SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P55824

- FAF_DROME

UniProt

P55824 - FAF_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Probable ubiquitin carboxyl-terminal hydrolase FAF
Gene
faf, CG1945
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 16771Nucleophile By similarity
Active sitei1986 – 19861Proton acceptor By similarity

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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27782778Probable ubiquitin carboxyl-terminal hydrolase FAF
PRO_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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2705 – 277874KCRRV…KSSLQ → VTRANNV in isoform 3.
VSP_005269Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341E → D in AAF01345. 1 Publication
Sequence conflicti234 – 2341E → D in AAF01346. 1 Publication
Sequence conflicti2725 – 27251T → S in AAF01345. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 123 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

Similar proteinsi