FBSP1_DROME
ID FBSP1_DROME Reviewed; 255 AA.
AC Q9V6L9; B7YZR5; Q0E992;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=F-box/SPRY domain-containing protein 1;
DE Short=DFsn;
GN Name=Fsn; ORFNames=CG4643;
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:0000312|EMBL:AAM68601.1}
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:AAM68601.1}
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:0000312|EMBL:AAM49963.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM49963.1};
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]
RP PROTEIN SEQUENCE OF 63-73; 91-114 AND 193-224, FUNCTION, INTERACTION WITH
RP HIW, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17697379; DOI=10.1186/1749-8104-2-16;
RA Wu C., Daniels R.W., DiAntonio A.;
RT "DFsn collaborates with Highwire to down-regulate the Wallenda/DLK kinase
RT and restrain synaptic terminal growth.";
RL Neural Dev. 2:16-16(2007).
RN [5]
RP FUNCTION, INTERACTION WITH VAS AND CUL1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-239.
RX PubMed=20123973; DOI=10.1128/mcb.01100-09;
RA Kugler J.M., Woo J.S., Oh B.H., Lasko P.;
RT "Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3
RT ligase specificity receptors.";
RL Mol. Cell. Biol. 30:1769-1782(2010).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH HIW AND FSN, INTERACTION WITH RAE1, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21874015; DOI=10.1038/nn.2922;
RA Tian X., Li J., Valakh V., DiAntonio A., Wu C.;
RT "Drosophila Rae1 controls the abundance of the ubiquitin ligase Highwire in
RT post-mitotic neurons.";
RL Nat. Neurosci. 14:1267-1275(2011).
CC -!- FUNCTION: Required in the presynaptic motoneuron to down-regulate the
CC levels of wnd and restrain synaptic terminal growth at the
CC neuromuscular junction (NMJ). Negatively regulates the localization of
CC vas to the posterior pole of the oocyte. Involved in primordial germ
CC cell formation. {ECO:0000269|PubMed:17697379,
CC ECO:0000269|PubMed:20123973}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of an E3 ubiquitin ligase complex composed of hiw
CC and Fsn (PubMed:17697379, PubMed:21874015). Interacts with Rae1,
CC probably as part of the hiw-Fsn complex (PubMed:21874015). Interacts
CC (via B30.2/SPRY domain) with vas (PubMed:20123973). Interacts with Cul1
CC (PubMed:20123973). {ECO:0000269|PubMed:17697379,
CC ECO:0000269|PubMed:20123973, ECO:0000269|PubMed:21874015}.
CC -!- INTERACTION:
CC Q9V6L9; P09052: vas; NbExp=2; IntAct=EBI-126933, EBI-134067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20123973}. Nucleus
CC {ECO:0000269|PubMed:17697379}. Synapse {ECO:0000269|PubMed:17697379}.
CC Cell projection, axon {ECO:0000269|PubMed:17697379}. Perikaryon
CC {ECO:0000269|PubMed:17697379}. Note=In mid- to late-stage oocytes,
CC recruited to the pole plasm. This posterior distribution is not
CC maintained in later developmental stages. Some cortical accumulation is
CC observed at mid- to late-stage oocytes. In mature eggs, present at high
CC levels throughout the ooplasm. {ECO:0000269|PubMed:20123973}.
CC -!- TISSUE SPECIFICITY: Expressed in nurse cells and oocytes (at protein
CC level) (PubMed:20123973). Expressed in the brain (PubMed:21874015).
CC Expressed in the neuromuscular junction (NMJ) (PubMed:17697379).
CC {ECO:0000269|PubMed:17697379, ECO:0000269|PubMed:20123973,
CC ECO:0000269|PubMed:21874015}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:20123973}.
CC -!- DISRUPTION PHENOTYPE: Dramatic overgrowth of synaptic termini, with a
CC large increase in the number of synaptic boutons and branches. Also
CC impaired synaptic transmission. {ECO:0000269|PubMed:17697379}.
CC -!- SIMILARITY: Belongs to the FBXO45/Fsn family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58404.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68601.1; -; Genomic_DNA.
DR EMBL; AY118594; AAM49963.1; -; mRNA.
DR RefSeq; NP_610849.1; NM_137005.2.
DR RefSeq; NP_725266.1; NM_165973.2.
DR AlphaFoldDB; Q9V6L9; -.
DR SMR; Q9V6L9; -.
DR BioGRID; 62223; 7.
DR IntAct; Q9V6L9; 4.
DR STRING; 7227.FBpp0086875; -.
DR PaxDb; Q9V6L9; -.
DR EnsemblMetazoa; FBtr0087762; FBpp0086875; FBgn0043010.
DR EnsemblMetazoa; FBtr0087763; FBpp0086876; FBgn0043010.
DR GeneID; 36460; -.
DR KEGG; dme:Dmel_CG4643; -.
DR UCSC; CG4643-RA; d. melanogaster.
DR CTD; 36460; -.
DR FlyBase; FBgn0043010; Fsn.
DR VEuPathDB; VectorBase:FBgn0043010; -.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_046756_1_0_1; -.
DR InParanoid; Q9V6L9; -.
DR OMA; YHAWNPN; -.
DR OrthoDB; 1027590at2759; -.
DR PhylomeDB; Q9V6L9; -.
DR SignaLink; Q9V6L9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 36460; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36460; -.
DR PRO; PR:Q9V6L9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0043010; Expressed in cleaving embryo and 21 other tissues.
DR Genevisible; Q9V6L9; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045495; C:pole plasm; IDA:FlyBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISM:FlyBase.
DR GO; GO:0060386; P:synapse assembly involved in innervation; IBA:GO_Central.
DR CDD; cd12907; SPRY_Fbox; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035784; SPRY_FBXO45.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Developmental protein;
KW Direct protein sequencing; Neurogenesis; Nucleus; Reference proteome;
KW Synapse; Ubl conjugation pathway.
FT CHAIN 1..255
FT /note="F-box/SPRY domain-containing protein 1"
FT /id="PRO_0000119949"
FT DOMAIN 3..51
FT /note="F-box"
FT /evidence="ECO:0000255"
FT DOMAIN 61..253
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT MUTAGEN 239
FT /note="Y->A: Abolishes interaction with vas."
FT /evidence="ECO:0000269|PubMed:20123973"
SQ SEQUENCE 255 AA; 28832 MW; 6475FF8BE046A4B3 CRC64;
MVDPVAALCN YNVLEVIFSY LELDDLSHCS QVCKSWYHFL NDENSDVWRW HCLNKLPKES
LKSDLLASVS TYKTKLRAYF HAWSPNDCSR NVYIKPNGFT LHRNPVAQST DAARGKIGFR
HGRHTWEVIW EGPLGTVAVI GISTKEAALQ CHGYVALLGS DDQSWGWNLV ENHLLHNGDM
QGSYPLLNNA PKYQVGERIR VILDCEDNTL SFEKNYEFLG VAFRGLPDKK LYPTVSAVYG
NTEVSMVYLG TPLDG
