CRBN_DROMO
ID CRBN_DROMO Reviewed; 676 AA.
AC B4KCG1;
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=GI23135;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW14780.1; -; Genomic_DNA.
DR RefSeq; XP_001999319.1; XM_001999283.2.
DR AlphaFoldDB; B4KCG1; -.
DR SMR; B4KCG1; -.
DR STRING; 7230.FBpp0172352; -.
DR PRIDE; B4KCG1; -.
DR EnsemblMetazoa; FBtr0173860; FBpp0172352; FBgn0145862.
DR GeneID; 6573232; -.
DR eggNOG; KOG1400; Eukaryota.
DR HOGENOM; CLU_028769_0_0_1; -.
DR InParanoid; B4KCG1; -.
DR OMA; PWPIEAC; -.
DR OrthoDB; 1069900at2759; -.
DR PhylomeDB; B4KCG1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009192; 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..676
FT /note="Protein cereblon"
FT /id="PRO_0000393882"
FT DOMAIN 314..540
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 541..650
FT /note="CULT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ SEQUENCE 676 AA; 75648 MW; DE3B73BA346C25C5 CRC64;
MDDEETAEID ETSSSSTNTN TNATAMATAT ETAAEMHVEL EQDEEIPQGS ENGAGTGAGD
GTRAEAGASA IHAETTAHVS SRARLENMIE EVDNMFEEVS ELMVDVTELM RRANQLREDA
GTGAVPQNPT VATNTTPPAE IEEEEEGPEQ QAEQALVNND SPSQASISSR HSGSDMSLDS
PGSEDDSDAE AVPRWMIPAN RVRSAVDMLV SQARNRDGGI ATLLRRENFL QRVRSMVFSQ
DRIRGRASDD ANNADVINTV PDDTSEASPP PPLDVDMEEG VRFDTNLPAE HSYFGTNLNR
VPGVDYLEVG STHRMLIFMH QHILFPGEVL PFMIDGNIID EEIEDTGRDG VIFGVGFPLM
QPPDDNPHKL YGVTCQIYEK GESGRQHVFY KSRALQRIVI NCDDIQGPPQ YIARNPTMKC
YSKVKILPEY FLPEPLKCID MGSLNRFRDI PSMQEKFRRF QLTTTPWPVE ACGEYSFEHI
VEKARQKLEI HKIDTMPKCP IQLSFWLVRN LHLTEKMMRL TFLTDSVNIR LQIIGTTLKH
ESLFYCRYCN SSLAYCSDLF AMSKHGVQTQ YCNSAGYIHE TNTVYRVIAH AIGYSGEPST
EFSWFPGYQW HIIICKFCAQ HVGWEFKAVE PNLAPKVFFG LAGSSVRIGK TSERTPTHGS
RFVVRNLLRL VSRELE
