ID KLHDB_DROSI Reviewed; 623 AA.
AC B4QLQ2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Kelch-like protein diablo {ECO:0000250|UniProtKB:Q9VUU5};
GN Name=dbo {ECO:0000250|UniProtKB:Q9VUU5}; ORFNames=GD14575;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX10601.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins. May have a role in synapse
CC differentiation and growth (By similarity).
CC {ECO:0000250|UniProtKB:Q9VUU5, ECO:0000250|UniProtKB:Q9Y2M5}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9Y2M5}.
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; CM000363; EDX10601.1; -; Genomic_DNA.
DR RefSeq; XP_016032031.1; XM_016171543.1.
DR AlphaFoldDB; B4QLQ2; -.
DR SMR; B4QLQ2; -.
DR STRING; 7240.B4QLQ2; -.
DR EnsemblMetazoa; FBtr0354299; FBpp0318704; FBgn0186255.
DR GeneID; 6738203; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR OMA; CAVFNNL; -.
DR OrthoDB; 5472491at2759; -.
DR PhylomeDB; B4QLQ2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000304; Chromosome 3l.
DR Bgee; FBgn0186255; Expressed in embryo and 3 other cell types or tissues.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:EnsemblMetazoa.
DR CDD; cd18459; BACK_KLHL20; 1.
DR CDD; cd18249; BTB_POZ_KLHL20_KLEIP; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF35; ACTIN-BINDING PROTEIN IPP; 1.
DR PANTHER; PTHR24412; KELCH PROTEIN; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
PE 3: Inferred from homology;
KW Actin-binding; Kelch repeat; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..623
FT /note="Kelch-like protein diablo"
FT /id="PRO_0000379953"
FT DOMAIN 72..139
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 174..276
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REPEAT 323..369
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 371..417
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 418..464
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 466..511
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 513..558
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 559..605
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 623 AA; 68995 MW; 89A3BD2812587167 CRC64;
MGDLPGSGST AQPRDAAVTG TGGNSTAGGG SSVGSTAVDR PPSPARLSHT SEKHPKVTLT
ELNMLRRHRE LCDVVLNVGG RKIFAHRVIL SACSSYFCAM FTGELEESRQ TEVTIRDIDE
NAMELLIDFC YTAHIIVEES NVQTLLPAAC LLQLVEIQDI CCEFLKRQLD PTNCLGIRAF
ADTHSCRELL RIADKFTQHN FQEVMESEEF LLLPVGQLVD IICSDELNVR SEEQVFNAVM
SWLKYNVAER RQHLAQVLQH VRLPLLSPKF LVGTVGSDLL VRSDEACRDL VDEAKNYLLL
PQERPLMQGP RTRPRKPTRR GEVLFAVGGW CSGDAIASVE RFDPQTNDWK MVAPMSKRRC
GVGVAVLNDL LYAVGGHDGQ SYLNSIERYD PQTNQWSCDV APTTSCRTSV GVAVLDEFLY
AVGGQDGVQC LNHVERYDPK ENKWSKVAPM TTRRLGVAVA VLGGFLYAIG GSDGQCPLNT
VERYDPRHNK WVAVSPMSTR RKHLGCAVFN NYIYAVGGRD DCMELSSAER YNPLTNTWSP
IVAMTSRRSG VGLAVVNGQL YAVGGFDGSA YLKTIEVYDP ETNQWRLCGC MNYRRLGGGV
GVMRAPQTEN YMWCENSFKQ PNS
//
