DDX6_MOUSE
ID DDX6_MOUSE Reviewed; 483 AA.
AC P54823; O54979; Q3UFI3; Q8BW68;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX6 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE AltName: Full=ATP-dependent RNA helicase p54;
DE AltName: Full=DEAD box protein 6;
DE AltName: Full=Oncogene RCK homolog;
GN Name=Ddx6; Synonyms=Hlr2, Rck;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=8543178; DOI=10.1016/0378-1119(95)00559-5;
RA Seto M., Yamamoto K., Takahashi T., Ueda R.;
RT "Cloning and expression of a murine cDNA homologous to the human RCK/P54, a
RT lymphoma-linked chromosomal translocation junction gene on 11q23.";
RL Gene 166:293-296(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Oviduct, and Pancreas;
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].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 26-478, AND DEVELOPMENTAL STAGE.
RC STRAIN=CB6F1/J; TISSUE=Oocyte;
RX PubMed=9883581;
RX DOI=10.1002/(sici)1520-6408(1998)23:4<285::aid-dvg4>3.0.co;2-w;
RA Paynton B.V.;
RT "RNA-binding proteins in mouse oocytes and embryos: expression of genes
RT encoding Y box, DEAD box RNA helicase, and polyA binding proteins.";
RL Dev. Genet. 23:285-298(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [6]
RP INTERACTION WITH RC3H1.
RX PubMed=20639877; DOI=10.1038/ni.1902;
RA Glasmacher E., Hoefig K.P., Vogel K.U., Rath N., Du L., Wolf C.,
RA Kremmer E., Wang X., Heissmeyer V.;
RT "Roquin binds inducible costimulator mRNA and effectors of mRNA decay to
RT induce microRNA-independent post-transcriptional repression.";
RL Nat. Immunol. 11:725-733(2010).
RN [7]
RP FUNCTION.
RX PubMed=26098573; DOI=10.1038/ncb3189;
RA Hu G., McQuiston T., Bernard A., Park Y.D., Qiu J., Vural A., Zhang N.,
RA Waterman S.R., Blewett N.H., Myers T.G., Maraia R.J., Kehrl J.H., Uzel G.,
RA Klionsky D.J., Williamson P.R.;
RT "A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation
RT regulates autophagy.";
RL Nat. Cell Biol. 17:930-942(2015).
CC -!- FUNCTION: Essential for the formation of P-bodies, cytosolic membrane-
CC less ribonucleoprotein granules involved in RNA metabolism through the
CC coordinated storage of mRNAs encoding regulatory functions (By
CC similarity). Plays a role in P-bodies to coordinate the storage of
CC translationally inactive mRNAs in the cytoplasm and prevent their
CC degradation (By similarity). In the process of mRNA degradation, plays
CC a role in mRNA decapping (By similarity). Blocks autophagy in nutrient-
CC rich conditions by repressing the expression of ATG-related genes
CC through degradation of their transcripts (PubMed:26098573).
CC {ECO:0000250|UniProtKB:P26196, ECO:0000269|PubMed:26098573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P26196};
CC -!- SUBUNIT: Interacts with LSM14A, LSM14B, EIF4ENIF1/4E-T, PATL1, EDC3 and
CC EDC4 (By similarity). Forms a complex with DCP1A, DCP2, EDC3 and
CC EDC4/HEDLS (By similarity). Interacts with LIMD1, WTIP and AJUBA (By
CC similarity). Interacts with APOBEC3G in an RNA-dependent manner (By
CC similarity). Interacts with RC3H1 (PubMed:20639877). Interacts with
CC ATXN2L (By similarity). Interacts with MCRIP1 (By similarity).
CC Interacts with MCRIP2 (By similarity). Interacts with NUFIP2 (By
CC similarity). Interacts with TRIM71 (via NHL repeats) in an RNA-
CC dependent manner (By similarity). Interacts with GIGYF1 and GIGYF2 (By
CC similarity). {ECO:0000250|UniProtKB:P26196,
CC ECO:0000269|PubMed:20639877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P26196}.
CC Cytoplasm {ECO:0000250|UniProtKB:P26196}. Nucleus
CC {ECO:0000250|UniProtKB:P26196}. Note=Imported in the nucleus via
CC interaction with EIF4ENIF1/4E-T via a piggy-back mechanism. Upon
CC cellular stress, relocalizes to stress granules.
CC {ECO:0000250|UniProtKB:P26196}.
CC -!- DEVELOPMENTAL STAGE: Abundant expression in growing oocytes, levels
CC decline in primary and secondary oocytes, and degradation appears to be
CC complete by the mid-late two-cell stage. {ECO:0000269|PubMed:9883581}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P26196}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC subfamily. {ECO:0000305}.
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DR EMBL; D50494; BAA09088.1; -; mRNA.
DR EMBL; AK054144; BAC35670.1; -; mRNA.
DR EMBL; AK148483; BAE28578.1; -; mRNA.
DR EMBL; BC021452; AAH21452.1; -; mRNA.
DR EMBL; AF038995; AAB94769.1; -; mRNA.
