FBSP1_CAEEL
ID FBSP1_CAEEL Reviewed; 332 AA.
AC Q18223;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=F-box/SPRY domain-containing protein 1;
DE AltName: Full=F-box synaptic protein 1;
GN Name=fsn-1; ORFNames=C26E6.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP PROTEIN SEQUENCE OF 25-35; 89-100; 131-150; 181-191; 270-275 AND 292-307,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (SEP-2005) to UniProtKB.
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CUL-1; RPM-1 AND SKR-1, INTERACTION WITH SCD-2,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15208641; DOI=10.1038/nature02647;
RA Liao E.H., Hung W., Abrams B., Zhen M.;
RT "An SCF-like ubiquitin ligase complex that controls presynaptic
RT differentiation.";
RL Nature 430:345-350(2004).
RN [4]
RP FUNCTION.
RX PubMed=21968191; DOI=10.1534/genetics.111.134791;
RA Tulgren E.D., Baker S.T., Rapp L., Gurney A.M., Grill B.;
RT "PPM-1, a PP2Calpha/beta phosphatase, regulates axon termination and
RT synapse formation in Caenorhabditis elegans.";
RL Genetics 189:1297-1307(2011).
RN [5]
RP FUNCTION, INTERACTION WITH EGL-3, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-191.
RX PubMed=23665919; DOI=10.1038/emboj.2013.91;
RA Hung W.L., Hwang C., Gao S., Liao E.H., Chitturi J., Wang Y., Li H.,
RA Stigloher C., Bessereau J.L., Zhen M.;
RT "Attenuation of insulin signalling contributes to FSN-1-mediated regulation
RT of synapse development.";
RL EMBO J. 32:1745-1760(2013).
CC -!- FUNCTION: Component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex which is required for the restriction and/or maturation
CC of synapses in GABAergic neuromuscular junction (NMJ) presynaptic
CC neurons (PubMed:15208641, PubMed:23665919). Promotes NRJ synapse
CC development and synaptic transmission by negatively regulating the daf-
CC 2/InsR pathway in muscles (PubMed:23665919). By targeting convertase
CC egl-3 for degradation, negatively modulates insulin-like protein ins-4
CC and ins-6 processing (PubMed:23665919). May stabilize synapse formation
CC by promoting the down-regulation of scd-2 (PubMed:15208641). Regulates
CC axon termination in PLM and ALM neurons (PubMed:21968191).
CC {ECO:0000269|PubMed:15208641, ECO:0000269|PubMed:21968191,
CC ECO:0000269|PubMed:23665919}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex composed of cul-1, fsn-1, rpm-1 and skr-1
CC (PubMed:15208641). Interacts (via SPRY domain) with scd-2 (via
CC cytoplasmic domain) (PubMed:15208641). Interacts (via SPRY domain) with
CC convertase egl-3 (via C-terminus) (PubMed:23665919).
CC {ECO:0000269|PubMed:15208641, ECO:0000269|PubMed:23665919}.
CC -!- INTERACTION:
CC Q18223; G5ECU1: skr-1; NbExp=4; IntAct=EBI-2003744, EBI-323117;
CC -!- SUBCELLULAR LOCATION: Synapse.
CC -!- TISSUE SPECIFICITY: Expressed in GABAergic neuromuscular junctions
CC (NMJs). {ECO:0000269|PubMed:15208641}.
CC -!- DISRUPTION PHENOTYPE: Synaptic defects that include both
CC overdevelopment and underdevelopment of presynaptic and postsynaptic
CC termini (PubMed:15208641). Abnormal morphology of cholinergic and
CC GABAergic neuromuscular junctions (NMJs) characterized by uneven
CC distribution of presynaptic markers snb-1 and unc-17 and post-synaptic
CC markers GABA receptor unc-49 and AChR unc-38. Also, formation of
CC abnormally large and small synapses (PubMed:23665919). Frequency of
CC spontaneous miniature synaptic release (mPSC) from cholinergic and
CC GABAergic NMJs is reduced (PubMed:23665919). In a daf-2 e1370 mutant
CC background, but not in a daf-2 e1370 and daf-16 mu86 mutant background,
CC the morphology of NMJs is normal and normal synaptic transmission is
CC partially restored (PubMed:23665919). Nuclear translocation of daf-16
CC (isoform a) is impaired in muscles but not in the intestine
CC (PubMed:23665919). {ECO:0000269|PubMed:15208641,
CC ECO:0000269|PubMed:23665919}.
CC -!- SIMILARITY: Belongs to the FBXO45/Fsn family. {ECO:0000305}.
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DR EMBL; FO080680; CCD65729.1; -; Genomic_DNA.
DR PIR; D88445; D88445.
DR RefSeq; NP_498046.1; NM_065645.5.
DR AlphaFoldDB; Q18223; -.
DR SMR; Q18223; -.
DR BioGRID; 40900; 6.
DR ComplexPortal; CPX-958; SCF-rpm-1 ubiquitin ligase complex.
DR IntAct; Q18223; 4.
DR STRING; 6239.C26E6.5; -.
DR EPD; Q18223; -.
DR PaxDb; Q18223; -.
DR PeptideAtlas; Q18223; -.
DR PRIDE; Q18223; -.
DR EnsemblMetazoa; C26E6.5.1; C26E6.5.1; WBGene00001499.
DR GeneID; 175667; -.
DR KEGG; cel:CELE_C26E6.5; -.
DR UCSC; C26E6.5; c. elegans.
DR CTD; 175667; -.
DR WormBase; C26E6.5; CE01163; WBGene00001499; fsn-1.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_046756_1_0_1; -.
DR InParanoid; Q18223; -.
DR OMA; DNVLMHN; -.
DR OrthoDB; 938259at2759; -.
DR PhylomeDB; Q18223; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q18223; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001499; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IGI:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; IGI:WormBase.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:WormBase.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:WormBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:UniProtKB.
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:1900073; P:regulation of neuromuscular synaptic transmission; IGI:UniProtKB.
DR GO; GO:0090128; P:regulation of synapse maturation; IC:ComplexPortal.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IGI:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR GO; GO:0060386; P:synapse assembly involved in innervation; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
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; PF00646; F-box; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Synapse;
KW Ubl conjugation pathway.
FT CHAIN 1..332
FT /note="F-box/SPRY domain-containing protein 1"
FT /id="PRO_0000119948"
FT DOMAIN 79..127
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 138..330
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 191
FT /note="R->C: In hp2; abnormal morphology of GABAergic
FT neuromuscular junctions and reduced synaptic transmission.
FT Severe impaired interaction with egl-3 and loss of egl-3
FT ubiquitination."
FT /evidence="ECO:0000269|PubMed:23665919"
SQ SEQUENCE 332 AA; 36825 MW; F0789FF53E9FB952 CRC64;
MAENDGETIV PDEQCNLTAS TPMKSSGLEQ VESPKERKTS MVECDDEGNP SSGTPDESPK
QLTPHSIPPR RRRSPRRPEV SASRLPLKVL NQIFQYLPLK DLRSAMLTCH SWNNALSMED
SDIWQYLLGK KLPEAAVSDP FLLAELGSAK KKLRAWYFAW NTSDISRNNY IRTNGFTVHR
QPVAQSTDGV RGKRGISKGV HAFDITWDGP LGTVAVVGIA TKHAALHCVG YVALLGSDDQ
SWGWNLVDNV LMHNGAQLGV YPKMNNPPKY EVGDKIRLII DCDTHVAYFE RNSEFLGIAF
NHIPPLRLYP AVCAVYGNTE VTMVYVGSPQ MG
