ID   FBX9_DANRE              Reviewed;         421 AA.
AC   Q6P3K3; Q6DG26;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=F-box only protein 9;
GN   Name=fbxo9; ORFNames=si:ch211-71k24.1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
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 target
CC       proteins and acts as a regulator of mTOR signaling. {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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; CR376766; CAX14513.1; -; Genomic_DNA.
DR   EMBL; BC063957; AAH63957.1; -; mRNA.
DR   EMBL; BC076528; AAH76528.1; -; mRNA.
DR   RefSeq; NP_956012.1; NM_199718.2.
DR   AlphaFoldDB; Q6P3K3; -.
DR   SMR; Q6P3K3; -.
DR   STRING; 7955.ENSDARP00000093542; -.
DR   PaxDb; Q6P3K3; -.
DR   PRIDE; Q6P3K3; -.
DR   DNASU; 325469; -.
DR   Ensembl; ENSDART00000102767; ENSDARP00000093542; ENSDARG00000011055.
DR   GeneID; 325469; -.
DR   KEGG; dre:325469; -.
DR   CTD; 26268; -.
DR   ZFIN; ZDB-GENE-030131-4194; fbxo9.
DR   eggNOG; KOG2997; Eukaryota.
DR   GeneTree; ENSGT00390000014256; -.
DR   HOGENOM; CLU_041758_0_0_1; -.
DR   InParanoid; Q6P3K3; -.
DR   OMA; DEFRENW; -.
DR   OrthoDB; 1407789at2759; -.
DR   PhylomeDB; Q6P3K3; -.
DR   TreeFam; TF324797; -.
DR   Reactome; R-DRE-8951664; Neddylation.
DR   Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6P3K3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000011055; Expressed in spleen and 37 other tissues.
DR   ExpressionAtlas; Q6P3K3; 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: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; Reference proteome; TPR repeat; Ubl conjugation pathway.
FT   CHAIN           1..421
FT                   /note="F-box only protein 9"
FT                   /id="PRO_0000421761"
FT   REPEAT          68..101
FT                   /note="TPR"
FT   DOMAIN          158..209
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        16
FT                   /note="E -> G (in Ref. 2; AAH76528)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  49371 MW;  43AA514CD93F0E03 CRC64;
     MAESNQNTDG AVEEGEDENT GDSNLQMELS AFRAKWMSEL QPSSGGQRSF SRNAELRRRQ
     ETAKEEKARE LFLKAVEEEQ NGAVYEAIKY YKSAMQLVPD IEFKINYSRT PDPERGGSYL
     ESSENNREID DLLTYFQHQL TLGNDAMKLC EHETETSQVH ISALPFEVLM YIFRWVVSCD
     LDLRALEQLS LVCRGFYICA RDPEIWRSAC LRVWGRSCTK MLPYSSWREM FLERPRVRFD
     GVYISKTSYI RQGEESLDGF YRAWHQVEYY RYLRFFPDGQ VMMLTTPEDP LVTVPRLRSK
     NSRMDSIMFG HYRLSQDTDN QTKVYVVVSK RKEEKVSEYQ RSRFCRRNPV PEAERSFHVG
     LQLSSGGRQR FNKLVWIHHS CHITYRSTGE TVVTAFDVDK MYTPLFFARV KSYTAFSERP
     L