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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}.
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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
 
 
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