DDX6_CAVPO
ID DDX6_CAVPO Reviewed; 472 AA.
AC Q9WTM2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX6;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P26196};
DE AltName: Full=DEAD box protein 6;
DE AltName: Full=Oncogene RCK homolog;
DE Flags: Fragment;
GN Name=DDX6; Synonyms=RCK;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Akao Y.;
RT "Cloning of guinea pig RCK gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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. Plays a
CC role in P-bodies to coordinate the storage of translationally inactive
CC mRNAs in the cytoplasm and prevent their degradation. In the process of
CC mRNA degradation, plays a role in mRNA decapping. Blocks autophagy in
CC nutrient-rich conditions by repressing the expression of ATG-related
CC genes through degradation of their transcripts.
CC {ECO:0000250|UniProtKB:P26196}.
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. Interacts with LIMD1, WTIP and AJUBA. Interacts with
CC APOBEC3G in an RNA-dependent manner (By similarity). Interacts with
CC RC3H1 (By similarity). Interacts with ATXN2L. Interacts with MCRIP1.
CC Interacts with MCRIP2. Interacts with NUFIP2. Interacts with TRIM71
CC (via NHL repeats) in an RNA-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P26196, ECO:0000250|UniProtKB:P54823}.
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 -!- 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; AB013609; BAA77391.1; -; mRNA.
DR RefSeq; NP_001166415.1; NM_001172944.1.
DR AlphaFoldDB; Q9WTM2; -.
DR SMR; Q9WTM2; -.
DR STRING; 10141.ENSCPOP00000009507; -.
DR GeneID; 100135517; -.
DR KEGG; cpoc:100135517; -.
DR CTD; 1656; -.
DR eggNOG; KOG0326; Eukaryota.
DR InParanoid; Q9WTM2; -.
DR OrthoDB; 583315at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN <1..472
FT /note="Probable ATP-dependent RNA helicase DDX6"
FT /id="PRO_0000274531"
FT DOMAIN 116..287
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 297..457
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 85..113
FT /note="Q motif"
FT MOTIF 235..238
FT /note="DEAD box"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26196"
FT NON_TER 1
SQ SEQUENCE 472 AA; 53214 MW; 9D12897E50A8DB8D CRC64;
MGLSSQNGQL RGPVKPSGGP GGGGTQTQQQ MNQLKNTNTI NNGTQQQAQS MTTTIKPGDD
WKKTLKLPPK DLRIKTSDVT STKGNEFEDY CLKRELLMGI FEMGWEKPSP IQEESIPIAL
TGRDILARAK NGTGKSGAYL IPLLERLDLK KDNIQAMVIV PTRELALQVS QICIQVSKHM
GGAKVMATTG GTNLRDDIMR LDDTVHVVIA TPGRILDLIK KGVAKVDHVQ MIVLDEADKL
LSQDFVQIME DIILTLPKNR QILLYSATFP LSVQKFMNSH LQKPYEINLM EELTLKGVTQ
YYAYVTERQK VHCLNTLFPR LQTNQSIIFC NSSQRVELLA KKISQLGYSC FYIHAKMRQE
HRNRVFHDFR NGLCRNLVCT DLFTRGIDIQ AVNVVINFDF PKLAETYLHR IGRSGRFGHL
GLAINLITYD DRFNLKSIEE QLGTEIKPIP SNIDKSLYVA EYHSEPVEDE KP
