ID   FXL15_BOVIN             Reviewed;         300 AA.
AC   E1BNS0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=F-box/LRR-repeat protein 15;
GN   Name=FBXL15;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
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   -!- SIMILARITY: Belongs to the FBXL15 family. {ECO:0000305}.
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DR   EMBL; AAFC03082941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1BNS0; -.
DR   SMR; E1BNS0; -.
DR   STRING; 9913.ENSBTAP00000003249; -.
DR   PaxDb; E1BNS0; -.
DR   PRIDE; E1BNS0; -.
DR   eggNOG; KOG1947; Eukaryota.
DR   HOGENOM; CLU_065717_2_0_1; -.
DR   InParanoid; E1BNS0; -.
DR   TreeFam; TF326769; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Unplaced.
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   3: Inferred from homology;
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_0000410903"
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"
SQ   SEQUENCE   300 AA;  33152 MW;  6E871A14127041E9 CRC64;
     MEPPMDPSGG EQEPGAVRLL DLPWEDVLLP HVLSRVPLRQ LLWLQRVSRA FRALVQLHLA
     RLRRFDAAQV GPQIPRAALA WLLRDAEGLQ ELALAPCHEW LSDEDLVPVL ARNPQLRSVA
     LAGCGQLSRR ALGALAEGCP RLQRLSLAHC DWVDGLALRG LADRCPALEE LDLTACRQLK
     DEAIVYLAQR RGAGLRNLSL AVNANVGDTA VQELARNCPE LQHLDLTGCL RVGSDGIRTL
     AEYCPALRSL RVRHCHHVAE PSLSRLRKRG VDIDVEPPLH QALVLLQDMV GFAPFVNLQV