CRBN_BOVIN
ID CRBN_BOVIN Reviewed; 444 AA.
AC Q0P564;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein cereblon;
GN Name=CRBN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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, such as MEIS2 or ILF2.
CC Normal degradation of key regulatory proteins is required for normal
CC limb outgrowth and expression of the fibroblast growth factor FGF8.
CC Maintains presynaptic glutamate release and consequently cognitive
CC functions, such as memory and learning, by negatively regulating large-
CC conductance calcium-activated potassium (BK) channels in excitatory
CC neurons. Likely to function by regulating the assembly and neuronal
CC surface expression of BK channels via its interaction with KCNT1 (By
CC similarity). May also be involved in regulating anxiety-like behaviors
CC via a BK channel-independent mechanism (By similarity).
CC {ECO:0000250|UniProtKB:Q8C7D2, ECO:0000250|UniProtKB:Q96SW2,
CC ECO:0000305}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96SW2}.
CC -!- SUBUNIT: Component of a DCX (DDB1-CUL4-X-box) protein ligase complex,
CC at least composed of CRBN, CUL4A, DDB1 and RBX1. Interacts directly
CC with DDB1 (By similarity). Interacts with KCNT1 (By similarity).
CC Interacts with ILF2 (By similarity). {ECO:0000250|UniProtKB:Q56AP7,
CC ECO:0000250|UniProtKB:Q96SW2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96SW2}. Nucleus
CC {ECO:0000250|UniProtKB:Q96SW2}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- PTM: Ubiquitinated, ubiquitination is mediated by its own DCX protein
CC ligase complex. {ECO:0000250|UniProtKB:Q96SW2}.
CC -!- SIMILARITY: Belongs to the CRBN family. {ECO:0000305}.
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DR EMBL; BC120452; AAI20453.1; -; mRNA.
DR RefSeq; NP_001068995.1; NM_001075527.1.
DR AlphaFoldDB; Q0P564; -.
DR SMR; Q0P564; -.
DR IntAct; Q0P564; 1.
DR MINT; Q0P564; -.
DR STRING; 9913.ENSBTAP00000026031; -.
DR PaxDb; Q0P564; -.
DR PRIDE; Q0P564; -.
DR Ensembl; ENSBTAT00000026031; ENSBTAP00000026031; ENSBTAG00000019536.
DR GeneID; 511585; -.
DR KEGG; bta:511585; -.
DR CTD; 51185; -.
DR VEuPathDB; HostDB:ENSBTAG00000019536; -.
DR VGNC; VGNC:27690; CRBN.
DR eggNOG; KOG1400; Eukaryota.
DR GeneTree; ENSGT00390000016404; -.
DR HOGENOM; CLU_025648_1_1_1; -.
DR InParanoid; Q0P564; -.
DR OMA; AYQMYDS; -.
DR OrthoDB; 1069900at2759; -.
DR TreeFam; TF106115; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000019536; Expressed in semitendinosus and 107 other tissues.
DR ExpressionAtlas; Q0P564; baseline and differential.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:1902607; P:negative regulation of large conductance calcium-activated potassium channel activity; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
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; IPR015947; PUA-like_sf.
DR InterPro; IPR004910; Yippee/Mis18/Cereblon.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR Pfam; PF03226; Yippee-Mis18; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS51788; CULT; 1.
DR PROSITE; PS51787; LON_N; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Metal-binding; Nucleus; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc.
FT CHAIN 1..444
FT /note="Protein cereblon"
FT /id="PRO_0000393875"
FT DOMAIN 83..319
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 320..428
FT /note="CULT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 380
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 382
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 388
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
SQ SEQUENCE 444 AA; 50800 MW; FECA3FCB5A2EB978 CRC64;
MAGEGDPEDA AHNMGNHLPL LPAEEEEEDE IEMEVEDQDN KEPKKPNIIN FDTSLPTSHT
YLGSDMEEFH GRTLHDDDSC PVIPVLPQVV MTLIPGQTLP LQLFSPQEVS MVRNLIQKDR
TFAVLAYSNV QEREAQFGTT AEIYAYREEQ DFGIEVVKVK AIGRQRFKVL EIRTQSDGIQ
QAKVQILPEC VLPSTMSAVQ LESLNKCRIF PSKPVSWEDQ CSYKWWQKYQ KRKFHCANLT
SWPRWLYSLY DAETLMDRIK KQLREWDENL KEDSLPSNPI DFSYRVAACL PIDDVLRIQL
LKIGSAIQRL RCELDIMNKC TSLCCKQCQE TEITTKNEIF SLSLCGPMAA YVNPHGYVHE
TLTVYKASNL NLIGRPSTDH SWFPGYAWTI AQCRICASHI GWKFTATKKD MSPQKFWGLT
RSALLPTIPD TEDDISPDKV ILCL
