FBXL7_MOUSE
ID FBXL7_MOUSE Reviewed; 491 AA.
AC Q5BJ29; Q6ZQ36;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=F-box/LRR-repeat protein 7;
DE AltName: Full=F-box and leucine-rich repeat protein 7;
GN Name=Fbxl7; Synonyms=Kiaa0840;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A SCF PROTEIN LIGASE
RP COMPLEX, AND INTERACTION WITH AURKA.
RX PubMed=22306998; DOI=10.4161/cc.11.4.19171;
RA Coon T.A., Glasser J.R., Mallampalli R.K., Chen B.B.;
RT "Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A,
RT causing mitotic arrest.";
RL Cell Cycle 11:721-729(2012).
RN [4]
RP FUNCTION, AND INTERACTION WITH BIRC5.
RX PubMed=25778398; DOI=10.1074/jbc.m114.629931;
RA Liu Y., Lear T., Iannone O., Shiva S., Corey C., Rajbhandari S., Jerome J.,
RA Chen B.B., Mallampalli R.K.;
RT "The Proapoptotic F-box Protein Fbxl7 Regulates Mitochondrial Function by
RT Mediating the Ubiquitylation and Proteasomal Degradation of Survivin.";
RL J. Biol. Chem. 290:11843-11852(2015).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex (PubMed:22306998,
CC PubMed:25778398). During mitosis, it mediates the ubiquitination and
CC subsequent proteasomal degradation of AURKA, causing mitotic arrest
CC (PubMed:22306998). It also regulates mitochondrial function by
CC mediating the ubiquitination and proteasomal degradation of the
CC apoptosis inhibitor BIRC5 (PubMed:25778398).
CC {ECO:0000269|PubMed:22306998, ECO:0000269|PubMed:25778398}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:22306998, ECO:0000269|PubMed:25778398}.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXL7) composed of CUL1, SKP1, RBX1 and FBXL7
CC (PubMed:22306998). Interacts with AURKA; interaction takes place during
CC mitosis but not in interphase (PubMed:22306998). Interacts with BIRC5;
CC this interaction allows BIRC5 to be polyubiquitinated by the SCF(FBXL7)
CC E3 ubiquitin-protein ligase complex (PubMed:25778398).
CC {ECO:0000269|PubMed:22306998, ECO:0000269|PubMed:25778398}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:22306998}. Note=Localizes to the
CC centrosome during spindle formation. {ECO:0000269|PubMed:22306998}.
CC -!- SIMILARITY: Belongs to the FBXL7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98037.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129227; BAC98037.1; ALT_INIT; mRNA.
DR EMBL; BC091646; AAH91646.1; -; mRNA.
DR CCDS; CCDS37052.1; -.
DR RefSeq; NP_795933.2; NM_176959.3.
DR AlphaFoldDB; Q5BJ29; -.
DR SMR; Q5BJ29; -.
DR BioGRID; 243078; 2.
DR IntAct; Q5BJ29; 1.
DR STRING; 10090.ENSMUSP00000061305; -.
DR iPTMnet; Q5BJ29; -.
DR PhosphoSitePlus; Q5BJ29; -.
DR MaxQB; Q5BJ29; -.
DR PaxDb; Q5BJ29; -.
DR PeptideAtlas; Q5BJ29; -.
DR PRIDE; Q5BJ29; -.
DR ProteomicsDB; 271557; -.
DR Antibodypedia; 5190; 67 antibodies from 19 providers.
DR DNASU; 448987; -.
DR Ensembl; ENSMUST00000059204; ENSMUSP00000061305; ENSMUSG00000043556.
DR GeneID; 448987; -.
DR KEGG; mmu:448987; -.
DR UCSC; uc007vjn.1; mouse.
DR CTD; 23194; -.
DR MGI; MGI:3052506; Fbxl7.
DR VEuPathDB; HostDB:ENSMUSG00000043556; -.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000158009; -.
DR HOGENOM; CLU_016072_5_0_1; -.
DR InParanoid; Q5BJ29; -.
DR OMA; MIYCASI; -.
DR OrthoDB; 1027299at2759; -.
DR PhylomeDB; Q5BJ29; -.
DR TreeFam; TF313434; -.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 448987; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fbxl7; mouse.
DR PRO; PR:Q5BJ29; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q5BJ29; protein.
DR Bgee; ENSMUSG00000043556; Expressed in manus and 168 other tissues.
DR Genevisible; Q5BJ29; MM.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13516; LRR_6; 5.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 10.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW Mitosis; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..491
FT /note="F-box/LRR-repeat protein 7"
FT /id="PRO_0000307720"
FT DOMAIN 111..157
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 185..210
FT /note="LRR 1"
FT REPEAT 211..236
FT /note="LRR 2"
FT REPEAT 237..262
FT /note="LRR 3"
FT REPEAT 271..296
FT /note="LRR 4"
FT REPEAT 297..322
FT /note="LRR 5"
FT REPEAT 323..348
FT /note="LRR 6"
FT REPEAT 349..374
FT /note="LRR 7"
FT REPEAT 375..400
FT /note="LRR 8"
FT REPEAT 401..426
FT /note="LRR 9"
FT REPEAT 427..452
FT /note="LRR 10"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 54646 MW; 52EC5B2A00EDC1E6 CRC64;
MGANNGKQYG SEGKGSSSVS SDVSSSTDHT PTKAQRNVAT SEDSDLSMRT LSTPSPALIC
PPTLPGFQNG RGSSTSSSSI TGETVAMVHS PPPTRLTHPL IRLASRPQKE QASIDRLPDH
SMVQIFSFLP TNQLCRCARV CRRWYNLAWD PRLWRTIRLT GETINVDRAL KVLTRRLCQD
TPNVCLMLET VIVSGCRRLT DRGLYTIAQC CPELRRLEVS GCYNISNEAV FDVVSLCPNL
EHLDVSGCSK VTCISLTREA SIKLSPLHGK QISIRYLDMT DCFVLEDEGL HTIAAHCTQL
THLYLRRCVR LTDEGLRYLV IYCTSIKELS VSDCRFVSDF GLREIAKLES RLRYLSIAHC
GRITDVGIRY VAKYCSKLRY LNARGCEGIT DHGVEYLAKN CTKLKSLDIG KCPLVSDTGL
ESLALNCFNL KRLSLKSCES ITGQGLQIVA ANCFDLQMLN VQDCEVSVEA LRFVKRHCKR
CVIEHTNPAF F
