ID   KLHL8_CAEEL             Reviewed;         690 AA.
AC   G5ED84;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Kelch-like protein 8;
GN   Name=kel-8; ORFNames=W02G9.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN
RP   LIGASE COMPLEX.
RC   STRAIN=Bristol N2;
RX   PubMed=16394099; DOI=10.1091/mbc.e05-08-0794;
RA   Schaefer H., Rongo C.;
RT   "KEL-8 is a substrate receptor for CUL3-dependent ubiquitin ligase that
RT   regulates synaptic glutamate receptor turnover.";
RL   Mol. Biol. Cell 17:1250-1260(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH RPY-1.
RX   PubMed=19158078; DOI=10.1074/jbc.m808230200;
RA   Nam S., Min K., Hwang H., Lee H.O., Lee J.H., Yoon J., Lee H., Park S.,
RA   Lee J.;
RT   "Control of rapsyn stability by the CUL-3-containing E3 ligase complex.";
RL   J. Biol. Chem. 284:8195-8206(2009).
CC   -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin ligase complex that regulates degradation of glutamate
CC       receptors in neurons. The BCR(kel-8) ubiquitin ligase complex mediates
CC       ubiquitination and subsequent degradation of rpy-1. Indirectly
CC       regulates the protein turnover of glr-1, possibly via ubiquitination
CC       and degradation of rpy-1. {ECO:0000269|PubMed:16394099,
CC       ECO:0000269|PubMed:19158078}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the BCR(kel-8) E3 ubiquitin ligase complex, at
CC       least composed of cul-3, kel-8 and rbx-1. Interacts with rpy-1.
CC       {ECO:0000269|PubMed:16394099, ECO:0000269|PubMed:19158078}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:16394099}.
CC       Note=Localizes to postsynaptic clusters.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons.
CC       {ECO:0000269|PubMed:16394099}.
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DR   EMBL; DQ338465; ABC67522.1; -; mRNA.
DR   EMBL; FO081762; CCD74270.1; -; Genomic_DNA.
DR   PIR; T33222; T33222.
DR   RefSeq; NP_503729.4; NM_071328.5.
DR   AlphaFoldDB; G5ED84; -.
DR   SMR; G5ED84; -.
DR   BioGRID; 532329; 12.
DR   IntAct; G5ED84; 44.
DR   STRING; 6239.W02G9.2; -.
DR   PaxDb; G5ED84; -.
DR   EnsemblMetazoa; W02G9.2a.1; W02G9.2a.1; WBGene00020952.
DR   EnsemblMetazoa; W02G9.2a.2; W02G9.2a.2; WBGene00020952.
DR   EnsemblMetazoa; W02G9.2a.3; W02G9.2a.3; WBGene00020952.
DR   GeneID; 3565011; -.
DR   CTD; 3565011; -.
DR   WormBase; W02G9.2a; CE39523; WBGene00020952; kel-8.
DR   eggNOG; KOG4441; Eukaryota.
DR   GeneTree; ENSGT00940000157583; -.
DR   HOGENOM; CLU_004253_14_2_1; -.
DR   InParanoid; G5ED84; -.
DR   OrthoDB; 709680at2759; -.
DR   PhylomeDB; G5ED84; -.
DR   Reactome; R-CEL-8951664; Neddylation.
DR   Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; G5ED84; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:G5ED84; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00020952; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; G5ED84; baseline and differential.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR   GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR   GO; GO:0014069; C:postsynaptic density; IDA:WormBase.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.120.10.80; -; 2.
DR   Gene3D; 3.30.710.10; -; 1.
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; IPR011333; SKP1/BTB/POZ_sf.
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; SSF117281; 2.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Kelch repeat; Reference proteome; Repeat; Synapse; Ubl conjugation pathway.
FT   CHAIN           1..690
FT                   /note="Kelch-like protein 8"
FT                   /id="PRO_0000424030"
FT   DOMAIN          111..178
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          213..314
FT                   /note="BACK"
FT   REPEAT          383..430
FT                   /note="Kelch 1"
FT   REPEAT          431..477
FT                   /note="Kelch 2"
FT   REPEAT          478..524
FT                   /note="Kelch 3"
FT   REPEAT          525..571
FT                   /note="Kelch 4"
FT   REPEAT          572..618
FT                   /note="Kelch 5"
FT   REPEAT          620..665
FT                   /note="Kelch 6"
SQ   SEQUENCE   690 AA;  76763 MW;  54489B3BA012449C CRC64;
     MPVYAKAIFG SFPSVQQVRV ENGERCLIEA MDELNKNEKG LYRPVRLENG DQISTTDDVL
     NGKLARVSYT PFEEFELVSN SKGSCMEYEN QEQSSKIMEQ MRILRQTEEL CDVELLVAGS
     VIRAHRYILA AASPYFKAMF TNGMVEMKKL TIELQDIPEE SVRIIVDYIY TDKIAITMNN
     VHQLIFTATV LQMDVIVVAC QQFLATMITS HNCMSLYHFS DIYNCTNLIS SIEDFASSQF
     RCIRKSPEFN SISFHHLKSL LNRSDLNVSE EQDVFETIVQ WVSSNPRDRQ HHFVQLFKTL
     RLHLVGWNFL CEAVNSNSYV KNSQECREII SAMVLDAMTP SKRKHPESNH ENTSEYSASM
     ACPSLTASSS SSTSTFRKSV AGAIFCAGGR GKAGGPFSSV EAYDWRRNQW IEVPDMMSQR
     RHVGVVSANG NLYAIGGHDG TAHLATAEAF QPSIRQWKRI ASMKTARRGI AVASIENVIY
     AVGGLDDTTC YKTVERYDIE EDEWSTVADM DVQRGGVGVA VIGRYLFAIG GNDGTSSLET
     CERFDPMIDK WKRIASMKNR RAGSGVCVLD GYLYAIGGFD DNAPLETCER YDPDADKWIT
     LDKMSSPRGG VGVAALGGKV YAIGGHDGSD YLNTVECYDP IANRWQPAAE IKECRAGAGV
     AWANVRMHQL SRTPEKCDSG CAPSGGSYCI