FBSP1_MOUSE
ID FBSP1_MOUSE Reviewed; 286 AA.
AC Q8K3B1; Q5M7B1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=F-box/SPRY domain-containing protein 1;
DE AltName: Full=F-box only protein 45;
DE Short=mFbxo45;
GN Name=Fbxo45 {ECO:0000312|EMBL:AAH26799.1, ECO:0000312|MGI:MGI:2447775};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAH26799.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH98203.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH26799.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH98203.1},
RC Mammary gland {ECO:0000312|EMBL:AAH26799.1}, and
RC Olfactory epithelium {ECO:0000312|EMBL:AAH88738.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, INTERACTION WITH MYCBP2 AND SKP1, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ARG-42.
RX PubMed=19398581; DOI=10.1128/mcb.00364-09;
RA Saiga T., Fukuda T., Matsumoto M., Tada H., Okano H.J., Okano H.,
RA Nakayama K.I.;
RT "Fbxo45 forms a novel ubiquitin ligase complex and is required for neuronal
RT development.";
RL Mol. Cell. Biol. 29:3529-3543(2009).
RN [3]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH UNC13A AND
RP SKP1.
RX PubMed=19996097; DOI=10.1074/jbc.m109.046284;
RA Tada H., Okano H.J., Takagi H., Shibata S., Yao I., Matsumoto M., Saiga T.,
RA Nakayama K.I., Kashima H., Takahashi T., Setou M., Okano H.;
RT "Fbxo45, a novel ubiquitin ligase, regulates synaptic activity.";
RL J. Biol. Chem. 285:3840-3849(2010).
CC -!- FUNCTION: Component of E3 ubiquitin ligase complexes. Required for
CC normal neuromuscular synaptogenesis, axon pathfinding and neuronal
CC migration. Plays a role in the regulation of neurotransmission at
CC mature neurons (By similarity). May control synaptic activity by
CC controlling UNC13A via ubiquitin dependent pathway. Specifically
CC recognizes TP73, promoting its ubiquitination and degradation (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:19398581}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms a complex with MYCBP2 and SKP1 but does not appear to
CC form an authentic SCF (SKP1-CUL1-F-box protein) complex. Interacts (via
CC B30.2/SPRY domain) with TP73 (via SAM domain); leading to its
CC ubiquitination and degradation (By similarity). Interacts (via SRY
CC domain) with UNC13A; leading to its degradation by the proteasome.
CC {ECO:0000250, ECO:0000269|PubMed:19398581,
CC ECO:0000269|PubMed:19996097}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}.
CC Presynaptic cell membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed speciffically in the central nervous
CC system, including cerebellum, medulla oblongata, olfactory bulb,
CC hippocampus, cortex and brain stem. {ECO:0000269|PubMed:19398581,
CC ECO:0000269|PubMed:19996097}.
CC -!- DISRUPTION PHENOTYPE: Homozygous animals die soon after birth due to
CC respiratory distress. Embryos show abnormal innervation of the
CC diaphragm, impaired synapse formation at neuromuscular junctions, and
CC aberrant development of axon fiber tracts in the brain.
CC {ECO:0000269|PubMed:19398581}.
CC -!- SIMILARITY: Belongs to the FBXO45/Fsn family. {ECO:0000305}.
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DR EMBL; BC026799; AAH26799.1; -; mRNA.
DR EMBL; BC088738; AAH88738.1; -; mRNA.
DR EMBL; BC098203; AAH98203.1; -; mRNA.
DR CCDS; CCDS28117.1; -.
DR RefSeq; NP_775615.2; NM_173439.2.
DR AlphaFoldDB; Q8K3B1; -.
DR SMR; Q8K3B1; -.
DR BioGRID; 234572; 5.
DR IntAct; Q8K3B1; 2.
DR STRING; 10090.ENSMUSP00000040168; -.
DR PhosphoSitePlus; Q8K3B1; -.
DR EPD; Q8K3B1; -.
DR MaxQB; Q8K3B1; -.
DR PaxDb; Q8K3B1; -.
DR PeptideAtlas; Q8K3B1; -.
DR PRIDE; Q8K3B1; -.
DR ProteomicsDB; 267716; -.
DR Antibodypedia; 51201; 67 antibodies from 16 providers.
DR DNASU; 268882; -.
DR Ensembl; ENSMUST00000042732; ENSMUSP00000040168; ENSMUSG00000035764.
DR GeneID; 268882; -.
DR KEGG; mmu:268882; -.
DR UCSC; uc007yyl.1; mouse.
DR CTD; 200933; -.
DR MGI; MGI:2447775; Fbxo45.
DR VEuPathDB; HostDB:ENSMUSG00000035764; -.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_046756_1_0_1; -.
DR InParanoid; Q8K3B1; -.
DR OMA; YHAWNPN; -.
DR OrthoDB; 1027590at2759; -.
DR PhylomeDB; Q8K3B1; -.
DR TreeFam; TF312822; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 268882; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fbxo45; mouse.
DR PRO; PR:Q8K3B1; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8K3B1; protein.
DR Bgee; ENSMUSG00000035764; Expressed in metanephric ureteric bud and 263 other tissues.
DR Genevisible; Q8K3B1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0021960; P:anterior commissure morphogenesis; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
DR GO; GO:0021800; P:cerebral cortex tangential migration; IMP:MGI.
DR GO; GO:0021957; P:corticospinal tract morphogenesis; IMP:MGI.
DR GO; GO:0060384; P:innervation; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0060386; P:synapse assembly involved in innervation; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
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; 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 Acetylation; Cell membrane; Cell projection; Developmental protein;
KW Membrane; Neurogenesis; Postsynaptic cell membrane; Reference proteome;
KW Synapse; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0C2W1"
FT CHAIN 2..286
FT /note="F-box/SPRY domain-containing protein 1"
FT /id="PRO_0000119947"
FT DOMAIN 33..82
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 92..284
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P0C2W1"
FT MUTAGEN 42
FT /note="R->E: Allows binding to CUL1 and RBX1 and formation
FT of an authentic SCF (SKP1-CUL1-F-box protein) complex."
FT /evidence="ECO:0000269|PubMed:19398581"
FT CONFLICT 27
FT /note="S -> C (in Ref. 1; AAH26799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 30605 MW; 78589911B5DA31B7 CRC64;
MAAPGPGAGA ASGGASGGGA GAGGGASAGS GSSGVGGRLP SRVLELVFSY LELSELRSCA
LVCKHWYRCL HGDENSEVWR SLCARSLAEE ALRTDILCNL PSYKAKVRAF QHAFSTNDCS
RNVYIKKNGF TLHRNPIAQS TDGARTKIGF SEGRHAWEVW WEGPLGTVAV IGIATKRAPM
QCQGYVALLG SDDQSWGWNL VDNNLLHNGE VNGSFPQCNN APKYQIGERI RVILDMEDKT
LAFERGYEFL GVAFRGLPKA CLYPAVSAVY GNTEVTLVYL GKPLDG
