DCA12_BOVIN
ID DCA12_BOVIN Reviewed; 453 AA.
AC Q3MHH0; A6QR04;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DDB1- and CUL4-associated factor 12 {ECO:0000305};
DE AltName: Full=WD repeat-containing protein 40A;
GN Name=DCAF12; Synonyms=WDR40A;
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=Hereford; TISSUE=Fetal liver, and Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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, such as MAGEA3, MAGEA6 and CCT5, leading
CC to their ubiquitination and degradation. Ubiquitination of MAGEA3,
CC MAGEA6 by DCX(DCAF12) complex is required for starvation-induced
CC autophagy. {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; BC105241; AAI05242.1; -; mRNA.
DR EMBL; BC150062; AAI50063.1; -; mRNA.
DR RefSeq; NP_001161368.1; NM_001167896.1.
DR AlphaFoldDB; Q3MHH0; -.
DR SMR; Q3MHH0; -.
DR STRING; 9913.ENSBTAP00000028744; -.
DR PaxDb; Q3MHH0; -.
DR PRIDE; Q3MHH0; -.
DR Ensembl; ENSBTAT00000028744; ENSBTAP00000028744; ENSBTAG00000021573.
DR GeneID; 525161; -.
DR KEGG; bta:525161; -.
DR CTD; 25853; -.
DR VEuPathDB; HostDB:ENSBTAG00000021573; -.
DR VGNC; VGNC:27901; DCAF12.
DR eggNOG; ENOG502QR7U; Eukaryota.
DR GeneTree; ENSGT00940000158028; -.
DR HOGENOM; CLU_020124_1_0_1; -.
DR InParanoid; Q3MHH0; -.
DR OMA; FDMCWLD; -.
DR OrthoDB; 885170at2759; -.
DR TreeFam; TF323731; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000021573; Expressed in semen and 105 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
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: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..453
FT /note="DDB1- and CUL4-associated factor 12"
FT /id="PRO_0000306839"
FT REPEAT 138..178
FT /note="WD 1"
FT REPEAT 182..220
FT /note="WD 2"
FT REPEAT 250..289
FT /note="WD 3"
FT REPEAT 338..375
FT /note="WD 4"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="A -> S (in Ref. 1; AAI05242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50636 MW; D353DA656E655DE4 CRC64;
MARKAVSRKR KAPALPGAGS DAQDPQFGWD HSLHKRKRLP PVKRSLVYYL KNREVRLQNE
TSYSRVLHGY AAQQLPSLLK EREFHLGTLN KVFASQWLNH RQVVCGTKCN TLFVVDVQTS
QITKIPILKD REPGCVTQQG CGIHAIELNP SRTLLATGGD NPNSLAIYRL PTLDPVCVGD
DGHKDWIFSI AWISDTMAVS GSRDGSMGLW EVTDDVLTKS DARHNVSRVP VYSHITHKAL
KDIPKEDTNP DNCKVRALAF NNKNKELGAV SLDGYFHLWK TENTLSKLLS TKLPYCRENV
CLAYGNEWSV YAVGSQAHVS FLDPRQPSYN VKSVCSRERG SGIRSVSFYE HIITVGTGQG
SLLFYDIRAQ RFLEEKLSAC YGSKPKLAGE NLKLTTGKGW LNHDETWRNY FSDIDFFPNA
VYTHCYDSSG TKLFVAGGPL PSGLHGNYAG LWS