ID   CRBN_DROER              Reviewed;         586 AA.
AC   B3P4M4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
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=GG17313;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
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; CH954181; EDV49677.1; -; Genomic_DNA.
DR   RefSeq; XP_001980719.1; XM_001980683.2.
DR   AlphaFoldDB; B3P4M4; -.
DR   SMR; B3P4M4; -.
DR   STRING; 7220.FBpp0135859; -.
DR   EnsemblMetazoa; FBtr0137367; FBpp0135859; FBgn0109540.
DR   GeneID; 6552043; -.
DR   KEGG; der:6552043; -.
DR   eggNOG; KOG1400; Eukaryota.
DR   HOGENOM; CLU_028769_0_0_1; -.
DR   OMA; AYQMYDS; -.
DR   OrthoDB; 1069900at2759; -.
DR   PhylomeDB; B3P4M4; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008711; 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; Ubl conjugation; Ubl conjugation pathway; Zinc.
FT   CHAIN           1..586
FT                   /note="Protein cereblon"
FT                   /id="PRO_0000393879"
FT   DOMAIN          226..450
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          451..560
FT                   /note="CULT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         456
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         525
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         528
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ   SEQUENCE   586 AA;  66746 MW;  4A7A7B9BBD17D7C2 CRC64;
     MDDEETSEIN SVQGRDEDVQ LEDHSQAQGL QDRRVDAMEQ AWNNAIQDEL SPPPEEAFQD
     PLAIEGEGGN APEAMVEDGL QDDTASEGSH PSSDMSLESP GSEDDSDLER LPRWMIPQNR
     LRSAVDMMVS QARNRDGGIA ALLNRDNFLQ RVRSMVFSQE RRRSRTSEET SQEDVEQPED
     PPPQQPPRPP IDIGFDTNLP AEHSYFGNHL SRVPGVDYLE VGSVHHMLIF LHQHILFPGE
     VLPFMIDGRM FDEDMPGLDG LIFGVGFPLM QPPEDNQLKL YGVTCQIYEK GESGRGLVFY
     KSRALQRIVI NFDDIQGSPQ YIARNPTSKC FSKVKILPEY FLPEPLQSVD MGSMARFRDI
     PSMRDKYRRF QLSTTNWPSD ACQEYSFASI VERARQRLES QKIDTMPKCP IQLSFWLVRN
     LHLTEKMMRL TFLTDSVNTR LQLIKSTFTD ESLFFCRYCN SSLAHCADLF AMSKHGVQTQ
     YCNPDGYIHE TNTVYRVMSH AIGYSGEPST KFSWFPGYQW HIILCKFCAQ HVGWEFKAVQ
     PNLTPRVFFG LAGSSVRIGK ASENTSFNGS PYVVRNMLRL ISNEME