DCAF6_MOUSE
ID DCAF6_MOUSE Reviewed; 876 AA.
AC Q9DC22; Q8BK50;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DDB1- and CUL4-associated factor 6;
DE AltName: Full=IQ motif and WD repeat-containing protein 1;
DE AltName: Full=Nuclear receptor interaction protein;
DE Short=NRIP;
GN Name=Dcaf6; Synonyms=Iqwd1;
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].
RC STRAIN=C57BL/6J; TISSUE=Lung, Ovary, and Uterus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; THR-670; SER-673;
RP SER-863 AND SER-866, 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: Ligand-dependent coactivator of nuclear receptors. Enhance
CC transcriptional activity of the nuclear receptors NR3C1 and AR. May
CC function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein
CC ligase complex (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the nuclear receptors NR3C1 and AR in the
CC presence of ligand. Interacts with DDB1, CUL4A and CUL4B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AK004618; BAB23414.1; -; mRNA.
DR EMBL; AK077238; BAC36701.1; -; mRNA.
DR CCDS; CCDS48424.1; -.
DR RefSeq; NP_083035.1; NM_028759.1.
DR AlphaFoldDB; Q9DC22; -.
DR SMR; Q9DC22; -.
DR BioGRID; 216497; 11.
DR IntAct; Q9DC22; 2.
DR STRING; 10090.ENSMUSP00000027856; -.
DR iPTMnet; Q9DC22; -.
DR PhosphoSitePlus; Q9DC22; -.
DR EPD; Q9DC22; -.
DR jPOST; Q9DC22; -.
DR MaxQB; Q9DC22; -.
DR PaxDb; Q9DC22; -.
DR PeptideAtlas; Q9DC22; -.
DR PRIDE; Q9DC22; -.
DR ProteomicsDB; 277960; -.
DR Antibodypedia; 34346; 154 antibodies from 26 providers.
DR Ensembl; ENSMUST00000027856; ENSMUSP00000027856; ENSMUSG00000026571.
DR GeneID; 74106; -.
DR KEGG; mmu:74106; -.
DR UCSC; uc007djb.2; mouse.
DR CTD; 55827; -.
DR MGI; MGI:1921356; Dcaf6.
DR VEuPathDB; HostDB:ENSMUSG00000026571; -.
DR eggNOG; KOG1310; Eukaryota.
DR eggNOG; KOG1334; Eukaryota.
DR GeneTree; ENSGT00950000182900; -.
DR HOGENOM; CLU_012381_0_1_1; -.
DR InParanoid; Q9DC22; -.
DR OMA; HIYSFDI; -.
DR OrthoDB; 1270484at2759; -.
DR PhylomeDB; Q9DC22; -.
DR TreeFam; TF326071; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 74106; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Dcaf6; mouse.
DR PRO; PR:Q9DC22; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9DC22; protein.
DR Bgee; ENSMUSG00000026571; Expressed in spermatocyte and 217 other tissues.
DR ExpressionAtlas; Q9DC22; baseline and differential.
DR Genevisible; Q9DC22; MM.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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; 2.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..876
FT /note="DDB1- and CUL4-associated factor 6"
FT /id="PRO_0000304402"
FT REPEAT 49..88
FT /note="WD 1"
FT REPEAT 92..133
FT /note="WD 2"
FT REPEAT 139..179
FT /note="WD 3"
FT REPEAT 189..229
FT /note="WD 4"
FT REPEAT 251..290
FT /note="WD 5"
FT DOMAIN 692..721
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REPEAT 734..772
FT /note="WD 6"
FT REPEAT 775..814
FT /note="WD 7"
FT REGION 288..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q58WW2"
FT MOD_RES 670
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 876 AA; 97588 MW; 6F7B1A3F8DFBB407 CRC64;
MARSGSCPHL LWDVRKRSLG LEDPSRLRSR YLGRREFIQR LKLEATLNVH DGCVNTICWN
DTGEYILSGS DDTKLVISNP YSRKVLTTIR SGHRANIFSA KFLPCTDDKQ IVSCSGDGVI
FYTNIEQDAE TNRQCQFTCH YGTTYEIMTV PNDPYTFLSC GEDGTVRWFD TRIKTSCTKE
DCKDDILINC RRAATSVAIC PPVPYYLAVG CSDSSVRIYD RRMLGTRATG NYAGRGTTGM
VARFIPSHLS NKSCRVTSLC YSEDGQEILV SYSSDYIYLF DPKDDTAREL KTPSAEERRE
ELRQPPVKRL RLRGDWSDTG PRARPESERE RDGEQSPNVS LMQRMSDMLS RWFEEASEVA
QSNRGRGRPR PRGGTNQPDV STLPTVPSSP NLEVCETAMD VDMPAALLQP STSSTDPVQA
QAATAAIESP RSSSLLSCPD SEPRQSVEAS GHHAHHQSDN SNERLSPKPG TGEPVLSLHY
STEGTTTSTI KLNFTDEWSS TASSSRGNGS HCKSEGQEEC LVPPSSVQPP EGDSETRAPE
ELSEKGTLPE NLTQNQIDTA QLDNFPAEPL DSNSGEKNNP SQDSPCGLPE EGTLSETDRE
TCEQASTESA TRHASTKPEL PSQTEAIEQA STESATRHTS ANPELPSQTE AIAPLAHEDP
SARDSALQDT DDSDDDPVLI PGARYRTGPG DRRSAVARIQ EFFRRRKERK EMEELDTLNI
RRPLVKMVYK GHRNSRTMIK EANFWGANFV MSGSDCGHIF IWDRHTAEHL MLLEADNHVV
NCLQPHPFDP ILASSGIDYD IKIWSPLEES RIFNRKLADE VITRNELMLE ETRNTITVPA
SFMLRMLASL NHIRADRLEG DRSEGSGQEN ENEDEE
