CRBN_DROSI
ID CRBN_DROSI Reviewed; 587 AA.
AC B4QVV3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=GD18661;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CM000364; EDX13533.1; -; Genomic_DNA.
DR RefSeq; XP_002104030.1; XM_002103994.2.
DR AlphaFoldDB; B4QVV3; -.
DR SMR; B4QVV3; -.
DR STRING; 7240.B4QVV3; -.
DR EnsemblMetazoa; FBtr0218571; FBpp0217063; FBgn0190182.
DR GeneID; 6728694; -.
DR HOGENOM; CLU_028769_0_0_1; -.
DR OMA; AYQMYDS; -.
DR PhylomeDB; B4QVV3; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000304; Chromosome 3r.
DR Bgee; FBgn0190182; Expressed in embryo and 3 other tissues.
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_0000393886"
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..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..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 157..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; 66481 MW; 8C9070D6C7637C5F CRC64;
MDEEENSEIN SVQARNEDVQ LEDQSQSQGL QDRQVDAIEQ AWNDAMPDEP SPPAEYAFHD
PLAIVGEGGD APEAMVEDVL QDDTASEGSH PSSDMSLESP GSEDDSDVQG LPNWMIPQNR
LRSAVDMMVS QARNRDGGIA ALLSGDNFLQ RVRSMVFSQE RRRSRTSEET SQEEAAEEPD
DPPPQQPPLP PIDIGFDTNL PAEHSYFGNH LSRVPGVDYL EVGSVHHMLI FLHHHILFPG
EVLPFMIDGQ MFDDDMPGLD GLIFGVSFPR LQPPEDNPHK LYGVTCQIYE RGESGRGLVF
YKSRALQRIV INCDDIKGSP QYIARNPTNK CFSNVKILPE YFLPEPLQSV DMGSMARFRD
IPSMRDKYRR FQLSTTTWPS DACQEYSFGS IVERARQRLE SQKIDTMPKC PIQLSFWLVR
NLHLTEKMMR LTFLTDSVNT RLQLIKSTFK DETLFFCRYC NSSLALCSDL FAMSKHGVQT
QYCNPEGYIH ETNTVYRVIS HAIGYSGEPS TKFSWFPGYQ WHIILCKFCA QHVGWEFKAV
LPNLTPNVFF GLSGSSVRIG KASEYSPFNG TTYVVRNMLR MISSDME