ID   DC12B_XENLA             Reviewed;         442 AA.
AC   Q6AX81;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=DDB1- and CUL4-associated factor 12-B {ECO:0000305};
DE   AltName: Full=WD repeat-containing protein 40A-B;
GN   Name=dcaf12-b; Synonyms=wdr40a-b;
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=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3
CC       ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC       degrons) pathway, which recognizes a C-degron located at the extreme C
CC       terminus of target proteins, leading to their ubiquitination and
CC       degradation. The C-degron recognized by the DesCEND pathway is usually
CC       a motif of less than ten residues and can be present in full-length
CC       proteins, truncated proteins or proteolytically cleaved forms. The
CC       DCX(DCAF12) complex specifically recognizes proteins with a diglutamate
CC       (Glu-Glu) at the C-terminus, leading to their ubiquitination and
CC       degradation. {ECO:0000250|UniProtKB:Q5T6F0}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q5T6F0}.
CC   -!- SUBUNIT: Component of the DCX(DCAF12) E3 ubiquitin ligase complex, at
CC       least composed of cul4 (cul4a or cul4b), ddb1, dcaf12 and rbx1.
CC       {ECO:0000250|UniProtKB:Q5T6F0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T6F0}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q5T6F0}.
CC   -!- SIMILARITY: Belongs to the WD repeat DCAF12 family. {ECO:0000305}.
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DR   EMBL; BC079715; AAH79715.1; -; mRNA.
DR   RefSeq; NP_001087395.1; NM_001093926.1.
DR   AlphaFoldDB; Q6AX81; -.
DR   SMR; Q6AX81; -.
DR   DNASU; 447219; -.
DR   GeneID; 447219; -.
DR   KEGG; xla:447219; -.
DR   CTD; 447219; -.
DR   Xenbase; XB-GENE-6254146; dcaf12.S.
DR   OMA; FDMCWLD; -.
DR   OrthoDB; 885170at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 447219; Expressed in testis and 19 other tissues.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Reference proteome; Repeat;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..442
FT                   /note="DDB1- and CUL4-associated factor 12-B"
FT                   /id="PRO_0000306846"
FT   REPEAT          132..173
FT                   /note="WD 1"
FT   REPEAT          177..215
FT                   /note="WD 2"
FT   REPEAT          245..284
FT                   /note="WD 3"
FT   REPEAT          333..370
FT                   /note="WD 4"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  49325 MW;  F6A5E5A21FF79404 CRC64;
     MTRRPVSRKR RATHGTGPGE QSDWDHSAHK RKRLQPEKKS LVFYLKSREL KPHNDSTYLH
     LLRGHAACTL PGILSEREFH LGNLNKVFAS QWLNHRQVVC GTKCNTLFVV DIQTGQITKI
     PILKDREPIS GSHQSCGIHA IEINPSRTLL ATGGENPNSI AVYRLPTLDP VCVGDGGHND
     WIFSIAWISD TMAVSGSRDG FMALWEMTDE VVNKRDFQHG LSRVPVYSHI SHKALKDIPK
     ESSNPVNCKV RALAFNGNNK ELGAVSLDGF FHLWKAEQTL SKLLSTKLPF CRENVCLAYG
     LEWSLYAVGS QAHVSFLDPR EPPQCAKSVY CREQGSGIRS VSFYEHIVTV GTGQGALLFY
     DIRAQRFLED LTGSCREGDL LKLNTGKGWL NHNEMWMNYF SDIDSCPNAV YTHCYDSSGT
     KLFVAGGPLP TGLHGNYAGL WS