ID   CRBN_DROAN              Reviewed;         520 AA.
AC   B3M1F2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-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=GF17853;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV42179.1; -; Genomic_DNA.
DR   RefSeq; XP_001953618.2; XM_001953582.2.
DR   AlphaFoldDB; B3M1F2; -.
DR   SMR; B3M1F2; -.
DR   STRING; 7217.FBpp0121045; -.
DR   eggNOG; KOG1400; Eukaryota.
DR   HOGENOM; CLU_028769_0_0_1; -.
DR   InParanoid; B3M1F2; -.
DR   OMA; PWPIEAC; -.
DR   PhylomeDB; B3M1F2; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007801; 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..520
FT                   /note="Protein cereblon"
FT                   /id="PRO_0000393878"
FT   DOMAIN          160..384
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          385..494
FT                   /note="CULT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         393
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         462
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ   SEQUENCE   520 AA;  59216 MW;  0C19EA528ABEEC97 CRC64;
     MDDEETAEVE VEANPLDPID DAIQDDLSPL DPPSSDMSLE SPGSEDDSDL EALPRWMIPQ
     NRLRSAVDMM VSQARTQNGG IAALLNRDNF LQRVRSMVFS QERRRSRTSD DTSQDGGEQA
     EEPPQPIPRT PIDIDMEEGV RFDTNLPAEH SYFGNHLSRV PGVDYLEHIL FPGEVLPFMI
     DGSLFDDEMP GLDGLIFGVG FPLMQPPEDN PHKLYGVTCQ VYEKGESGRQ LVFYKSRALQ
     RIVINCDDIQ GPPQYIARNP TSKCFSKVKI LPEYFLPEPL KCVDMGSMSR FRDIPSMRDK
     YRRYQLSSTP WPADACQEYA YEEIVERARK KLEIHKIDTM PRCPIQLSFW LVRNLHLTEK
     MMRLTFLTDS VNTRLQLIGS TLKEESLFYC RYCNSSLAYC SDLFAMSKHG VQTQYCNPEG
     YIHETNTVYR VMSHAIGYSG EPSTKFSWFP GYQWHIILCK FCAQHVGWEF KAVEPNLAPK
     VFFGLAGSSV RIGKASESTP VNGSSFVVRN MLRLISNEME