DCAF8_RAT
ID DCAF8_RAT Reviewed; 591 AA.
AC Q5U2M6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DDB1- and CUL4-associated factor 8;
DE AltName: Full=WD repeat-containing protein 42A;
GN Name=Dcaf8; Synonyms=Wdr42a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-22; SER-99; SER-123
RP AND SER-124, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DDB1, CUL4A and CUL4B. Interacts with KPNA1,
CC KPNB1 and XPO1. {ECO:0000250, ECO:0000250|UniProtKB:Q5TAQ9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TAQ9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5TAQ9}. Note=It shuttles between the nucleus
CC and the cytoplasm. Nuclear import is mediated by KPNA1 and KPNB1 under
CC the regulation of nuclear GTPase RAN. Nuclear export to the cytoplasm
CC is XPO1 dependent. {ECO:0000250|UniProtKB:Q5TAQ9}.
CC -!- SIMILARITY: Belongs to the WD repeat DCAF8 family. {ECO:0000305}.
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DR EMBL; BC085957; AAH85957.1; -; mRNA.
DR RefSeq; NP_001014253.1; NM_001014231.1.
DR RefSeq; XP_006250359.1; XM_006250297.3.
DR RefSeq; XP_006250360.1; XM_006250298.2.
DR AlphaFoldDB; Q5U2M6; -.
DR SMR; Q5U2M6; -.
DR IntAct; Q5U2M6; 2.
DR STRING; 10116.ENSRNOP00000008944; -.
DR iPTMnet; Q5U2M6; -.
DR PhosphoSitePlus; Q5U2M6; -.
DR PaxDb; Q5U2M6; -.
DR PRIDE; Q5U2M6; -.
DR Ensembl; ENSRNOT00000101398; ENSRNOP00000095537; ENSRNOG00000006785.
DR GeneID; 364050; -.
DR KEGG; rno:364050; -.
DR UCSC; RGD:1308513; rat.
DR CTD; 50717; -.
DR RGD; 1308513; Dcaf8.
DR eggNOG; KOG1334; Eukaryota.
DR GeneTree; ENSGT00950000182900; -.
DR HOGENOM; CLU_012381_4_1_1; -.
DR InParanoid; Q5U2M6; -.
DR OMA; IFQTKIM; -.
DR OrthoDB; 1270484at2759; -.
DR PhylomeDB; Q5U2M6; -.
DR TreeFam; TF326071; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5U2M6; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000006785; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q5U2M6; baseline and differential.
DR Genevisible; Q5U2M6; RN.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15574; PTHR15574; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..591
FT /note="DDB1- and CUL4-associated factor 8"
FT /id="PRO_0000296960"
FT REPEAT 185..224
FT /note="WD 1"
FT REPEAT 228..269
FT /note="WD 2"
FT REPEAT 275..315
FT /note="WD 3"
FT REPEAT 323..363
FT /note="WD 4"
FT REPEAT 379..418
FT /note="WD 5"
FT REPEAT 426..466
FT /note="WD 6"
FT REPEAT 470..509
FT /note="WD 7"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..50
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q5TAQ9"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 198
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q5TAQ9"
SQ SEQUENCE 591 AA; 66156 MW; 47492CD82D820E60 CRC64;
MSSKRPSTDG RRDLANGSLS SSPEEMSGAE EGRETSSGIE VEASDLSLSL TGDDGGPNRT
STESRGTDTE SSGEEKDSDS MEDTGHYSIN DENRVHGHSD EEEEEEQPRH RVQRKRASRD
QDSSDDERAL EDWVSSETTA LPRPRWQALP ALRERELGSS ARFVYEACGA RVFVQRFRLQ
HGLEGHTGCV NTLHFNQRGT WLASGSDDLK VVVWDWVRRQ PVLDFESGHK SNVFQAKFLP
NSGDSTLAMC ARDGQVRVAE LSATQCCKNT KRVAQHKGAS HKLALEPDSP CTFLSAGEDA
VVFTIDLRQD RPASKLVVTK EKEKKVGLYT IYVNPANTHQ FAVGGRDQFV RIYDQRKIDE
NENNGVLKKF CPHHLVNSES KANITCLVYS HDGTELLASY NDEDIYLFNS SHSDGAQYIK
RYKGHRNNAT VKGVNFYGPK SEFVVSGSDC GHIFLWEKSS CQIIQFMEGD KGGVVNCLEP
HPHLPVLATS GLDHDVKIWA PTAEASTELT GLKDVIKKNK RERDEDSLHH TDLFDSHMLW
FLMHHLRQRR HHRRWREPGV GATDADSDES PSSSDTSDEE EGPDRVQCMP S
