FXL15_DICLA
ID FXL15_DICLA Reviewed; 292 AA.
AC E6ZHJ8; E6ZHJ9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=F-box/LRR-repeat protein 15;
GN Name=fbxl15; ORFNames=DLA_Ib03740, DLA_Ib03750;
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kuhl H., Tine M., Beck A., Timmermann B., Reinhardt R.;
RT "Chromosome directed sequencing of European seabass (Dicentrarchus labrax
RT L.) by comparatively mapped BAC clones.";
RL Submitted (JUN-2010) 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 target
CC proteins. Acts as a positive regulator of the BMP signaling pathway).
CC Required for dorsal/ventral pattern formation (By similarity.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXL15). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FBXL15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBN81533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FQ310507; CBN81532.1; -; Genomic_DNA.
DR EMBL; FQ310507; CBN81533.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; E6ZHJ8; -.
DR SMR; E6ZHJ8; -.
DR Ensembl; ENSDLAT00005056512; ENSDLAP00005053134; ENSDLAG00005022905.
DR GeneTree; ENSGT00940000160250; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000694389; Unassembled WGS sequence.
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; 2.
DR SMART; SM00367; LRR_CC; 6.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Leucine-rich repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..292
FT /note="F-box/LRR-repeat protein 15"
FT /id="PRO_0000410907"
FT DOMAIN 12..59
FT /note="F-box"
FT REPEAT 134..155
FT /note="LRR 1"
FT REPEAT 160..181
FT /note="LRR 2"
FT REPEAT 186..207
FT /note="LRR 3"
FT REPEAT 212..233
FT /note="LRR 4"
FT REPEAT 238..259
FT /note="LRR 5"
SQ SEQUENCE 292 AA; 32866 MW; DAC1B93FB8634CBE CRC64;
MDEEAKIRTC QLLDLPWEDV LIPHILCYLP LQHLVSLQRV SKQFHSLIQV YLTNCRTFDL
TSIGPSIPKE AFCSMLKDNK VLHSLSLQNC SDWVTDKELL PVIGQNQHLQ RVDMSGCVCL
TRHSLVAVSL SCMHLQHLGL AHCEWVDSLS LRSLADHCGG LQSIDLTACR QLKDDAICYL
AKKCLKLRSL SLAVNANITD ESVEEVAKNC RGLEQLDLTG CLRVRNQSIR TLAEYCPKLQ
SLKVNHCHNV TESSLDPLRK RNVVIDVEPP LQRALVLLQD VLGFAPFINL QI
