DCAF8_MOUSE
ID DCAF8_MOUSE Reviewed; 591 AA.
AC Q8N7N5; Q8CII7; Q8CIK6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=DDB1- and CUL4-associated factor 8;
DE AltName: Full=WD repeat-containing protein 42A;
GN Name=Dcaf8; Synonyms=D1Ucla4, H326, Wdr42a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Oshima A., Takahashi-Fujii A., Tanase T., Imose N., Takeuchi K., Arita M.,
RA Musashino K., Yuuki H., Hara H., Sugiyama T., Irie R., Otsuki T., Sato H.,
RA Ota T., Wakamatsu A., Ishii S., Yamamoto J., Isono Y., Kawai-Hio Y.,
RA Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K., Nakamura Y.,
RA Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., Kanehori K.,
RA Sugiyama A., Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y.,
RA Nagai K., Isogai T.;
RT "NEDO cDNA sequencing project.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11401431; DOI=10.1006/geno.2000.6463;
RA Doudney K., Murdoch J.N., Paternotte C., Bentley L., Gregory S., Copp A.J.,
RA Stanier P.;
RT "Comparative physical and transcript maps of approximately 1 Mb around
RT loop-tail, a gene for severe neural tube defects on distal mouse chromosome
RT 1 and human chromosome 1q22-q23.";
RL Genomics 72:180-192(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-23; SER-100; SER-123
RP AND SER-124, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N7N5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N7N5-2; Sequence=VSP_027266, VSP_027267;
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:11401431}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the brain at 8.5 dpc, 9.5 dpc and
CC 10.5 dpc. {ECO:0000269|PubMed:11401431}.
CC -!- MISCELLANEOUS: The homozygous loop-tail (Lp) mouse has a severe neural
CC tube closure defect, analogous to the craniorachischisis phenotype seen
CC in humans. This gene has been mapped to The Lp critical region.
CC -!- SIMILARITY: Belongs to the WD repeat DCAF8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK098114; BAC05237.1; -; mRNA.
DR EMBL; AK146825; BAE27462.1; -; mRNA.
DR EMBL; BC023704; AAH23704.1; ALT_INIT; mRNA.
DR EMBL; BC023804; AAH23804.1; -; mRNA.
DR CCDS; CCDS15509.1; -. [Q8N7N5-1]
DR RefSeq; NP_705783.1; NM_153555.2. [Q8N7N5-1]
DR RefSeq; XP_006497128.1; XM_006497065.3.
DR RefSeq; XP_011237191.1; XM_011238889.2. [Q8N7N5-1]
DR AlphaFoldDB; Q8N7N5; -.
DR SMR; Q8N7N5; -.
DR BioGRID; 221007; 4.
DR IntAct; Q8N7N5; 6.
DR MINT; Q8N7N5; -.
DR STRING; 10090.ENSMUSP00000073778; -.
DR iPTMnet; Q8N7N5; -.
DR PhosphoSitePlus; Q8N7N5; -.
DR EPD; Q8N7N5; -.
DR jPOST; Q8N7N5; -.
DR MaxQB; Q8N7N5; -.
DR PaxDb; Q8N7N5; -.
DR PeptideAtlas; Q8N7N5; -.
DR PRIDE; Q8N7N5; -.
DR ProteomicsDB; 277961; -. [Q8N7N5-1]
DR ProteomicsDB; 277962; -. [Q8N7N5-2]
DR Antibodypedia; 20487; 89 antibodies from 17 providers.
DR Ensembl; ENSMUST00000074144; ENSMUSP00000073778; ENSMUSG00000026554. [Q8N7N5-1]
DR Ensembl; ENSMUST00000191689; ENSMUSP00000141731; ENSMUSG00000026554. [Q8N7N5-1]
DR Ensembl; ENSMUST00000192704; ENSMUSP00000141732; ENSMUSG00000026554. [Q8N7N5-1]
DR Ensembl; ENSMUST00000193638; ENSMUSP00000141836; ENSMUSG00000026554. [Q8N7N5-2]
DR GeneID; 98193; -.
DR KEGG; mmu:98193; -.
DR UCSC; uc007dpr.2; mouse. [Q8N7N5-2]
DR UCSC; uc007dps.2; mouse. [Q8N7N5-1]
DR CTD; 50717; -.
DR MGI; MGI:91860; Dcaf8.
DR VEuPathDB; HostDB:ENSMUSG00000026554; -.
DR eggNOG; KOG1334; Eukaryota.
DR GeneTree; ENSGT00950000182900; -.
DR HOGENOM; CLU_012381_4_1_1; -.
DR InParanoid; Q8N7N5; -.
DR OMA; IFQTKIM; -.
DR OrthoDB; 1270484at2759; -.
DR PhylomeDB; Q8N7N5; -.
DR TreeFam; TF326071; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 98193; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dcaf8; mouse.
DR PRO; PR:Q8N7N5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8N7N5; protein.
DR Bgee; ENSMUSG00000026554; Expressed in retinal neural layer and 258 other tissues.
DR ExpressionAtlas; Q8N7N5; baseline and differential.
DR Genevisible; Q8N7N5; MM.
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; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 Alternative splicing; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..591
FT /note="DDB1- and CUL4-associated factor 8"
FT /id="PRO_0000296958"
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 40..51
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q5TAQ9"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 198
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q5TAQ9"
FT VAR_SEQ 376..411
FT /note="VNSESKANITCLVYSHDGTELLASYNDEDIYLFNSS -> SSWPVTMMKTFT
FT FSTLLTVMGPSILRDTKAIEIMLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027266"
FT VAR_SEQ 412..591
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027267"
SQ SEQUENCE 591 AA; 66031 MW; 2FFC175E1E2D1F4A CRC64;
MSNKRPNTTD GRTDLANGSL SSSPEEMSGA EEGRETSSGI EVEASDLSLS LTGDDGGPNR
TSTESRGTDT ESSGEEKDSD SMEDTGHYSI NDESRGHGHS DEEDEEQPRH RGQRKRASRD
QDSSDDERAL EDWVSSETTA LPRPRWQALP ALRERELGSS ARFVYEACGA RVFVQRFRLQ
HGLEGHTGCV NTLHFNQRGT WLASGSDDLK VVVWDWVRRQ PVLDFESGHK SNVFQAKFLP
NSGDSTLAMC ARDGQVRVAE LSATQCCKNT KRVAQHKGAS HKLALEPDSP CTFLSAGEDA
VVFTIDLRQD RPASKLVVTK EKEKKVGLYT IYVNPANTHQ FAVGGRDQYV RIYDQRKIDE
NENNGVLKKF CPHHLVNSES KANITCLVYS HDGTELLASY NDEDIYLFNS SHSDGAQYIK
RYKGHRNNAT VKGVNFYGPK SEFVVSGSDC GHIFLWEKSS CQIIQFMEGD KGGVVNCLEP
HPHLPVLATS GLDHDVKIWA PTAEASTELT GLKEVIKKNK RERDEDSLHH TDLFDSHMLW
FLMHHLRQRR HHRRWREPGV GATDADSDES PSSSDTSDEE EGPDRVQCMP S
