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F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7) (Protein archipelago)

 FBXW7_DROME             Reviewed;        1326 AA.
Q9VZF4; A4V1G6;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 150.
RecName: Full=F-box/WD repeat-containing protein 7;
AltName: Full=F-box and WD-40 domain-containing protein 7;
AltName: Full=Protein archipelago;
Name=ago {ECO:0000312|EMBL:AAL28848.1}; ORFNames=CG15010;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF47869.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF47869.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000305, ECO:0000312|EMBL:AAL28848.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4] {ECO:0000305}
FUNCTION, INTERACTION WITH CYCE, TISSUE SPECIFICITY, AND MUTAGENESIS
OF ALA-1117 AND GLY-1131.
PubMed=11565033; DOI=10.1038/35095068;
Moberg K.H., Bell D.W., Wahrer D.C.R., Haber D.A., Hariharan I.K.;
"Archipelago regulates cyclin E levels in Drosophila and is mutated in
human cancer cell lines.";
Nature 413:311-316(2001).
[5] {ECO:0000305}
FUNCTION, INTERACTION WITH MYC, AND TISSUE SPECIFICITY.
PubMed=15182669; DOI=10.1016/j.cub.2004.04.040;
Moberg K.H., Mukherjee A., Veraksa A., Artavanis-Tsakonas S.,
Hariharan I.K.;
"The Drosophila F box protein archipelago regulates dMyc protein
levels in vivo.";
Curr. Biol. 14:965-974(2004).
[6] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15175253; DOI=10.1242/dev.01172;
Shcherbata H.R., Althauser C., Findley S.D., Ruohola-Baker H.;
"The mitotic-to-endocycle switch in Drosophila follicle cells is
executed by Notch-dependent regulation of G1/S, G2/M and M/G1 cell-
cycle transitions.";
Development 131:3169-3181(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-813 AND SER-825, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[8]
INTERACTION WITH MYC AND PUF, AND DISRUPTION PHENOTYPE.
PubMed=24173801; DOI=10.1242/dev.096941;
Li L., Anderson S., Secombe J., Eisenman R.N.;
"The Drosophila ubiquitin-specific protease Puffyeye regulates dMyc-
mediated growth.";
Development 140:4776-4787(2013).
-!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-
box protein) E3 ubiquitin-protein ligase complex which mediates
the ubiquitination and subsequent proteasomal degradation of
target proteins (By similarity). Probably recognizes and binds to
phosphorylated target proteins (By similarity). In the wing and
eye, negatively regulates cell growth and proliferation by
mediating the degradation of Myc and cyclin E, respectively
(PubMed:11565033, PubMed:15182669). Required for endocycles, but
not mitosis in follicle cell epithelium (PubMed:15175253).
{ECO:0000250, ECO:0000269|PubMed:11565033,
ECO:0000269|PubMed:15175253, ECO:0000269|PubMed:15182669,
ECO:0000269|PubMed:24173801}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of a SCF E3 ubiquitin-protein ligase complex.
Interacts with Myc and puf (PubMed:15182669, PubMed:24173801).
Interacts with CycE (PubMed:11565033).
{ECO:0000269|PubMed:11565033, ECO:0000269|PubMed:15182669,
ECO:0000269|PubMed:24173801}.
-!- INTERACTION:
Q9W4S7:Myc; NbExp=2; IntAct=EBI-138334, EBI-120162;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in follicle cell epithelium and
imaginal disks, particularly in the morphogenetic furrow.
{ECO:0000269|PubMed:11565033, ECO:0000269|PubMed:15175253,
ECO:0000269|PubMed:15182669}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the posterior
compartment of the larval wing disk increases cell size in the
posterior compartment of the adult wing, resulting in an increase
in the size of the posterior compartment as well as an increase in
the ratio between the posterior and anterior areas.
{ECO:0000269|PubMed:24173801}.
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EMBL; AE014296; AAF47869.1; -; Genomic_DNA.
EMBL; AE014296; AAG22246.1; -; Genomic_DNA.
EMBL; AE014296; AAG22247.1; -; Genomic_DNA.
EMBL; AY061300; AAL28848.1; -; mRNA.
EMBL; AY075401; AAL68231.1; -; mRNA.
RefSeq; NP_523922.1; NM_079198.3.
RefSeq; NP_728964.1; NM_168072.2.
RefSeq; NP_728965.1; NM_168073.2.
UniGene; Dm.2559; -.
ProteinModelPortal; Q9VZF4; -.
SMR; Q9VZF4; -.
BioGrid; 63994; 58.
DIP; DIP-32477N; -.
IntAct; Q9VZF4; 12.
STRING; 7227.FBpp0073101; -.
iPTMnet; Q9VZF4; -.
PaxDb; Q9VZF4; -.
PRIDE; Q9VZF4; -.
EnsemblMetazoa; FBtr0073245; FBpp0073101; FBgn0041171.
EnsemblMetazoa; FBtr0073246; FBpp0073102; FBgn0041171.
EnsemblMetazoa; FBtr0073247; FBpp0073103; FBgn0041171.
GeneID; 38516; -.
KEGG; dme:Dmel_CG15010; -.
UCSC; CG15010-RA; d. melanogaster.
CTD; 38516; -.
FlyBase; FBgn0041171; ago.
eggNOG; KOG0274; Eukaryota.
eggNOG; ENOG410XRWX; LUCA.
GeneTree; ENSGT00940000154986; -.
InParanoid; Q9VZF4; -.
KO; K10260; -.
OMA; EEICTCQ; -.
OrthoDB; EOG091G04EW; -.
Reactome; R-DME-8951664; Neddylation.
Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q9VZF4; -.
UniPathway; UPA00143; -.
GenomeRNAi; 38516; -.
PRO; PR:Q9VZF4; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0041171; Expressed in 27 organ(s), highest expression level in embryo.
Genevisible; Q9VZF4; DM.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:FlyBase.
GO; GO:0030332; F:cyclin binding; TAS:FlyBase.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
GO; GO:0071456; P:cellular response to hypoxia; IMP:FlyBase.
GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IMP:FlyBase.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IGI:FlyBase.
GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:FlyBase.
GO; GO:0007096; P:regulation of exit from mitosis; TAS:FlyBase.
GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
GO; GO:0030162; P:regulation of proteolysis; TAS:FlyBase.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:FlyBase.
GO; GO:0060438; P:trachea development; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 5.
PROSITE; PS50082; WD_REPEATS_2; 7.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Cell cycle; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
CHAIN 1 1326 F-box/WD repeat-containing protein 7.
/FTId=PRO_0000050996.
DOMAIN 889 935 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 992 1030 WD 1. {ECO:0000255}.
REPEAT 1033 1070 WD 2. {ECO:0000255}.
REPEAT 1073 1110 WD 3. {ECO:0000255}.
REPEAT 1113 1150 WD 4. {ECO:0000255}.
REPEAT 1153 1190 WD 5. {ECO:0000255}.
REPEAT 1193 1232 WD 6. {ECO:0000255}.
REPEAT 1236 1273 WD 7. {ECO:0000255}.
COMPBIAS 337 580 Ser-rich.
MOD_RES 813 813 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 1117 1117 A->V: In ago-4; increased cell
proliferation.
{ECO:0000269|PubMed:11565033}.
MUTAGEN 1131 1131 G->E: In ago-3; increased cell
proliferation and decrease in ability to
bind CycE. {ECO:0000269|PubMed:11565033}.
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


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