CRBN_DROGR
ID CRBN_DROGR Reviewed; 671 AA.
AC B4JSL2;
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=GH22576;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916373; EDV94752.1; -; Genomic_DNA.
DR RefSeq; XP_001994016.1; XM_001993980.1.
DR AlphaFoldDB; B4JSL2; -.
DR SMR; B4JSL2; -.
DR STRING; 7222.FBpp0156482; -.
DR EnsemblMetazoa; FBtr0157990; FBpp0156482; FBgn0130034.
DR GeneID; 6567587; -.
DR KEGG; dgr:6567587; -.
DR eggNOG; KOG1400; Eukaryota.
DR HOGENOM; CLU_028769_0_0_1; -.
DR InParanoid; B4JSL2; -.
DR OMA; PWPIEAC; -.
DR OrthoDB; 1069900at2759; -.
DR PhylomeDB; B4JSL2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001070; 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..671
FT /note="Protein cereblon"
FT /id="PRO_0000393880"
FT DOMAIN 309..535
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 536..645
FT /note="CULT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
SQ SEQUENCE 671 AA; 75174 MW; 1EA0AABD728EAE27 CRC64;
MDGEEAADID ETNSSNPHAA AVVATEMQAV AEAERPEEQQ QQQMPQTSSG EADGDVDGDG
VSAIAALATR VRLENMLEVV DNMFDEVSEL MVDVTELMQR ASELTGTTTP TPTAPENQAE
NAPEIEPAQP ATPPEIAELL EEAIAANPLG HNVLNPGDDA RSISSRHSGS DMSLDSPGSE
DDSDAEAVPR WIIPENRVRS AVDMLVSQAR NQDGGIATLL RRENFLQRVR SMVFSQDRVR
GRESDEANLD AGNVVDEELS PELSPAPLDI DMEEGVRFDT NLPAEHSYFG PNLNRVPGVD
YLEVGSTHRM LIFMHQHILF PGEVLPFMID GSIIDEEIHD TGRDGVIFGV GFPLMQPPDD
NPHKLYGVTC QIYEKGESGR QMVFYKSRAL QRIVINCDDI QGPPQYIARN PTMKCYSKVK
VLPEYFLPEP LKCIDMGSLN RFRDLPSMQD KFRRYQLTST PWPLEACEEY SFEHIVEMAR
KKLEVHKIDT MPKCPIQLSY WLVRNLHLTE KMMRLTFLTD SVNTRLQIIG STLKQESLFY
CRYCNSSLAY CSDLFAMSKH GVQTQYCNSA GYIHETNTVY RIIAHAVGYS GEPSTEFSWF
PGYQWHIIIC KFCAQHVGWE FKAVDPNLAP KVFFGLAGSS VRIGKTSERT PTQGNPFVVR
NLLHLVFREI E
