DDX6_PONAB
ID DDX6_PONAB Reviewed; 483 AA.
AC Q5RFQ5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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;
GN Name=DDX6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}.
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; CR857097; CAH89402.1; -; mRNA.
DR RefSeq; NP_001128971.1; NM_001135499.1.
DR AlphaFoldDB; Q5RFQ5; -.
DR SMR; Q5RFQ5; -.
DR STRING; 9601.ENSPPYP00000004516; -.
DR GeneID; 100190811; -.
DR KEGG; pon:100190811; -.
DR CTD; 1656; -.
DR eggNOG; KOG0326; Eukaryota.
DR InParanoid; Q5RFQ5; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; 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; Proto-oncogene; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..483
FT /note="Probable ATP-dependent RNA helicase DDX6"
FT /id="PRO_0000274532"
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..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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"
SQ SEQUENCE 483 AA; 54260 MW; F9CFDA879387393E CRC64;
MSTARTENPV IMGLSSQNGQ LRGPVKPTGG PGGGGTQTQQ QMNQLKNTNT INNGTQQQAQ
SMTTTIKPGD DWKKTLKLPP KDLRIKTSDV TSTKGNEFED YCLKRELLMG IFEMGWEKPS
PIQEESIPIA LSGRDILARA KNGTGKSGAY LIPLLERLDL KKDNIQAMVI VPTRELALQV
SQICIQVSKH MGGAKVMATT GGTNLRGDIM RLDDTVHVVI ATPGRILDLI KKGVAKVDHV
QMIVLDEADK LLSQDFVQIM EDIILTLPKN RQILLYSATF PLSVQKFMNS HLQKPYEINL
MEELTLKGVT QYYAYVTERQ KVHCLNTLFS RLQINQSIIF CNSSQRVELL AKKISQLGYS
CFYIHAKMRQ EHRNRVFHDF RNGLCRNLVC TDLFTRGIDI QAVNVVINFD FPKLAETYLH
RIGGSGRFGH LGLAINLITY DDRFNLKSIE EQLGTEIKPI PSNIDKSLYV AEYHSEPVED
EKP
