ID   FBX9_BOVIN              Reviewed;         437 AA.
AC   Q3ZBT2; F1MVQ0;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=F-box only protein 9;
GN   Name=FBXO9;
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=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 TTI1 and TELO2
CC       in a CK2-dependent manner, thereby directly regulating mTOR signaling.
CC       SCF(FBXO9) recognizes and binds mTORC1-bound TTI1 and TELO2 when they
CC       are phosphorylated by CK2 following growth factor deprivation, leading
CC       to their degradation. In contrast, the SCF(FBXO9) does not mediate
CC       ubiquitination of TTI1 and TELO2 when they are part of the mTORC2
CC       complex. As a consequence, mTORC1 is inactivated to restrain cell
CC       growth and protein translation, while mTORC2 is activated due to the
CC       relief of feedback inhibition by mTORC1 (By 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(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Interacts
CC       with TTI1 and TELO2; when TTI1 and TELO2 are phosphorylated by CK2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; DAAA02055275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC103124; AAI03125.1; -; mRNA.
DR   RefSeq; NP_001029584.1; NM_001034412.2.
DR   AlphaFoldDB; Q3ZBT2; -.
DR   STRING; 9913.ENSBTAP00000020074; -.
DR   PaxDb; Q3ZBT2; -.
DR   PRIDE; Q3ZBT2; -.
DR   Ensembl; ENSBTAT00000020074; ENSBTAP00000020074; ENSBTAG00000015083.
DR   GeneID; 511798; -.
DR   KEGG; bta:511798; -.
DR   CTD; 26268; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015083; -.
DR   VGNC; VGNC:28921; FBXO9.
DR   eggNOG; KOG2997; Eukaryota.
DR   GeneTree; ENSGT00390000014256; -.
DR   HOGENOM; CLU_041758_0_0_1; -.
DR   InParanoid; Q3ZBT2; -.
DR   OMA; DEFRENW; -.
DR   OrthoDB; 1407789at2759; -.
DR   TreeFam; TF324797; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000015083; Expressed in retina and 107 other tissues.
DR   ExpressionAtlas; Q3ZBT2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0032006; P:regulation of TOR signaling; ISS:UniProtKB.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR045118; FBXO9/FBXO48.
DR   InterPro; IPR045464; Hrt3/FBXO9_C.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   PANTHER; PTHR12874; PTHR12874; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF19270; FBO_C; 1.
DR   SUPFAM; SSF116846; SSF116846; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; TPR repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..437
FT                   /note="F-box only protein 9"
FT                   /id="PRO_0000259956"
FT   REPEAT          84..117
FT                   /note="TPR"
FT   DOMAIN          175..226
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UK97"
FT   CONFLICT        189
FT                   /note="V -> I (in Ref. 2; AAI03125)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   437 AA;  50817 MW;  C4D85EB424BC0661 CRC64;
     MAEAEEDCHS EAVREGDDDD ENESPAETDL QAQLQRFRAQ WMFELAPGGG SGNLESRPCR
     AARGSLLRAA DTRGKQELAK EEKARELFLK AVEEEQNGAL YEAIKFYRRA MQLVPDIEFK
     ITYTRSPDGD GVGNSYIEDT DDDSKMADLL SYFQQQLTFQ ESVLKLCQPE LESSQTHISA
     LPMEVLMYVF RWVVSSDLDL RSLEQLSQVC RGFYICARDP EIWRLACLKV WGRSCIKLVP
     YTSWREMFLE RPRVRFDGVY ISKTTYIRQG EQSLDGFYRA WHQVEYYRYV RFFPDGHVMM
     LTTPEEPQSI VPRLRTRNTR TDAILLGHYR LSQDTDNQTK VFAVITKKKE EKALDHKYRY
     FRRAPVQEAD QNFHVGLQLC SSGHQSFNKL IWIHHSCHIT YKSTGETAVT AFEIDKMYTP
     LLFARVRSYT AFSERPL