ID   CRBN_DROPE              Reviewed;         616 AA.
AC   B4GZ07;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
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=GL27201;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479198; EDW28025.1; -; Genomic_DNA.
DR   RefSeq; XP_002023822.1; XM_002023786.1.
DR   AlphaFoldDB; B4GZ07; -.
DR   SMR; B4GZ07; -.
DR   STRING; 7234.FBpp0191308; -.
DR   EnsemblMetazoa; FBtr0192816; FBpp0191308; FBgn0164782.
DR   GeneID; 6598641; -.
DR   KEGG; dpe:6598641; -.
DR   eggNOG; KOG1400; Eukaryota.
DR   HOGENOM; CLU_028769_0_0_1; -.
DR   OMA; AYQMYDS; -.
DR   PhylomeDB; B4GZ07; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008744; 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: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; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..616
FT                   /note="Protein cereblon"
FT                   /id="PRO_0000393883"
FT   DOMAIN          257..480
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          481..590
FT                   /note="CULT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         486
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         489
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         555
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         558
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ   SEQUENCE   616 AA;  69099 MW;  935850ED0AD2739A CRC64;
     MDEEETAEIN AQEQEVAGSA GEAAAGPSGA EVQPNDDSVA VERVIDVFEE TAEMEAAMIE
     RFFGPSGEVA EEGTLPVPGP SADGEGSANA GGERPSEEDI VLDDGTESDG SYNRPGSDMS
     LDSPNSEDDS DVEAMPRWMI PQNRLRFAVD MMVSQARNQD GGIAALLNRD NFLQRVRSMV
     FSQERRRSRN SDEVSPEAED DELPEHPPPP PPRPPIDIDM EEGVHFDTNL PAEHSYFGPN
     LNRVPGVNYQ EVGSTHHMLI FLHQYILFPG EVLPFMIDGS LFDDDMSGLD GLIFAVAFPL
     MKPPEDSKKL YGVTCQIYEK GDNGRHLTFY KSRALQRIVI NCSDIKGLPQ YIARNPTNKC
     HSKVKILPEY FLPEPLKCID MGSMSRFRDI PSMRDKYLRY QISSTPWPVE VCQEYAYEDI
     VERARKKLEV HKIDTMPKCP IQMSFWLVRN LHLTEKMMSQ MFLTDSVNLR LQLIGGILKE
     ETLFYCRYCN SSLAYCSDLF AMSKHGVQTQ YCNPGGYIHE TNTVYRVISH AIGYSGEPST
     RFSWFPGYQW HIILCKFCAQ HVGWEFKAVE PNLAPKVFYG LAGSSVRIGK AGDSATVNGN
     NFVVRNMLRV ISEGME