CRBN_XENTR
ID CRBN_XENTR Reviewed; 447 AA.
AC Q640S2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein cereblon;
GN Name=crbn;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) 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 (Probable).
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 {ECO:0000250|UniProtKB:Q96SW2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96SW2}. Nucleus
CC {ECO:0000250|UniProtKB:Q96SW2}.
CC -!- SIMILARITY: Belongs to the CRBN family. {ECO:0000305}.
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DR EMBL; BC082517; AAH82517.1; -; mRNA.
DR RefSeq; NP_001008192.1; NM_001008191.1.
DR AlphaFoldDB; Q640S2; -.
DR SMR; Q640S2; -.
DR STRING; 8364.ENSXETP00000011183; -.
DR PaxDb; Q640S2; -.
DR DNASU; 493554; -.
DR Ensembl; ENSXETT00000011183; ENSXETP00000011183; ENSXETG00000005146.
DR GeneID; 493554; -.
DR KEGG; xtr:493554; -.
DR CTD; 51185; -.
DR Xenbase; XB-GENE-973907; crbn.
DR eggNOG; KOG1400; Eukaryota.
DR HOGENOM; CLU_025648_1_1_1; -.
DR InParanoid; Q640S2; -.
DR OMA; CQVYERG; -.
DR OrthoDB; 1069900at2759; -.
DR PhylomeDB; Q640S2; -.
DR TreeFam; TF106115; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000005146; Expressed in skeletal muscle tissue and 13 other tissues.
DR ExpressionAtlas; Q640S2; baseline.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding; Nucleus; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..447
FT /note="Protein cereblon"
FT /id="PRO_0000076164"
FT DOMAIN 82..320
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 321..429
FT /note="CULT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01124"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 383
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 389
FT /ligand="(S)-thalidomide"
FT /ligand_id="ChEBI:CHEBI:61918"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96SW2"
SQ SEQUENCE 447 AA; 50667 MW; FA2E651B2C8B04B3 CRC64;
MADDEGEEDP GINNMGNLLQ VISSESEEED EMELEDAKTA DSESPNIINF DTSLPTSHAY
LGVDMEEFHG RTLHDDDSCQ QIPVLPHVQV MLIPGQTLPL HLSRPQEVSM VRGLIQRDRT
FAVLAYSDGL QREAHFGTTA EIYAYREEHE FGIETVKVKA IGRQRFQVLE TRTQADGIQV
ARVQILPERV LPCPMTSLQL DSQSRHLLFP TNKPVSGRSP QSKCQWLHKY RRRKFLGASL
TSWPSWLYAL YDADSLMERV KLQLHEWDEN LRDDSLPANP IDFSYRVAAC LPIDDALRIQ
LLQIGNAIQR LRCELDIMSK CTSLCCKHCP DTEITTKNEI FSLSLCGPMA AYVNPHGYVH
ETLTVYKAFN LSLVGRPSTE NSWFPGFAWT IAQCRVCGSH MGWKFTAVRK DLSPQKFWGL
TRSALQPRIP EPDEGEMGHD HSPILCL
