ID   CRBN_DROSE              Reviewed;         587 AA.
AC   B4HJA7;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-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=GM23853;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH480815; EDW42779.1; -; Genomic_DNA.
DR   RefSeq; XP_002031793.1; XM_002031757.1.
DR   AlphaFoldDB; B4HJA7; -.
DR   SMR; B4HJA7; -.
DR   STRING; 7238.B4HJA7; -.
DR   EnsemblMetazoa; FBtr0206838; FBpp0205330; FBgn0178718.
DR   GeneID; 6607004; -.
DR   KEGG; dse:6607004; -.
DR   HOGENOM; CLU_028769_0_0_1; -.
DR   OMA; AYQMYDS; -.
DR   PhylomeDB; B4HJA7; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001292; 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..587
FT                   /note="Protein cereblon"
FT                   /id="PRO_0000393885"
FT   DOMAIN          227..451
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          452..561
FT                   /note="CULT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..103
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         457
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         460
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         526
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT   BINDING         529
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ   SEQUENCE   587 AA;  66528 MW;  D1A65A918965B57C CRC64;
     MDEEENSEIN SVQARNEDVQ LEDQSQSQGL QDRQVDAIEQ AWNDAMPDEP SPPAEYAFQD
     PLAIVGEGGD APEAMVEDVL QDDTVSEGSH PSSDMSLESP GSEDDSDVQG LPNWMIPQNR
     LRSAVDMMVS QARNRDGGIA ALLSGDNFLQ RVRSMVFSQE RRRSRTSEET SQEEAAEEPD
     DPPPQQPPLP PIDIGFDTNL PAEHSYFGNH LSRVPGVDYL EVGSVHHMLI FLHHHILFPG
     EVLPFMIDGQ MFDDDMPGLD GLIFGVSFPR LQPPEDNPHK LYGVTCQIYE RGESGRGLVF
     YKSRALQRIV INCDDIKGSP QYIARNPTNK CFSKVKILPE YFLPEPLQSV DMGSMARFRD
     IPSMRDKYRR FQLSTTTWPS DACQEYSFAS IVERARQRLE SQKIDTMPKC PIQLSFWLVR
     NLHLTEKMMR LTFLTDSVNT RLQLIKSTFK DETLFFCRYC NSSLALCSDL FAMSKHGVQT
     QYCNPEGYIH ETNTVYRVIS HAIGYSGEPS TKFSWFPGYQ WHIILCKFCA QHVGWEFKAV
     LPNLTPNVFF GLSGSSVRIG KASEYSPFNG TTYVVRNMLR MISSDME