 650
    LIRDICCLYD TTTNHAQRTQ TSTNRQQVIE RLQNDYSLVI LVTNSLTAYM 700
    EKVRQMVTDS PGLDATRILI DGRFPHHVQI AERLEFLKFL LKDGQLWLCA 750
    DQAKQIWHCL AVNAVFPADR EECFRWFGKL MGEEPDLDPG INKDFFENNI 800
    LQLDPHLLTE SGIKCFERFF KAVNSKEDKL KAIHRGYMLD NEDLIGKDYL 850
    WRVITTGGEE IASKAIDLLK EVSTALGPRL QENIAEFHEM FIGECCSRLR 900
    THYGNIVILG KTQLQEELDA PDQSDNTNDE SKDSKMRFIE AEKMCRILKV 950
    LQEYVKECDR SFSGDRVHLP LSRVTRGKNT ILYIRFQNPG RSIDDMEIVT 1000
    HSNETMAAFK RNLLKRIKGT STANIKVDLF YANDEMIGVS DEINPLYQYT 1050
    IRDKMNLTAK LTPVGTGLAS SPDSSSDSST GSPPRPCPDM QRVESESTLP 1100
    GVIISQNYQY TEFFLKLYQL GSDLEHGRLR DSAKVLLHLL PCDRQTIRQL 1150
    KIMCKVPKAA VTVAVTGDKI AKDEEEKLYP TEQAGIEDEE EHCTPEQMFL 1200
    HPTPAQVLYN LSVLHGLLIP ALDPLGESAL LVQSAWMHSG CAHFVLELLT 1250
    KNNFLPSADM HTKRASFQCV LRLAKLFLYI VGSVLSRVGD EPMICDLDNG 1300
    SRSQVDILKQ NFSTMPSSSQ GTLRAISAKL AVILAREMLS ASPEGDRCRT 1350
    LFSSTLQWSC PDISTIKAVV QLAWASSCGN LQALGNSSGD FEDEVIVPDG 1400
    QDFSMCKEAL EVLTISFILN PSANEALTSD PNWPKFITSI VLKNPLRHVR 1450
    QVASEQLFLA STYCAGDRRP FVYMVNLLVG ALKTLVPQYE STCAEFFSVL 1500
    CRTLSYGCIY NWPLQISEGL LGDEIKWLQR IRENVHATGD TQVHEELLEG 1550
    HLCLAKELMF FLGADSKAQL NELIHELIDD FLFTASREFL HLRRHGSLRQ 1600
    DTVPPPVCRS PHTIAAACDL LIALCQLCVP NMKLLTNTLI DFVCTDTDPL 1650
    REWDYLPPVG ARPTKGFCGL KNAGATCYMN SVLQQLYMVP AVRVGILRAH 1700
    GAATTDGEDF SGDSDLTGGG LGSALFSGPA SALVSLPSSS STIEDGLHDV 1750
    RKNYHVVILK HVQAIFAHLG HSALQYYVPR GLWTHFKLLG EPVNLREQQD 1800
    AVEFFMSLLE SLDEGLKALG QPQLMNATLG GSFSDQKICQ ECPHRYSKEE 1850
    PFSVFSVDIR NHSSLTESLE QYVKGELLEG ADAYHCDKCD KKVVTVKRVC 1900
    VKKLPPVLAI QLKRFEYDYE RVCAIKFNDY FEFPRILDME PYTVSGLAKL 1950
    EGEVVEVGDN CQTNVETTKY ELTGIVVHSG QASGGHYFSY ILSKNPANGK 2000
    CQWYKFDDGE VTECKMHEDE EMKAECFGGE YMGETYDNNL KRMQYRRQKR 2050
    WWNAYMLFYT RCDQTPVQYE PSVEQLSLAE SRNMVLPLPK PIERSVRHQN 2100
    IRFLHSRSIF SVEFFNFIKK LVSCNLLSAR SNKITPAAEE LSLLGVQLAS 2150
    QFLFHTGFRT KKSLRGPVME WYDALSHHIR SSALVRKWFA NHALLSPPSR 2200
    LGEYILMAPS PDVRTVFVKL VVFFCHFAIN DEPLTGYDGA NLCEQVLISV 2250
    LRLLKSEAAD YGKHLPHYFS LFSMYVGLGT REKQQLLRLN VPLQFIQVAL 2300
    DDGPGPAIKY QYPEFSKLHQ VVSHLIRCSD VSEKCQSSNQ NARPLSNPFK 2350
    DPNVAHEELT PLSTECMDLL FNRTGYIKKV IEDTNVGDEG LKLLQYCSWE 2400
    NPHFSRAVLT ELLWQCGFAY CHDMRHHTDL LLNILLIDDS WQHHRIHNAL 2450
    NGVAEEREGL LETIQRAKTH YQKRAYQIIK CLTQLFHKSP IALQMLHTNS 2500
    NITRHWSIAV EWLQGELDRQ RGIGCQYNSY SWSPPAQSND NTNGYMLERS 2550
    QSAKNTWSMA FELCPDEVSE KTDENNEPNL ETNMDENKSE PVAQPGGVLE 2600
    GSTGGTEQLP ENKTPTTSSP STAAWPARGD SNAIPRLSRQ LFGAYTSTGS 2650
    GSTSGGSAPT SALTTTAGSG ANSETESSAQ ETTGETTING LTNSLDQMEI 2700
    TAKKKCRRVI IKKLVESKDE EDATTATTAA TTEVTTSPAT AIATAATLEP 2750
    AGMSELTTMV EKNLIISQEN PQAKSSLQ 2778
    Length:2,778
    Mass (Da):311,143
    Last modified:November 28, 2002 - v2
    Checksum:iFFB90438BA53A02B
    GO
    Isoform 3 (identifier: P55824-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2705-2778: KCRRVIIKKL...ENPQAKSSLQ → VTRANNV

