FBXW7_DROME
ID FBXW7_DROME Reviewed; 1326 AA.
AC Q9VZF4; A4V1G6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=F-box/WD repeat-containing protein 7;
DE AltName: Full=F-box and WD-40 domain-containing protein 7;
DE AltName: Full=Protein archipelago;
GN Name=ago {ECO:0000312|EMBL:AAL28848.1}; ORFNames=CG15010;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF47869.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF47869.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAL28848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CYCE, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ALA-1117 AND GLY-1131.
RX PubMed=11565033; DOI=10.1038/35095068;
RA Moberg K.H., Bell D.W., Wahrer D.C.R., Haber D.A., Hariharan I.K.;
RT "Archipelago regulates cyclin E levels in Drosophila and is mutated in
RT human cancer cell lines.";
RL Nature 413:311-316(2001).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MYC, AND TISSUE SPECIFICITY.
RX PubMed=15182669; DOI=10.1016/j.cub.2004.04.040;
RA Moberg K.H., Mukherjee A., Veraksa A., Artavanis-Tsakonas S.,
RA Hariharan I.K.;
RT "The Drosophila F box protein archipelago regulates dMyc protein levels in
RT vivo.";
RL Curr. Biol. 14:965-974(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15175253; DOI=10.1242/dev.01172;
RA Shcherbata H.R., Althauser C., Findley S.D., Ruohola-Baker H.;
RT "The mitotic-to-endocycle switch in Drosophila follicle cells is executed
RT by Notch-dependent regulation of G1/S, G2/M and M/G1 cell-cycle
RT transitions.";
RL Development 131:3169-3181(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-813 AND SER-825, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP INTERACTION WITH MYC AND PUF, AND DISRUPTION PHENOTYPE.
RX PubMed=24173801; DOI=10.1242/dev.096941;
RA Li L., Anderson S., Secombe J., Eisenman R.N.;
RT "The Drosophila ubiquitin-specific protease Puffyeye regulates dMyc-
RT mediated growth.";
RL Development 140:4776-4787(2013).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). Probably recognizes and binds to
CC phosphorylated target proteins (By similarity). In the wing and eye,
CC negatively regulates cell growth and proliferation by mediating the
CC degradation of Myc and cyclin E, respectively (PubMed:11565033,
CC PubMed:15182669). Required for endocycles, but not mitosis in follicle
CC cell epithelium (PubMed:15175253). {ECO:0000250,
CC ECO:0000269|PubMed:11565033, ECO:0000269|PubMed:15175253,
CC ECO:0000269|PubMed:15182669, ECO:0000269|PubMed:24173801}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF E3 ubiquitin-protein ligase complex. Interacts
CC with Myc and puf (PubMed:15182669, PubMed:24173801). Interacts with
CC CycE (PubMed:11565033). {ECO:0000269|PubMed:11565033,
CC ECO:0000269|PubMed:15182669, ECO:0000269|PubMed:24173801}.
CC -!- INTERACTION:
CC Q9VZF4; Q9W4S7: Myc; NbExp=2; IntAct=EBI-138334, EBI-120162;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in follicle cell epithelium and imaginal
CC disks, particularly in the morphogenetic furrow.
CC {ECO:0000269|PubMed:11565033, ECO:0000269|PubMed:15175253,
CC ECO:0000269|PubMed:15182669}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the posterior
CC compartment of the larval wing disk increases cell size in the
CC posterior compartment of the adult wing, resulting in an increase in
CC the size of the posterior compartment as well as an increase in the
CC ratio between the posterior and anterior areas.
CC {ECO:0000269|PubMed:24173801}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAF47869.1; -; Genomic_DNA.
DR EMBL; AE014296; AAG22246.1; -; Genomic_DNA.
DR EMBL; AE014296; AAG22247.1; -; Genomic_DNA.
DR EMBL; AY061300; AAL28848.1; -; mRNA.
DR EMBL; AY075401; AAL68231.1; -; mRNA.
DR RefSeq; NP_523922.1; NM_079198.3.
DR RefSeq; NP_728964.1; NM_168072.2.
DR RefSeq; NP_728965.1; NM_168073.2.
DR AlphaFoldDB; Q9VZF4; -.
DR SMR; Q9VZF4; -.
DR BioGRID; 63994; 60.
DR DIP; DIP-32477N; -.
DR IntAct; Q9VZF4; 12.
DR STRING; 7227.FBpp0073101; -.
DR iPTMnet; Q9VZF4; -.
DR PaxDb; Q9VZF4; -.
DR EnsemblMetazoa; FBtr0073245; FBpp0073101; FBgn0041171.
DR EnsemblMetazoa; FBtr0073246; FBpp0073102; FBgn0041171.
DR EnsemblMetazoa; FBtr0073247; FBpp0073103; FBgn0041171.
DR GeneID; 38516; -.
DR KEGG; dme:Dmel_CG15010; -.
DR UCSC; CG15010-RA; d. melanogaster.
DR CTD; 38516; -.
DR FlyBase; FBgn0041171; ago.
