ID W8CDG4_CERCA Unreviewed; 619 AA.
AC W8CDG4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Kelch-like protein diablo {ECO:0000256|ARBA:ARBA00013699};
GN Name=KLH18 {ECO:0000313|EMBL:JAC04565.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAC04565.1};
RN [1] {ECO:0000313|EMBL:JAC04565.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAC04565.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
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. {ECO:0000256|ARBA:ARBA00043912}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; GAMC01001991; JAC04565.1; -; mRNA.
DR AlphaFoldDB; W8CDG4; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd18247; BTB_POZ_KLHL18; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030603; KLHL18_BTB/POZ.
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; SSF117281; Kelch motif; 2.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 85..152
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
SQ SEQUENCE 619 AA; 69808 MW; 1C706C800117A640 CRC64;
MDQWPEFSME RLNISGRDTL PSSQTKQMQQ QSQFTQQQQA FSSIMDLPDF GDCGDDQKYV
IYKHDDLFGE SYPLMREIRR QGKLCDVTLK VEEQSFSAHR IVLAGTIPYF YAMFTNNMAE
SRIKEITMKE IEPNALESLI NYAYSGQVRI DNQNVQSLMV GASFLQLTKV RNACADFLIS
RFHPHNVLGI RHFADSMSCT HLIEAADKYI DQNFAKVVQS DEFLGLDFDE LVDLIRRDEL
NVPTEEVIFE ACMKWVKHME EKRSVHFPQV LAKVRLPLLS PQFLADRVAR EELIRSSHQC
RDLLDEAKDF HLMPERRGLL QSFRTRQRCG EFIMGQIYAV GGLASNGESV STVEIYDPVV
KKWEMGEQMS MMRSRVGVAV MDGKLYAFGG FNGTERLSTV EVYDPKKNKW SQGRAMLCKR
SAVGVAALDD CIYVCGGYDG VTSLNTVECY CPKTDIWKTV APMMKYRSAG GVAALGGYVY
ALGGHDGLSI FDSVERYDPV KDVWLKMHSM LNRRCRLGVA ALNGKLYACG GYDGTSFLRS
VEVYDPITDT WSLVTPMNCK RSRVALAANM GKLWAIGGYD GETNLSTVEV YDPEADEWSF
EPSMCAHSGG VGAGVIRKQ
//
