ID   CRBN_DROVI              Reviewed;         640 AA.
AC   B4M686;
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=GJ10436;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
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; CH940652; EDW59162.1; -; Genomic_DNA.
DR   RefSeq; XP_002056050.1; XM_002056014.2.
DR   AlphaFoldDB; B4M686; -.
DR   SMR; B4M686; -.
DR   STRING; 7244.FBpp0224853; -.
DR   EnsemblMetazoa; FBtr0226361; FBpp0224853; FBgn0197716.
DR   GeneID; 6632727; -.
DR   KEGG; dvi:6632727; -.
DR   eggNOG; KOG1400; Eukaryota.
DR   HOGENOM; CLU_028769_0_0_1; -.
DR   InParanoid; B4M686; -.
DR   OMA; PWPIEAC; -.
DR   OrthoDB; 1069900at2759; -.
DR   PhylomeDB; B4M686; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008792; 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   Gene3D; 2.30.130.40; -; 1.
DR   InterPro; IPR034750; CULT.
DR   InterPro; IPR003111; Lon_prtase_N.
DR   InterPro; IPR046336; Lon_prtase_N_sf.
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..640
FT                   /note="Protein cereblon"
FT                   /id="PRO_0000393887"
FT   DOMAIN          278..504
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          505..614
FT                   /note="CULT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         510
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         513
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         579
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         582
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ   SEQUENCE   640 AA;  72352 MW;  2727185A893E359C CRC64;
     MDDEETAEID ETNSAAADMQ VELGPEQLQQ EMPQNGSGDG AAVSAIAAVS TAHVNSRARL
     ENMIEEVDNM FEEVSELMVD VTELMRRANE LREDPGTAAL AENARPPAEI EEQPAQQEEQ
     ASLPYDSPSR ASISSRHSGS DMSLDSPGSE DDSDAEAVPR WMIPANRVRS AVDMLVSQAR
     NRDGGIATLL RRENFLQRVR SMVFSQDRIR GRASDEANAD VINTVPDETP ESPPAPLDVD
     MEEGVRFDTN LPAEHSYFGT NLNRVPGVDY LEVGSTHRML IFMHQHILFP GEVLPFMIHG
     SIIDEEIQDS GRDGVIFGVG FPLMQPPDDN PHKLYGVTCQ IYEKGESGRQ HVFYKSRALQ
     RIVINCDDIQ GPPQYIARNP TMKCYSKVKI LPEYFLPEPL KCIDMGSLNR FRDIPSMEKK
     FRRYQLTSTP WPYEACEEYS FEHIVEKARQ KLEIHKIDTM PKCPIQLSFW LVRNLHLTEK
     MMRLTFLTDS VNIRLQIIDT TLKQESLFYC RYCNSSLAYC SDLFAMSKHG VQTQYCNSAG
     YIHETNTVYR VIAHAIGYSG EPSTEFSWFP GYQWHIIICK FCAQHVGWEF KAVEPNLAPK
     VFFGLAGSSV RIGKTSERTP THGSTFVVRN LLRLVSRELE