ID   DDA1_BOVIN              Reviewed;         102 AA.
AC   Q5E9A9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=DET1- and DDB1-associated protein 1 {ECO:0000250|UniProtKB:Q9BW61};
GN   Name=DDA1 {ECO:0000250|UniProtKB:Q9BW61};
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a component of numerous distinct DCX (DDB1-CUL4-
CC       X-box) E3 ubiquitin-protein ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. In the DCX complexes, acts as a scaffolding subunit required
CC       to stabilize the complex. {ECO:0000250|UniProtKB:Q9BW61}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9BW61}.
CC   -!- SUBUNIT: Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC       protein ligase complexes which consist of a core of DDB1, cullin-4
CC       (CUL4A or CUL4B), DDA1 and RBX1. Component of the DCX(DCAF15) complex,
CC       also named CLR4(DCAF15) complex, composed of DCAF15, DDB1, cullin-4
CC       (CUL4A or CUL4B), DDA1 and RBX1. Part of the DDD core complex
CC       containing DET1, DDA1 and DDB1; the DDD core complex recruits a
CC       specific UBE2E enzyme, such as UBE2E1, UBE2E2 UBE2E3, to form specific
CC       DDD-E2 complexes. {ECO:0000250|UniProtKB:Q9BW61}.
CC   -!- SIMILARITY: Belongs to the DDA1 family. {ECO:0000305}.
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DR   EMBL; BT021011; AAX09028.1; -; mRNA.
DR   EMBL; BC120366; AAI20367.1; -; mRNA.
DR   RefSeq; NP_001015583.1; NM_001015583.1.
DR   AlphaFoldDB; Q5E9A9; -.
DR   SMR; Q5E9A9; -.
DR   STRING; 9913.ENSBTAP00000022696; -.
DR   PaxDb; Q5E9A9; -.
DR   PRIDE; Q5E9A9; -.
DR   Ensembl; ENSBTAT00000022696; ENSBTAP00000022696; ENSBTAG00000017068.
DR   GeneID; 512898; -.
DR   KEGG; bta:512898; -.
DR   CTD; 79016; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017068; -.
DR   eggNOG; KOG4816; Eukaryota.
DR   GeneTree; ENSGT00390000007029; -.
DR   HOGENOM; CLU_144562_1_0_1; -.
DR   InParanoid; Q5E9A9; -.
DR   OMA; MARTDSE; -.
DR   OrthoDB; 1521756at2759; -.
DR   TreeFam; TF323534; -.
DR   Reactome; R-BTA-8951664; Neddylation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000017068; Expressed in temporal cortex and 105 other tissues.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   InterPro; IPR033575; DDA1.
DR   InterPro; IPR018276; DDA1_N.
DR   PANTHER; PTHR31879; PTHR31879; 1.
DR   Pfam; PF10172; DDA1; 1.
PE   3: Inferred from homology;
KW   Acetylation; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
FT   CHAIN           2..102
FT                   /note="DET1- and DDB1-associated protein 1"
FT                   /id="PRO_0000310269"
FT   REGION          66..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW61"
SQ   SEQUENCE   102 AA;  11835 MW;  94E43C3528589F01 CRC64;
     MADFLKGLPV YNKSNFSRFH ADSVCKASNR RPSVYLPTRE YPSEQIIVTE KTNILLRYLH
     QQWDKKNAAK KRDQEQVELE GESSAPPRKV ARTDSPDMHE DT