DR VEuPathDB; VectorBase:FBgn0041171; -.
DR eggNOG; KOG0274; Eukaryota.
DR GeneTree; ENSGT00940000154986; -.
DR HOGENOM; CLU_005079_1_0_1; -.
DR InParanoid; Q9VZF4; -.
DR OMA; QGFFNED; -.
DR OrthoDB; 666965at2759; -.
DR PhylomeDB; Q9VZF4; -.
DR SignaLink; Q9VZF4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 38516; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38516; -.
DR PRO; PR:Q9VZF4; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0041171; Expressed in eye disc (Drosophila) and 23 other tissues.
DR Genevisible; Q9VZF4; DM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:FlyBase.
DR GO; GO:0030332; F:cyclin binding; TAS:FlyBase.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:FlyBase.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IMP:FlyBase.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IGI:FlyBase.
DR GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
DR GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:FlyBase.
DR GO; GO:0007096; P:regulation of exit from mitosis; TAS:FlyBase.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR GO; GO:0030162; P:regulation of proteolysis; TAS:FlyBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:FlyBase.
DR GO; GO:0060438; P:trachea development; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..1326
FT /note="F-box/WD repeat-containing protein 7"
FT /id="PRO_0000050996"
FT DOMAIN 889..935
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 992..1030
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1033..1070
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1073..1110
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1113..1150
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 1153..1190
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 1193..1232
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 1236..1273
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 813
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 1117
FT /note="A->V: In ago-4; increased cell proliferation."
FT /evidence="ECO:0000269|PubMed:11565033"
FT MUTAGEN 1131
FT /note="G->E: In ago-3; increased cell proliferation and
FT decrease in ability to bind CycE."
FT /evidence="ECO:0000269|PubMed:11565033"
SQ SEQUENCE 1326 AA; 141361 MW; 3F42C873CFA3027F CRC64;
MERGCPAASS ESVTSAGERT QSAVTSSTST WVKSQASTSR KTEASEESGL GAVDAEVGAG
REAFVSMSTL REDVEDVCVS SNSQHGFAVV LDDESSTFEI SSSNSLPTSA GAASTVGVVA
VDDSSSTDTL NGGHPDLGHP ASSEHSRQGF FNEDNEDPPV VCLINDDDDD EEPEPEEDDE
EELIEDEDED AVDIVTGAIS CPNTSQLALA DGTIMAADGS KIFLETPVVE EAQPHPGQVV
TTGSQSELTG KPKRLSDEFL LGEEDQAENL ALGRCIKSEP VNPVDDNPSE GDDGATCFSL
HDRLMSVRLK QMSLTANTVS NPSPAASANA AAPEEASTSN SSSTSSSALS RADIESMDLI
ERRDFETEQR LTGGIILRTS SMVSQNKLNL SLIKSMAGGS KAANGSGTAN SDDWPSSSNG
RTVSSDSKYT YKDLSTTPTS SRKYTNSRLS KSTAKLNLGS SLGASSCSQH RSGSSSTSKS
MESSTSCTGA ARTDVYTNTN SNDYPSLAPT TSGSSTSGGS CQQDQEENVS ASVSYSSVGS
QTSQESGCSR TTAINPTAAC STGSACLGDS QASTSASTSS GAGASNRCQY ATTSTTKAAR
QVNASAQTQE RFLTRSNPPA ASGAGSVGAN PTASVRQRRN GSSDVVHLEV VVEEGAGGGD
GGVVEPGDFS AEEPWANCDE ENNCSDLEEI CTCQNGNGSS YGGSNASLSE TFDMDAMDPD
EPISLSLSSA SAGFTEYSLT NPSSLMSHQR KRKFNEGRLL DGGDYSVTIS SSGEVGGPGS
GVSDNCRKRI AYDFASTPRS SQHLGPTAVL SVTPSSHLTS STPGSALGRR TPRSVPSRDN
PPPELQHWLA QFQRWSHVER LLALDRLIDH CDPSQVRHMM KVIEPQFQRD FISLLPRELA
LFVLSYLEPK DLLRAAQTCR SWRFLCDDNL LWKEKCRKAQ ILAEPRSDRP KRGRDGNMPP
IASPWKAAYM RQHIIEMNWR SRPVRKPKVL KGHDDHVITC LQFSGNRIVS GSDDNTLKVW
SAVNGKCLRT LVGHTGGVWS SQMSGNIIIS GSTDRTLKVW DMDSGACVHT LQGHTSTVRC
MHLHGSKVVS GSRDATLRVW DIEQGSCLHV LVGHLAAVRC VQYDGKLIVS GAYDYMVKIW
HPERQECLHT LQGHTNRVYS LQFDGLHVVS GSLDTSIRVW DVETGNCKHT LMGHQSLTSG
MELRQNILVS GNADSTVKVW DITTGQCLQT LSGPNKHHSA VTCLQFNSRF VVTSSDDGTV
KLWDVKTGDF IRNLVALDSG GSGGVVWRIR ANDTKLICAV GSRNGTEETK LMVLDFDVEG
ACVKCS
