ID   DCA15_BOVIN             Reviewed;         600 AA.
AC   Q3SZD5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DDB1- and CUL4-associated factor 15 {ECO:0000250|UniProtKB:Q66K64};
GN   Name=DCAF15 {ECO:0000250|UniProtKB:Q66K64};
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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, possibly by mediating ubiquitination and degradation of
CC       cohesin subunits SMC1A and SMC3. May play a role in the activation of
CC       antigen-presenting cells (APC) and their interaction with NK cells.
CC       {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, composed of DCAF15, DDB1, cullin-4 (CUL4A or CUL4B), DDA1 and
CC       RBX1. {ECO:0000250|UniProtKB:Q66K64}.
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DR   EMBL; BC102945; AAI02946.1; -; mRNA.
DR   RefSeq; NP_001029857.1; NM_001034685.2.
DR   AlphaFoldDB; Q3SZD5; -.
DR   SMR; Q3SZD5; -.
DR   STRING; 9913.ENSBTAP00000011642; -.
DR   PaxDb; Q3SZD5; -.
DR   PRIDE; Q3SZD5; -.
DR   Ensembl; ENSBTAT00000011642; ENSBTAP00000011642; ENSBTAG00000008841.
DR   GeneID; 539970; -.
DR   KEGG; bta:539970; -.
DR   CTD; 90379; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008841; -.
DR   VGNC; VGNC:27902; DCAF15.
DR   eggNOG; ENOG502QQCQ; Eukaryota.
DR   GeneTree; ENSGT00390000011987; -.
DR   HOGENOM; CLU_031970_0_0_1; -.
DR   InParanoid; Q3SZD5; -.
DR   OMA; QILYTKG; -.
DR   OrthoDB; 471103at2759; -.
DR   TreeFam; TF329680; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000008841; Expressed in parenchyma of mammary gland and 105 other tissues.
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:0036094; F:small molecule binding; IEA:Ensembl.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; Phosphoprotein; Reference proteome;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..600
FT                   /note="DDB1- and CUL4-associated factor 15"
FT                   /id="PRO_0000314484"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..314
FT                   /note="Pro 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"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66K64"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66K64"
SQ   SEQUENCE   600 AA;  66269 MW;  E21F35BC45267E5D CRC64;
     MAPSSKSERN SGAGSGGGGP GGAGGKRAAG RRREHVLKQL ERVKISGQLS PRLFRKLPPR
     VCVSLKNIVD EDFLYAGHIF LGFSKCGRYV LSYTSSSGDD DFSFYIYHLY WWEFNVHSKL
     KLVRQVRLFQ DEEIYSDLYL TVCEWPSDAS KVIVFGFNTR SANGMLMNMM VMSDENHRDI
     YISTVAVPPP GRCAACRDAS RAHPGDPSAQ CLRHGFMLHT KYQVVYPFPT FQPAFQLKKD
     QVVLLNTSYS LVACAVSVHS AGDSSFCQIL YDHTTYPPAP PSPPGPQSPE LPPVLPSLCP
     EAAPAWPSGP PDPSPAIAKA KEFVADIFRR AKEAKGGTSE EVRPPPCPGP SGSRCRLPSE
     PLGPGGEAVP RDSPPAAEAP APEPGYVNYT KLYYVLGSGE GTEPEDEFED DKISLPFVVT
     DLRGRNLRPM REQAVVQGQY LTVEQLTLDF EYVINEVIRH DATWGHQFCS FSDYDIVILE
     VCPETNQVLI NIGLLLLAFP SPTEEGQLRP KTYHTSLKVA WDLNTGIFVT VSVGDLTEVK
     GQTSGSVWSS YRKSCVDMVM KWLVPESSGR YVNRMTNEAL HKGCSLKVLA DSERYTWIVL