FBSP1_CAEBR
ID FBSP1_CAEBR Reviewed; 332 AA.
AC A8XT88;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=F-box/SPRY domain-containing protein 1;
DE AltName: Full=F-box synaptic protein 1;
GN Name=fsn-1; ORFNames=CBG18196;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Promotes NRJ synapse development and synaptic transmission by
CC negatively regulating the daf-2/InsR pathway in muscles. By targeting
CC convertase egl-3 for degradation, negatively modulates insulin-like
CC protein ins-4 and ins-6 processing. May stabilize synapse formation by
CC promoting the down-regulation of scd-2. Regulates axon termination in
CC PLM and ALM neurons. {ECO:0000250|UniProtKB:Q18223}.
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. Interacts
CC (via SPRY domain) with scd-2 (via cytoplasmic domain). Interacts (via
CC SPRY domain) with convertase egl-3 (via C-terminus).
CC {ECO:0000250|UniProtKB:Q18223}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FBXO45/Fsn family. {ECO:0000305}.
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DR EMBL; HE600936; CAP35691.1; -; Genomic_DNA.
DR RefSeq; XP_002642222.1; XM_002642176.1.
DR AlphaFoldDB; A8XT88; -.
DR SMR; A8XT88; -.
DR STRING; 6238.CBG18196; -.
DR EnsemblMetazoa; CBG18196.1; CBG18196.1; WBGene00037661.
DR EnsemblMetazoa; CBG18196.2; CBG18196.2; WBGene00037661.
DR GeneID; 8584218; -.
DR KEGG; cbr:CBG_18196; -.
DR CTD; 8584218; -.
DR WormBase; CBG18196; CBP04261; WBGene00037661; Cbr-fsn-1.
DR eggNOG; KOG3953; Eukaryota.
DR HOGENOM; CLU_046756_1_0_1; -.
DR InParanoid; A8XT88; -.
DR OMA; DNVLMHN; -.
DR OrthoDB; 938259at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; IEA:EnsemblMetazoa.
DR GO; GO:0043005; C:neuron projection; IEA:EnsemblMetazoa.
DR GO; GO:0098793; C:presynapse; IEA:EnsemblMetazoa.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IEA:EnsemblMetazoa.
DR GO; GO:0040024; P:dauer larval development; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:0030517; P:negative regulation of axon extension; IEA:EnsemblMetazoa.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IEA:EnsemblMetazoa.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:EnsemblMetazoa.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:EnsemblMetazoa.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
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:0010212; P:response to ionizing radiation; IEA:EnsemblMetazoa.
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; 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 3: Inferred from homology;
KW Reference proteome; Synapse; Ubl conjugation pathway.
FT CHAIN 1..332
FT /note="F-box/SPRY domain-containing protein 1"
FT /id="PRO_0000383748"
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..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 37225 MW; 11E67CA7CA71259F CRC64;
MTENNEETIV PDEQCNLTSS TPMKSSDLEN VESPIERKIS IVECDGEGNP PIESSEETPP
DLTSHSVAPR RRRSPRRPEV SASRLPLKVL NQIFQYLSLK DLRSAMLTCH SWNNALSMED
SDIWQQLLVQ KLPEAAHSDP FLFVELRSAR KKLRAWYFAW NTNDISRNNY IRTNGFTVHR
QPVAQSTDGV RGKRGVSQGV HAFDITWDGP LGTVAVVGFA TKHAALHCVG YIALLGSDDQ
SWGWNLVDNV LMHNGVQLGV YPKMNNPPKY EVGEKIRLVI DCDMHVAYFE RNSEFLGIAF
SHIPPLRLFP AVCAVYGNTE VTMVYVGSPQ MG