DR CCDS; CCDS23116.1; -.
DR RefSeq; NP_001104296.1; NM_001110826.1.
DR RefSeq; NP_031867.1; NM_007841.4.
DR RefSeq; NP_851841.2; NM_181324.3.
DR RefSeq; XP_011240693.1; XM_011242391.2.
DR RefSeq; XP_011240694.1; XM_011242392.2.
DR RefSeq; XP_017168613.1; XM_017313124.1.
DR AlphaFoldDB; P54823; -.
DR SMR; P54823; -.
DR BioGRID; 199087; 45.
DR IntAct; P54823; 6.
DR MINT; P54823; -.
DR STRING; 10090.ENSMUSP00000128421; -.
DR iPTMnet; P54823; -.
DR PhosphoSitePlus; P54823; -.
DR SwissPalm; P54823; -.
DR EPD; P54823; -.
DR jPOST; P54823; -.
DR MaxQB; P54823; -.
DR PaxDb; P54823; -.
DR PeptideAtlas; P54823; -.
DR PRIDE; P54823; -.
DR ProteomicsDB; 279906; -.
DR Antibodypedia; 3315; 451 antibodies from 38 providers.
DR DNASU; 13209; -.
DR Ensembl; ENSMUST00000170489; ENSMUSP00000128421; ENSMUSG00000032097.
DR Ensembl; ENSMUST00000217034; ENSMUSP00000149620; ENSMUSG00000032097.
DR GeneID; 13209; -.
DR KEGG; mmu:13209; -.
DR UCSC; uc009pdy.2; mouse.
DR CTD; 1656; -.
DR MGI; MGI:104976; Ddx6.
DR VEuPathDB; HostDB:ENSMUSG00000032097; -.
DR eggNOG; KOG0326; Eukaryota.
DR GeneTree; ENSGT00900000141067; -.
DR HOGENOM; CLU_003041_30_0_1; -.
DR InParanoid; P54823; -.
DR OMA; VCADEAP; -.
DR OrthoDB; 583315at2759; -.
DR PhylomeDB; P54823; -.
DR TreeFam; TF300440; -.
DR BRENDA; 3.6.4.13; 3474.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR BioGRID-ORCS; 13209; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Ddx6; mouse.
DR PRO; PR:P54823; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P54823; protein.
DR Bgee; ENSMUSG00000032097; Expressed in aortic valve and 261 other tissues.
DR Genevisible; P54823; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0033391; C:chromatoid body; ISO:MGI.
DR GO; GO:0061830; C:concave side of sperm head; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001520; C:outer dense fiber; ISO:MGI.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0016442; C:RISC complex; ISO:MGI.
DR GO; GO:0097227; C:sperm annulus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0033962; P:P-body assembly; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR GO; GO:0019074; P:viral RNA genome packaging; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..483
FT /note="Probable ATP-dependent RNA helicase DDX6"
FT /id="PRO_0000054984"
FT DOMAIN 127..298
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 308..468
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..316
FT /note="Gyf binding"
FT /evidence="ECO:0000250|UniProtKB:P26196"
FT REGION 307..483
FT /note="RecA-like domain 2"
FT /evidence="ECO:0000250|UniProtKB:P26196"
FT MOTIF 96..124
FT /note="Q motif"
FT MOTIF 246..249
FT /note="DEAD box"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26196"
FT CONFLICT 38..42
FT /note="PQPQL -> TQQQM (in Ref. 4; AAB94769)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="G -> P (in Ref. 4; AAB94769)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="Q -> R (in Ref. 3; BAC35670)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Q -> E (in Ref. 3; BAC35670)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="R -> E (in Ref. 4; AAB94769)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="I -> M (in Ref. 3; BAC35670)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="I -> V (in Ref. 4; AAB94769)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> V (in Ref. 4; AAB94769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54192 MW; 9AD22D171F8BC14D CRC64;
MSTARTENPV IMGLSSQNGQ LRGPVKASAG PGGGGTQPQP QLNQLKNTST INNGTPQQAQ
SMAATIKPGD DWKKTLKLPP KDLRIKTSDV TSTKGNEFED YCLKRELLMG IFEMGWEKPS
PIQEESIPIA LSGRDILARA KNGTGKSGAY LIPLLERLDL KKDNIQAMVI VPTRELALQV
SQICIQVSKH MGGAKVMATT GGTNLRDDIM RLDDTVHVVI ATPGRILDLI KKGVAKVDHV
QMIVLDEADK LLSQDFVQIM EDIILTLPKN RQILLYSATF PLSVQKFMNS HLQKPYEINL
MEELTLKGVT QYYAYVTERQ KVHCLNTLFS RLQINQSIIF CNSSQRVELL AKKISQLGYS
CFYIHAKMRQ EHRNRVFHDF RNGLCRNLVC TDLFTRGIDI QAVNVVINFD FPKLAETYLH
RIGRSGRFGH LGLAINLITY DDRFNLKSIE EQLGTEIKPI PSNIDKSLYV AEYHSEPAED
EKP
