FXL15_MOUSE
ID FXL15_MOUSE Reviewed; 300 AA.
AC Q91W61; Q3T9R4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=F-box/LRR-repeat protein 15;
DE AltName: Full=F-box only protein 37;
GN Name=Fbxl15; Synonyms=Fbxo37;
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=NOD;
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=Kidney;
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;
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 TISSUE SPECIFICITY.
RX PubMed=21572392; DOI=10.1038/emboj.2011.155;
RA Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F.,
RA Zhang L.;
RT "SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-
RT type ubiquitin ligase Smurf1.";
RL EMBO J. 30:2675-2689(2011).
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 SMURF1,
CC thereby acting as a positive regulator of the BMP signaling pathway.
CC Required for dorsal/ventral pattern formation and bone mass
CC maintenance. Also mediates ubiquitination of SMURF2 and WWP2 (By
CC similarity). {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(FBXL15) composed of CUL1, SKP1, RBX1 and FBXL15.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, liver, spleen, bone, muscle,
CC brain and kidney (at protein level). {ECO:0000269|PubMed:21572392}.
CC -!- SIMILARITY: Belongs to the FBXL15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK003032; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK003032; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK172339; BAE42956.1; -; mRNA.
DR EMBL; CH466534; EDL41989.1; -; Genomic_DNA.
DR EMBL; BC016499; AAH16499.1; -; mRNA.
DR CCDS; CCDS38007.1; -.
DR RefSeq; NP_598455.2; NM_133694.2.
DR AlphaFoldDB; Q91W61; -.
DR SMR; Q91W61; -.
DR BioGRID; 212850; 5.
DR STRING; 10090.ENSMUSP00000026256; -.
DR iPTMnet; Q91W61; -.
DR PhosphoSitePlus; Q91W61; -.
DR EPD; Q91W61; -.
DR MaxQB; Q91W61; -.
DR PaxDb; Q91W61; -.
DR PeptideAtlas; Q91W61; -.
DR PRIDE; Q91W61; -.
DR ProteomicsDB; 271653; -.
DR Antibodypedia; 53264; 90 antibodies from 16 providers.
DR DNASU; 68431; -.
DR Ensembl; ENSMUST00000026256; ENSMUSP00000026256; ENSMUSG00000025226.
DR Ensembl; ENSMUST00000177667; ENSMUSP00000137489; ENSMUSG00000025226.
DR GeneID; 68431; -.
DR KEGG; mmu:68431; -.
DR UCSC; uc008hte.1; mouse.
DR CTD; 79176; -.
DR MGI; MGI:1915681; Fbxl15.
DR VEuPathDB; HostDB:ENSMUSG00000025226; -.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000160250; -.
DR HOGENOM; CLU_065717_2_0_1; -.
DR InParanoid; Q91W61; -.
DR OMA; HCHNVAE; -.
DR OrthoDB; 1154571at2759; -.
DR PhylomeDB; Q91W61; -.
DR TreeFam; TF326769; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 68431; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q91W61; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91W61; protein.
DR Bgee; ENSMUSG00000025226; Expressed in right kidney and 138 other tissues.
DR Genevisible; Q91W61; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
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; PF00646; F-box; 1.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00367; LRR_CC; 6.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Leucine-rich repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..300
FT /note="F-box/LRR-repeat protein 15"
FT /id="PRO_0000119932"
FT DOMAIN 19..66
FT /note="F-box"
FT REPEAT 141..162
FT /note="LRR 1"
FT REPEAT 167..188
FT /note="LRR 2"
FT REPEAT 194..215
FT /note="LRR 3"
FT REPEAT 220..241
FT /note="LRR 4"
FT REPEAT 246..267
FT /note="LRR 5"
FT REGION 113..269
FT /note="Interaction with SMURF1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H469"
FT CONFLICT 13
FT /note="E -> D (in Ref. 1; AK003032)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="P -> S (in Ref. 1; AK003032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33125 MW; D5DD5B9428F4887C CRC64;
MEPPMEQSGG EQEPGAVRLL DLPWEDVLLP HVLNWVPLRQ LLRLQRVSRA FRALVQLHLA
RLRRFDAAQV GPQIPRAALA RLLRDAEGLQ ELALAPCHEW LSDEDLVPVL ARNPQLRSVA
LAGCGQLSRR ALGALAEGCP RLQRLSLAHC DWVDGLALRG LADRCPALEE LDLTACRQLK
DEAIVYLAQR RGAGLRSLSL AVNANVGDTA VQELARNCPQ LEHLDLTGCL RVGSDGVRTL
AEYCPALRSL RVRHCHHVAE PSLSRLRKRG VDIDVEPPLH QALVLLQDMA GFAPFVNLQV
