FBW15_MOUSE
ID FBW15_MOUSE Reviewed; 466 AA.
AC L7N1X6; Q4FZL6; Q4PLJ2; Q8BI39;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=F-box/WD repeat-containing protein 15 {ECO:0000303|PubMed:18094359};
GN Name=Fbxw15 {ECO:0000312|MGI:MGI:3505701};
GN Synonyms=Fbxo12J {ECO:0000303|PubMed:18094359,
GN ECO:0000312|MGI:MGI:3505701};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAY68032.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAY68032.1};
RX PubMed=18094359; DOI=10.1095/biolreprod.107.063826;
RA De La Chesnaye E., Kerr B., Paredes A., Merchant-Larios H., Mendez J.P.,
RA Ojeda S.R.;
RT "Fbxw15/Fbxo12J is an F-box protein-encoding gene selectively expressed in
RT oocytes of the mouse ovary.";
RL Biol. Reprod. 78:714-725(2008).
RN [2] {ECO:0000312|EMBL:BAC39962.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC39962.1};
RC TISSUE=Ovary {ECO:0000312|EMBL:BAC39962.1};
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] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [4] {ECO:0000312|EMBL:AAH99378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH99378.1};
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAH99378.1};
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 [5] {ECO:0000305}
RP FUNCTION, PATHWAY, IDENTIFICATION IN AN SCF COMPLEX, INTERACTION WITH KAT7
RP AND SKP1, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23319590; DOI=10.1074/jbc.m112.426882;
RA Zou C., Chen Y., Smith R.M., Snavely C., Li J., Coon T.A., Chen B.B.,
RA Zhao Y., Mallampalli R.K.;
RT "SCF(Fbxw15) mediates histone acetyltransferase binding to origin
RT recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate
RT cell proliferation.";
RL J. Biol. Chem. 288:6306-6316(2013).
CC -!- FUNCTION: Substrate-recognition component of an SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex. Promotes KAT7 ubiquitination
CC and subsequent degradation in collaboration with MAP2K1 kinase, leading
CC to reduced histone H3K14 acetylation and increased cell proliferation.
CC {ECO:0000269|PubMed:23319590}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23319590}.
CC -!- SUBUNIT: Part of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein
CC ligase complex. Interacts with KAT7 and SKP1.
CC {ECO:0000269|PubMed:23319590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18094359,
CC ECO:0000269|PubMed:23319590}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:18094359}. Nucleus {ECO:0000269|PubMed:23319590}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=L7N1X6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=L7N1X6-2; Sequence=VSP_059276;
CC -!- TISSUE SPECIFICITY: Specifically expressed in oocytes from follicles of
CC the medullary region of the ovary. {ECO:0000269|PubMed:18094359}.
CC -!- DEVELOPMENTAL STAGE: Detected at 18 dpc, and then decreases thereafter
CC to a very low level at the day of birth. Detected again at 48 hours
CC postpartum, and then increases at 96 hours until 6 days after birth.
CC {ECO:0000269|PubMed:18094359}.
CC -!- INDUCTION: Up-regulated in response to bacterial lipopolysaccharides
CC (LPS). {ECO:0000269|PubMed:23319590}.
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; DQ067445; AAY68032.1; -; mRNA.
DR EMBL; AK087669; BAC39962.1; -; mRNA.
DR EMBL; AC161593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099378; AAH99378.1; -; mRNA.
DR CCDS; CCDS23553.1; -. [L7N1X6-1]
DR RefSeq; NP_950201.2; NM_199036.2. [L7N1X6-1]
DR RefSeq; XP_006512232.1; XM_006512169.2. [L7N1X6-2]
DR AlphaFoldDB; L7N1X6; -.
DR STRING; 10090.ENSMUSP00000058175; -.
DR PaxDb; L7N1X6; -.
DR PRIDE; L7N1X6; -.
DR DNASU; 382105; -.
DR Ensembl; ENSMUST00000056745; ENSMUSP00000058175; ENSMUSG00000074060. [L7N1X6-1]
DR Ensembl; ENSMUST00000198397; ENSMUSP00000143385; ENSMUSG00000074060. [L7N1X6-2]
DR GeneID; 382105; -.
DR KEGG; mmu:382105; -.
DR UCSC; uc009rsl.1; mouse. [L7N1X6-1]
DR UCSC; uc012hbe.1; mouse.
DR CTD; 382105; -.
DR MGI; MGI:3505701; Fbxw15.
DR VEuPathDB; HostDB:ENSMUSG00000074060; -.
DR eggNOG; ENOG502QT73; Eukaryota.
DR GeneTree; ENSGT00940000162557; -.
DR HOGENOM; CLU_046549_1_0_1; -.
DR InParanoid; L7N1X6; -.
DR OrthoDB; 770934at2759; -.
DR PhylomeDB; L7N1X6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 382105; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fbxw15; mouse.
DR PRO; PR:L7N1X6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; L7N1X6; protein.
DR Bgee; ENSMUSG00000074060; Expressed in primary oocyte and 15 other tissues.
DR ExpressionAtlas; L7N1X6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..466
FT /note="F-box/WD repeat-containing protein 15"
FT /id="PRO_0000442736"
FT DOMAIN 1..45
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 101..143
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 146..185
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 187..228
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 339..379
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 381..419
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT VAR_SEQ 208..390
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VSP_059276"
FT CONFLICT 229
FT /note="V -> D (in Ref. 1; AAY68032)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="L -> W (in Ref. 2; BAC39962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 53586 MW; 3FF5E0FF8C091E43 CRC64;
MAIHLPCLPM MKILSYLDAY SLLQAAQVNK DWNELASSDV LWRKLCQKRW LYCDMDTLQL
QGKETWKQFF IDRIWQERAK FRAKAKDFTY KEIPLMCGLF GYACYISGCG LTRKGQDKSV
VCMVNSKNTI STWDVHKSVI TWKSPEQPAS IKLLTTLPEM HIAVTVDIQS TIKLWDCHNR
EALATNNLKS PCKSLKAVFT KDGPIVLIGD TLGNIHIFRI PDLYLISTVN VLPYGFDGIY
CSPQKKWVLL SKKHPHILPK VFYMSSFLRT SEFSAPVSTV LKLSLYERVF WTPRREDRIT
LMSRSGFPQV KMFETYDIKL EEFGNKRIVK GKLIASFELQ CHKVNPQRFG VSDKNVIVCS
TESSLLLFDI NGLRLKTFQY CPEMIVKLSV DPLHVIVICN TGSMDVYAWE ERSLLLRKCY
RLHIERPLPL YGFIYKAACD DVSIIQLITD ELSLSSLTSY ALNICS
