ID   FXL17_XENLA             Reviewed;         673 AA.
AC   B1H1X1; A0A1L8I1L2;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=F-box/LRR-repeat protein 17 {ECO:0000303|PubMed:30190310};
DE   AltName: Full=F-box and leucine-rich repeat protein 17 {ECO:0000305};
GN   Name=fbxl17 {ECO:0000303|PubMed:30190310,
GN   ECO:0000312|Xenbase:XB-GENE-4755769};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J;
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA   Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=30190310; DOI=10.1126/science.aap8236;
RA   Mena E.L., Kjolby R.A.S., Saxton R.A., Werner A., Lew B.G., Boyle J.M.,
RA   Harland R., Rape M.;
RT   "Dimerization quality control ensures neuronal development and survival.";
RL   Science 362:eaap8236-eaap8236(2018).
CC   -!- FUNCTION: Substrate-recognition component of the SCF(FBXL17) E3
CC       ubiquitin ligase complex, a key component of a quality control pathway
CC       required to ensure functional dimerization of BTB domain-containing
CC       proteins (dimerization quality control, DQC) (PubMed:30190310). FBXL17
CC       specifically recognizes and binds a conserved degron of non-consecutive
CC       residues present at the interface of BTB dimers of aberrant
CC       composition: aberrant BTB dimer are then ubiquitinated by the
CC       SCF(FBXL17) complex and degraded by the proteasome (By similarity). The
CC       ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers
CC       is required for the differentiation and survival of neural crest and
CC       neuronal cells (PubMed:30190310). {ECO:0000250|UniProtKB:Q9UF56,
CC       ECO:0000269|PubMed:30190310}.
CC   -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC       complex SCF(FBXL17). Interacts with BTB domain-containing proteins;
CC       specifically recognizes and binds a conserved degron of non-consecutive
CC       residues present at the interface of BTB dimers of aberrant
CC       composition. {ECO:0000250|UniProtKB:Q9UF56}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UF56}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9UF56}. Note=Present in the cytoplasm and
CC       nucleus; more abundant in the cytoplasm.
CC       {ECO:0000250|UniProtKB:Q9UF56}.
CC   -!- TISSUE SPECIFICITY: Expressed in the neuro-ectoderm of embryos.
CC       {ECO:0000269|PubMed:30190310}.
CC   -!- DISRUPTION PHENOTYPE: Impaired nervous system development caused by
CC       inability to eliminate aberrant BTB domain-containing protein dimers.
CC       {ECO:0000269|PubMed:30190310}.
CC   -!- SIMILARITY: Belongs to the FBXL17 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=OCU02262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM004466; OCU02262.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC160768; AAI60768.1; -; mRNA.
DR   RefSeq; NP_001121244.1; NM_001127772.1.
DR   AlphaFoldDB; B1H1X1; -.
DR   SMR; B1H1X1; -.
DR   STRING; 8355.B1H1X1; -.
DR   GeneID; 100158323; -.
DR   KEGG; xla:100158323; -.
DR   CTD; 100158323; -.
DR   Xenbase; XB-GENE-4755769; fbxl17.L.
DR   OrthoDB; 524674at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 100158323; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR   GO; GO:0014033; P:neural crest cell differentiation; IMP:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.80.10.10; -; 2.
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; PF12937; F-box-like; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 11.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Neurogenesis; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..673
FT                   /note="F-box/LRR-repeat protein 17"
FT                   /id="PRO_0000445655"
FT   DOMAIN          291..338
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  73081 MW;  496B8ACF210F4EA8 CRC64;
     MGHVAPHASK KEHVAPHAAE KDHVAPHASK KEHVAPHAAE KGQVAPYAAG EGQVAPNAAG
     ERPVAPYAAG EGQVAPYAAG EGQVAPYAAG EGQVAPYAAG EGQVAPYAAG EAQVAPHAAG
     EGRVAPHAAG DGQVEHCTVE DREEGHIGTT EQGHMSHYTS KLEHMAPPSA QTEAVVSYVA
     GERHAPPDCT VSGPAMCCSA EARQTTPDWT TTGPEISQGT LPGLTVLHVG GTWQTFAAED
     EPCVTTLLSP VKPLSSSRKY APYNLQIPSY SESEPQAHKG LSSETFGPCE PLHINQLPSS
     LLLKIFSNLS LNERCILASL VCKYWRDLCL DSQFWKQLDL SNRQQIKDNI LEEIASRSQN
     ITEINISDCF SVSDQGVCVV ALKCPGLVKY TAYRCKQLSD ISLIALAAHC PSLQKVHVGN
     QDKLSDEALI QMGRRCKELK DIHFGQCYKI SDEGLIVIAK GCQKLQKIYM QENKLVSDES
     VKAFAEHCPG LQYVGFMGCS VTSEGVINLT KLKHLSSLDL RHITELDNET VMEIVKQCQH
     LTSLNLCLNR SINDRCVEVI AKEGRSLKEL YLVTCKITDY ALIAIGRYSK SIETVDVGWC
     KEITDYGAKQ IAQSSKSIRY LGLMRCDKVN EATVEQLVQQ YPHITFSTVL QDCKRTLERA
     YQMGWTPNAS PAT