    Show »
    Length:2,711
    Mass (Da):304,080
    Checksum:i0D6319FFCC88EA5C
    GO

    Sequence cautioni

    Isoform 1 : The sequence AAF01345.1 differs from that shown. Reason: Frameshift at positions 2742 and 2750.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2341E → D in AAF01345. (PubMed:1295747)Curated
    Sequence conflicti234 – 2341E → D in AAF01346. (PubMed:1295747)Curated
    Sequence conflicti2725 – 27251T → S in AAF01345. (PubMed:1295747)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2705 – 277874KCRRV…KSSLQ → VTRANNV in isoform 3. 1 PublicationVSP_005269Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04959 mRNA. Translation: AAF01345.1. Frameshift.
    L04958 mRNA. Translation: AAF01346.1.
    L04960 Genomic DNA. Translation: AAF01347.1.
    L04960 Genomic DNA. Translation: AAF01348.1.
    AE014297 Genomic DNA. Translation: AAF57198.1.
    AE014297 Genomic DNA. Translation: AAN14291.1.
    AF145677 mRNA. Translation: AAD38652.1.
    PIRiB49132.
    RefSeqiNP_524612.2. NM_079873.4. [P55824-1]
    NP_733455.1. NM_170576.2. [P55824-3]
    UniGeneiDm.3133.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085843; FBpp0085202; FBgn0005632. [P55824-1]
    GeneIDi43749.
    KEGGidme:Dmel_CG1945.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04959 mRNA. Translation: AAF01345.1 . Frameshift.
    L04958 mRNA. Translation: AAF01346.1 .
    L04960 Genomic DNA. Translation: AAF01347.1 .
    L04960 Genomic DNA. Translation: AAF01348.1 .
    AE014297 Genomic DNA. Translation: AAF57198.1 .
    AE014297 Genomic DNA. Translation: AAN14291.1 .
    AF145677 mRNA. Translation: AAD38652.1 .
    PIRi B49132.
    RefSeqi NP_524612.2. NM_079873.4. [P55824-1 ]
    NP_733455.1. NM_170576.2. [P55824-3 ]
    UniGenei Dm.3133.

    3D structure databases

    ProteinModelPortali P55824.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68590. 15 interactions.

    Protein family/group databases

    MEROPSi C19.007.

    Proteomic databases

    PaxDbi P55824.
    PRIDEi P55824.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085843 ; FBpp0085202 ; FBgn0005632 . [P55824-1 ]
    GeneIDi 43749.
    KEGGi dme:Dmel_CG1945.

    Organism-specific databases

    FlyBasei FBgn0005632. faf.

    Phylogenomic databases

    eggNOGi COG5077.
    GeneTreei ENSGT00740000115055.
    InParanoidi P55824.
    KOi K11840.
    OMAi MAQEQFF.
    OrthoDBi EOG722J7K.
    PhylomeDBi P55824.

    Enzyme and pathway databases

    Reactomei REACT_181669. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

    Miscellaneous databases

    ChiTaRSi faf. drosophila.
    GenomeRNAii 43749.
    NextBioi 835588.
    PROi P55824.

    Gene expression databases

    Bgeei P55824.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 6 hits.
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The fat facets gene is required for Drosophila eye and embryo development."
      Fischer-Vize J.A., Rubin G.M., Lehmann R.
      Development 116:985-1000(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY.
      Tissue: Eye imaginal disk.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1089-2778 (ISOFORM 1).
      Strain: Berkeley.
      Tissue: Embryo.
    5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiFAF_DROME
    AccessioniPrimary (citable) accession number: P55824
    Secondary accession number(s): Q9V9T6, Q9Y0Z7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 28, 2002
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3