ID   CRBN_DROWI              Reviewed;         612 AA.
AC   B4N8G7;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=GK12054;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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; CH964232; EDW81418.1; -; Genomic_DNA.
DR   RefSeq; XP_002070432.1; XM_002070396.2.
DR   AlphaFoldDB; B4N8G7; -.
DR   SMR; B4N8G7; -.
DR   STRING; 7260.FBpp0241197; -.
DR   EnsemblMetazoa; FBtr0242705; FBpp0241197; FBgn0214065.
DR   GeneID; 6646980; -.
DR   KEGG; dwi:6646980; -.
DR   eggNOG; KOG1400; Eukaryota.
DR   HOGENOM; CLU_028769_0_0_1; -.
DR   InParanoid; B4N8G7; -.
DR   OMA; PWPIEAC; -.
DR   OrthoDB; 1069900at2759; -.
DR   PhylomeDB; B4N8G7; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..612
FT                   /note="Protein cereblon"
FT                   /id="PRO_0000393888"
FT   DOMAIN          250..476
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          477..586
FT                   /note="CULT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         482
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         485
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         551
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         554
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ   SEQUENCE   612 AA;  68797 MW;  0612480DDB52D47C CRC64;
     MDDEETAEIE DVNVLVPATG GEGPVDGASA MGAVQETENV NEESEAQREE DVVRDYMMEL
     IRQSDEQLAA DAPDAAASTG SDGSGDDDEQ PNQNEEVGAG SGEQEDEAAS HDSDMSLDSP
     GSEDDSVVWN PHPPGWMIPP NRLHSAVDMM VTQARNSDAG IAGLLSRHHF LQRIRSIVFS
     QERRRSRTSE EGEASSEPPH TPPPPRSPYD VEMEEGIRFD TNLAAEHSYF GNNSSRVPGV
     DYLEEGSTHH MLIFLHQHIL FPGEVLPFMI DGSLIDEEMQ QNGLDGLIFA VGFPLMQPPE
     DCPNRLYGVT CQIYEKGESG RQLVFYKSRA LQRIVINCDD IQGLPQYIAR NPTNKCYSKV
     KILPEYFLPE PLKCIDMGSM SRFRDIPSMR NMYQRYQITS TPWPLDACLE YSYTDIVEKA
     RKKLEIHKID TMPKCPIQLS FWLVRNLHLT EKLMRSTFLT DSVNTRLQII GSTLKDESVF
     YCRYCNSSLA YCSDLFAMSK HGVQTQYCNS AGYIHETNTV YRVMTHAIGY SGEPTTEFSW
     FPGYQWHIIL CKFCAQHVGW EFKAVQPNLT PKLFFGLAGS SVRIGKLVEN TPVNGSTFVV
     RNLLRMVSSE ME