FXL20_MOUSE
ID FXL20_MOUSE Reviewed; 436 AA.
AC Q9CZV8; A7YE80; Q3UMN2; Q571F7; Q8BZ95;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=F-box/LRR-repeat protein 20;
DE AltName: Full=F-box and leucine-rich repeat protein 20;
DE AltName: Full=F-box/LRR-repeat protein 2-like;
GN Name=Fbxl20; Synonyms=Fbl2;
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 [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH RIMS1; SKP1 AND CUL1, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=17803915; DOI=10.1016/j.cell.2007.06.052;
RA Yao I., Takagi H., Ageta H., Kahyo T., Sato S., Hatanaka K., Fukuda Y.,
RA Chiba T., Morone N., Yuasa S., Inokuchi K., Ohtsuka T., Macgregor G.R.,
RA Tanaka K., Setou M.;
RT "SCRAPPER-dependent ubiquitination of active zone protein RIM1 regulates
RT synaptic vesicle release.";
RL Cell 130:943-957(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Natural killer cell;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
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).
CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex. Isoform 3 regulates neural
CC transmission by binding and ubiquitinating RIMS1, a modulator of
CC presynaptic plasticity. {ECO:0000269|PubMed:17803915}.
CC -!- SUBUNIT: Interacts with SKP1 and CUL1. {ECO:0000269|PubMed:17803915}.
CC -!- INTERACTION:
CC Q9CZV8; Q99NE5: Rims1; NbExp=4; IntAct=EBI-1551033, EBI-775541;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17803915}.
CC Note=Isoform 3 is present at the presynaptic membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CZV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZV8-4; Sequence=VSP_038354;
CC Name=3; Synonyms=Scrapper;
CC IsoId=Q9CZV8-3; Sequence=VSP_030770;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {ECO:0000269|PubMed:17803915}.
CC -!- DISRUPTION PHENOTYPE: Altered electrophysiological synaptic activity,
CC with increased frequency of miniature excitatory postsynaptic currents.
CC {ECO:0000269|PubMed:17803915}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29349.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAD90157.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF649694; ABU95014.1; -; mRNA.
DR EMBL; AK012109; BAB28039.1; -; mRNA.
DR EMBL; AK036217; BAC29349.1; ALT_SEQ; mRNA.
DR EMBL; AK144786; BAE26066.1; -; mRNA.
DR EMBL; AK220232; BAD90157.1; ALT_INIT; mRNA.
DR EMBL; AL591205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25339.1; -. [Q9CZV8-1]
DR RefSeq; NP_082425.1; NM_028149.1. [Q9CZV8-1]
DR RefSeq; XP_006534361.1; XM_006534298.3. [Q9CZV8-3]
DR RefSeq; XP_006534362.1; XM_006534299.3. [Q9CZV8-4]
DR AlphaFoldDB; Q9CZV8; -.
DR SMR; Q9CZV8; -.
DR BioGRID; 215210; 4.
DR CORUM; Q9CZV8; -.
DR IntAct; Q9CZV8; 5.
DR STRING; 10090.ENSMUSP00000099432; -.
DR iPTMnet; Q9CZV8; -.
DR PhosphoSitePlus; Q9CZV8; -.
DR SwissPalm; Q9CZV8; -.
DR EPD; Q9CZV8; -.
DR jPOST; Q9CZV8; -.
DR MaxQB; Q9CZV8; -.
DR PaxDb; Q9CZV8; -.
DR PeptideAtlas; Q9CZV8; -.
DR PRIDE; Q9CZV8; -.
DR ProteomicsDB; 271819; -. [Q9CZV8-1]
DR ProteomicsDB; 271820; -. [Q9CZV8-4]
DR ProteomicsDB; 271821; -. [Q9CZV8-3]
DR Antibodypedia; 28248; 164 antibodies from 26 providers.
DR DNASU; 72194; -.
DR Ensembl; ENSMUST00000103143; ENSMUSP00000099432; ENSMUSG00000020883. [Q9CZV8-1]
DR GeneID; 72194; -.
DR KEGG; mmu:72194; -.
DR UCSC; uc007lfm.1; mouse. [Q9CZV8-1]
DR UCSC; uc009vah.1; mouse. [Q9CZV8-3]
DR CTD; 84961; -.
DR MGI; MGI:1919444; Fbxl20.
DR VEuPathDB; HostDB:ENSMUSG00000020883; -.
DR eggNOG; KOG4341; Eukaryota.
DR GeneTree; ENSGT00940000153845; -.
DR HOGENOM; CLU_016072_7_1_1; -.
DR InParanoid; Q9CZV8; -.
DR OMA; TKTTDAX; -.
DR OrthoDB; 1046098at2759; -.
DR PhylomeDB; Q9CZV8; -.
DR TreeFam; TF313434; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 72194; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fbxl20; mouse.
DR PRO; PR:Q9CZV8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CZV8; protein.
DR Bgee; ENSMUSG00000020883; Expressed in cleaving embryo and 219 other tissues.
DR ExpressionAtlas; Q9CZV8; baseline and differential.
DR Genevisible; Q9CZV8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0099575; P:regulation of protein catabolic process at presynapse, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
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; 4.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 12.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..436
FT /note="F-box/LRR-repeat protein 20"
FT /id="PRO_0000119871"
FT DOMAIN 22..68
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 74..100
FT /note="LRR 1"
FT REPEAT 101..126
FT /note="LRR 2"
FT REPEAT 127..152
FT /note="LRR 3"
FT REPEAT 153..178
FT /note="LRR 4"
FT REPEAT 179..204
FT /note="LRR 5"
FT REPEAT 205..230
FT /note="LRR 6"
FT REPEAT 231..256
FT /note="LRR 7"
FT REPEAT 257..282
FT /note="LRR 8"
FT REPEAT 283..308
FT /note="LRR 9"
FT REPEAT 309..334
FT /note="LRR 10"
FT REPEAT 335..363
FT /note="LRR 11"
FT REPEAT 364..388
FT /note="LRR 12"
FT REPEAT 389..414
FT /note="LRR 13"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038354"
FT VAR_SEQ 1..14
FT /note="MRRDVNGVTKSRFE -> MAPSRDRLLHFGFKAT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17803915"
FT /id="VSP_030770"
FT CONFLICT 40
FT /note="L -> P (in Ref. 2; BAB28039)"
FT /evidence="ECO:0000305"
FT CONFLICT 379..381
FT /note="HSL -> PSF (in Ref. 2; BAB28039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48396 MW; 3218F38C02EA1BCE CRC64;
MRRDVNGVTK SRFEMFSNSD EAVINKKLPK ELLLRIFSFL DVVTLCRCAQ VSRAWNVLAL
DGSNWQRIDL FDFQRDIEGR VVENISKRCG GFLRKLSLRG CLGVGDNALR TFAQNCRNIE
VLSLNGCTKT TDATCTSLSK FCSKLRHLDL ASCTSITNMS LKALSEGCPL LEQLNISWCD
QVTKDGIQAL VRGCGGLKAL FLKGCTQLED EALKYIGAHC PELVTLNLQT CLQITDEGLI
TICRGCHKLQ SLCASGCSNI TDAILNALGQ NCPRLRILEV ARCSQLTDVG FTTLARNCHE
LEKMDLEECV QITDSTLIQL SIHCPRLQVL SLSHCELITD DGIRHLGNGA CAHDQLEVIE
LDNCPLITDA SLEHLKSCHS LERIELYDCQ QITRAGIKRL RTHLPNIKVH AYFAPVTPPP
SVGGSRQRFC RCCIIL
