FBX7_MOUSE
ID FBX7_MOUSE Reviewed; 523 AA.
AC Q3U7U3; Q3UBC1; Q8K0A5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=F-box only protein 7;
GN Name=Fbxo7;
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 STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-432; ARG-452 AND ARG-519, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1
CC in the clearance of damaged mitochondria via selective autophagy
CC (mitophagy) by targeting PRKN to dysfunctional depolarized
CC mitochondria. Promotes MFN1 ubiquitination (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7. Interacts via
CC its C-terminal proline-rich region with DLGAP5. Interacts with BIRC2.
CC Interacts with CDK6 and promotes its interaction with D-type cyclin.
CC Interacts (via the N-terminal Ubl domain) with PRKN. Interacts (via N-
CC terminal region) with PINK1. Interacts with PSMF1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Mitochondrion {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC Note=Predominantly cytoplasmic. A minor proportion is detected in the
CC nucleus. Relocates from the cytosol to depolarized mitochondria (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The ubiquitin-like region mediates interaction with PRKN.
CC {ECO:0000250}.
CC -!- DOMAIN: The proline-rich region is important for protein-protein
CC interactions. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK147797; BAE28145.1; -; mRNA.
DR EMBL; AK151025; BAE30043.1; -; mRNA.
DR EMBL; AK150626; BAE29716.1; -; mRNA.
DR EMBL; AK152513; BAE31276.1; -; mRNA.
DR EMBL; CH466539; EDL21433.1; -; Genomic_DNA.
DR EMBL; BC032153; AAH32153.1; -; mRNA.
DR CCDS; CCDS24095.1; -.
DR RefSeq; NP_001334080.1; NM_001347151.1.
DR RefSeq; NP_694875.2; NM_153195.2.
DR AlphaFoldDB; Q3U7U3; -.
DR SMR; Q3U7U3; -.
DR BioGRID; 213659; 17.
DR STRING; 10090.ENSMUSP00000120840; -.
DR iPTMnet; Q3U7U3; -.
DR PhosphoSitePlus; Q3U7U3; -.
DR EPD; Q3U7U3; -.
DR MaxQB; Q3U7U3; -.
DR PaxDb; Q3U7U3; -.
DR PeptideAtlas; Q3U7U3; -.
DR PRIDE; Q3U7U3; -.
DR ProteomicsDB; 270968; -.
DR Antibodypedia; 25270; 179 antibodies from 32 providers.
DR DNASU; 69754; -.
DR Ensembl; ENSMUST00000130320; ENSMUSP00000120840; ENSMUSG00000001786.
DR GeneID; 69754; -.
DR KEGG; mmu:69754; -.
DR UCSC; uc007gnk.1; mouse.
DR CTD; 25793; -.
DR MGI; MGI:1917004; Fbxo7.
DR VEuPathDB; HostDB:ENSMUSG00000001786; -.
DR eggNOG; ENOG502QTNJ; Eukaryota.
DR GeneTree; ENSGT00390000006670; -.
DR HOGENOM; CLU_039588_0_0_1; -.
DR InParanoid; Q3U7U3; -.
DR OMA; ICLVLED; -.
DR OrthoDB; 999024at2759; -.
DR PhylomeDB; Q3U7U3; -.
DR TreeFam; TF329830; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 69754; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Fbxo7; mouse.
DR PRO; PR:Q3U7U3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3U7U3; protein.
DR Bgee; ENSMUSG00000001786; Expressed in right kidney and 233 other tissues.
DR ExpressionAtlas; Q3U7U3; baseline and differential.
DR Genevisible; Q3U7U3; MM.
DR GO; GO:0097414; C:classical Lewy body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097409; C:glial cytoplasmic inclusion; ISO:MGI.
DR GO; GO:1990037; C:Lewy body core; ISO:MGI.
DR GO; GO:1990038; C:Lewy body corona; ISO:MGI.
DR GO; GO:0097462; C:Lewy neurite; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:0030098; P:lymphocyte differentiation; IMP:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; ISO:MGI.
DR GO; GO:0045620; P:negative regulation of lymphocyte differentiation; IMP:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:MGI.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0040012; P:regulation of locomotion; ISO:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR021625; PI31_Prot_N.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF11566; PI31_Prot_N; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methylation; Mitochondrion; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..523
FT /note="F-box only protein 7"
FT /id="PRO_0000307722"
FT DOMAIN 330..376
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 1..88
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000250"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..129
FT /note="Important for interaction with PINK1"
FT /evidence="ECO:0000250"
FT REGION 129..169
FT /note="Important for interaction with CDK6"
FT /evidence="ECO:0000250"
FT REGION 180..325
FT /note="Important for dimerization and interaction with
FT PSMF1"
FT /evidence="ECO:0000250"
FT REGION 382..523
FT /note="Important for interaction with CDK6"
FT /evidence="ECO:0000250"
FT REGION 494..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 482..485
FT /note="RFDP motif"
FT COMPBIAS 86..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 432
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 452
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 519
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 204
FT /note="H -> R (in Ref. 1; BAE29716/BAE31276)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="K -> N (in Ref. 3; AAH32153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 57649 MW; 5FEC744477081929 CRC64;
MKLRVRLQKR TQPLEVPESE PTLGQLRAHL SQVLLPTLGF SSDTRFAITL NNKDALTGDE
ETLASYGIVS GDLICLVLED DMPAPNLPSS TDTEHSSLQD NDQPSLAATP SQTNIPDEQG
TDSSQGQATP FDAWTDDSME GPSQNVEAES IQDAMSMEEV SGFHPLEPML CNETEDGQVP
HSLETLYQSA GCSNISDALI VLVHLLMLES GYIPQGTETK AVTMPEKWKS SGVYKLQYTH
PLCEGGFAVL TCVPLGNLII INATIKVNGG IKNVKSVQLQ PGSYVAAGVE PGESAAKVYK
DLKKLSRLFK DQLVYPLLAF TRQVLNLPDV FGLVVLPLEL KLRIFRLLDV HSVLALSAVC
HDLLIASNDP LLWRCLYLRD FRDGTVRGPD TDWKELYRKK HIQRKEAQRM RHAMFLPSAH
PIPFCPIPVY PRAYLPTSLL PPGIIGGEYD ERPILPSVGD PVTSLIPRPG ELPGQFRPLR
PRFDPVDPLP GPHSLLPGRA IPNNRFPFRP GRGRSADSRL PFL
