ID   CRBN_DROYA              Reviewed;         588 AA.
AC   B4PVI7;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Protein cereblon {ECO:0000250|UniProtKB:Q9VH36};
DE   AltName: Full=Protein ohgata {ECO:0000250|UniProtKB:Q9VH36};
GN   Name=ohgt {ECO:0000250|UniProtKB:Q9VH36};
GN   Synonyms=crbn {ECO:0000250|UniProtKB:Q9VH36}; ORFNames=GE26004;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
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: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3
CC       protein ligase complex that mediates the ubiquitination and subsequent
CC       proteasomal degradation of target proteins. Has an essential role in
CC       mediating growth by negatively regulating insulin signaling. It also
CC       has a role in maintaining presynaptic function in the neuromuscular
CC       junction synapses of third-instar larvae.
CC       {ECO:0000250|UniProtKB:Q9VH36}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q96SW2}.
CC   -!- SUBUNIT: Likely a component of a DCX (DDB1-CUL4-X-box) protein ligase
CC       complex (By similarity). May interact with pic/DDB1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q96SW2, ECO:0000250|UniProtKB:Q9VH36}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9VH36}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9VH36}.
CC   -!- SIMILARITY: Belongs to the CRBN family. {ECO:0000305}.
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DR   EMBL; CM000160; EDW96760.1; -; Genomic_DNA.
DR   RefSeq; XP_002097048.1; XM_002097012.2.
DR   AlphaFoldDB; B4PVI7; -.
DR   SMR; B4PVI7; -.
DR   STRING; 7245.FBpp0271014; -.
DR   EnsemblMetazoa; FBtr0272522; FBpp0271014; FBgn0243047.
DR   GeneID; 6536467; -.
DR   KEGG; dya:Dyak_GE26004; -.
DR   eggNOG; KOG1400; Eukaryota.
DR   HOGENOM; CLU_028769_0_0_1; -.
DR   OMA; AYQMYDS; -.
DR   OrthoDB; 1069900at2759; -.
DR   PhylomeDB; B4PVI7; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd15777; CRBN_C_like; 1.
DR   InterPro; IPR034750; CULT.
DR   InterPro; IPR003111; Lon_prtase_N.
DR   InterPro; IPR004910; Yippee/Mis18/Cereblon.
DR   Pfam; PF03226; Yippee-Mis18; 1.
DR   PROSITE; PS51788; CULT; 1.
DR   PROSITE; PS51787; LON_N; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Nucleus; Ubl conjugation; Ubl conjugation pathway; Zinc.
FT   CHAIN           1..588
FT                   /note="Protein cereblon"
FT                   /id="PRO_0000393889"
FT   DOMAIN          228..452
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          453..562
FT                   /note="CULT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         461
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         527
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         530
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ   SEQUENCE   588 AA;  66707 MW;  6975DC015C16A2E4 CRC64;
     MDDEETSEIN SVQGQDEDVQ LEVQPQAQGP QDRQVDAIEQ AWNNATQDEQ SPPAEEAFQD
     PLAIDGEGGN APEAMVEDVL QDDTASEGSH PSSDMSLETP GSEDDSDLEL LPRWMIPQNR
     LRSAVDMMVS QARNRDGGIA ALLNRDNFLQ RVRSIVFSQE RRRSRTSEET SQEAADAEQP
     NDPPPQQPPR PPIDIGFDTN LPAEHSYFGN HLSRVPGVDY LEVGSVHHML IFLHQHILFP
     GEVLPFMIDG RMFDEDMPGL DGLIFGVGFP LMQPPEDNPL KLYGVTCQIY ERGESGRGLV
     FYKSRALQRI VINCEDIQGS PQYIARNPTS KCFSKVKILP EYFLPEPLQS VEMGSMARFR
     DIPSMRDKYR RFQLSTTTWP SDACQEYSFA SIVERARQRL ESQKIDTMPK CPIQLSFWLV
     RNLHLTEKMM RLTFLTDSVN TRLQLIKSTF KDESLFFCRY CNSSLAHCAD LFAMSKHGVQ
     TQYCNPDGYI HETNTVYRVM SHAIGYSGEP STKFSWFPGY QWHIILCKFC AQHVGWEFKA
     VQPNLTPRVF FGLAGSSVRI GKASENTPFN GSTYVVRNML RLISNEME