ID   FBX9_RAT                Reviewed;         435 AA.
AC   Q5U2X1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=F-box only protein 9;
GN   Name=Fbxo9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; BC085831; AAH85831.1; -; mRNA.
DR   RefSeq; NP_001011998.1; NM_001011998.1.
DR   AlphaFoldDB; Q5U2X1; -.
DR   STRING; 10116.ENSRNOP00000010961; -.
DR   iPTMnet; Q5U2X1; -.
DR   PhosphoSitePlus; Q5U2X1; -.
DR   PaxDb; Q5U2X1; -.
DR   GeneID; 300849; -.
DR   KEGG; rno:300849; -.
DR   UCSC; RGD:1310374; rat.
DR   CTD; 26268; -.
DR   RGD; 1310374; Fbxo9.
DR   VEuPathDB; HostDB:ENSRNOG00000008214; -.
DR   eggNOG; KOG2997; Eukaryota.
DR   HOGENOM; CLU_041758_0_0_1; -.
DR   InParanoid; Q5U2X1; -.
DR   OMA; DEFRENW; -.
DR   OrthoDB; 1407789at2759; -.
DR   PhylomeDB; Q5U2X1; -.
DR   TreeFam; TF324797; -.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5U2X1; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000008214; Expressed in cerebellum and 19 other tissues.
DR   Genevisible; Q5U2X1; RN.
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; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; ISO:RGD.
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   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; TPR repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..435
FT                   /note="F-box only protein 9"
FT                   /id="PRO_0000119888"
FT   REPEAT          82..115
FT                   /note="TPR"
FT   DOMAIN          173..224
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   435 AA;  50689 MW;  737BE1C8C2C2EAD9 CRC64;
     MAEAEEDCHS DAVRVGDEGH ESPAERDLQA QLQMFRAQWM FELTPGVGSS NVESRPCRAG
     RSSILKAAAD KGRQELAKEE KARELFLKAV EEEQNGALYE AIKFYRRAMQ LVPDIEFKIT
     YTRSPDGDGV GSSYIEDNED ASKMADLLSY FQQQLTFQES VLKLCQPELE TSQTHISVLP
     MEVLMYIFRW VVSSDLDLRS LEQLSLVCRG FYICARDPEI WRLACLKVWG RSCMKLVPFS
     SWREMFLERP RVRFDGVYIS KTTYIRQGEQ SLDGFYRAWH QVEYYRYIRF FPDGHVMMLT
     TPEEPPSIVP RLRTRNTRTD AILLGHYRLS QDADNQTKVF AVITKKKEEK PLDHKYRYFR
     RVPVQEADHN FHVGLQLCSS GHQRFNKLIW IHHSCHITYR STGETAVSAF DIDKMYTPLF
     FARVRSYTAF SERPL