DCA15_XENLA
ID DCA15_XENLA Reviewed; 600 AA.
AC A2BDA5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=DDB1- and CUL4-associated factor 15 {ECO:0000250|UniProtKB:Q66K64};
GN Name=dcaf15 {ECO:0000250|UniProtKB:Q66K64};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate-recognition component of the DCX(DCAF15) complex, a
CC cullin-4-RING E3 ubiquitin-protein ligase complex that mediates
CC ubiquitination and degradation of target proteins. The DCX(DCAF15)
CC complex acts as a regulator of the natural killer (NK) cells effector
CC functions. {ECO:0000250|UniProtKB:Q66K64}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q66K64}.
CC -!- SUBUNIT: Component of the DCX(DCAF15) complex, also named CLR4(DCAF15)
CC complex. {ECO:0000250|UniProtKB:Q66K64}.
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DR EMBL; BC130142; AAI30143.1; -; mRNA.
DR RefSeq; NP_001091275.1; NM_001097806.1.
DR AlphaFoldDB; A2BDA5; -.
DR SMR; A2BDA5; -.
DR MaxQB; A2BDA5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0032814; P:regulation of natural killer cell activation; ISS:UniProtKB.
DR InterPro; IPR038914; DCAF15.
DR InterPro; IPR032734; DCAF15_WD40.
DR PANTHER; PTHR28541; PTHR28541; 1.
DR Pfam; PF14939; DCAF15_WD40; 1.
PE 2: Evidence at transcript level;
KW Immunity; Metal-binding; Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..600
FT /note="DDB1- and CUL4-associated factor 15"
FT /id="PRO_0000314487"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q66K64"
SQ SEQUENCE 600 AA; 66643 MW; EB45516DD355C7A8 CRC64;
MAPSSKSERN SGAGSAGGGP GGTGGKRAVG RRREHVLKQL ERVKISGQLS PRLFRKLPPR
VCVSLKNIVD EDFLYAGHIF LGFSKCGRYV LSYTSSSGDD DFSFYIYHLY WWEFNVHSKL
KLVRQVRLFQ DEEIYSDLYL TVCEWPSDAS KVIVFGFNTR SANGMLMNMM MMSDENHRDI
YISTVAVPPR GRCAACQDAS RAHPGDPSAQ CLRHGFMLHT KYQVVYPFPT FQPAFQLKKD
QVVLLNTSYS LVACAVSVHS AGDSSFCQIL YDHTALPPAP PSSPGPWSPE AAPAFPSLGV
EVVPAQPSGA PEPSPAIAKA KEFVADIFRR AKEAKGSPLE ETRLPSSLGP SSSRCRPSLE
PQAPSGEVVP RDSPPAAETT APEPGYINYT KLHYVLQSGE GTEPEDEFED DKISLPFVVT
DLRGRNLRPM RERTDMQGQY LTVEQLTLDF EYVINEVIRH DATWGHQFCS FSDYDIVILE
VCPETNQVLI NIGLLLLAFP APTEEGQLRP KTYHTSLKVA WDLNTGIFET VSVGDLTEVK
GQTSGSVWSS YRKSCVDMVM KWLVPESSGR YVNRMTNEAL HKGCSLKVLA DSERYTWIVL