DDX3_XENLA
ID DDX3_XENLA Reviewed; 697 AA.
AC P24346;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Putative ATP-dependent RNA helicase an3;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O00571};
GN Name=an3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1996140; DOI=10.1038/349717a0;
RA Gururajan R., Perry-O'Keefe H., Melton D.A., Weeks D.L.;
RT "The Xenopus localized messenger RNA An3 may encode an ATP-dependent RNA
RT helicase.";
RL Nature 349:717-719(1991).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23413191; DOI=10.1126/science.1231499;
RA Cruciat C.M., Dolde C., de Groot R.E., Ohkawara B., Reinhard C.,
RA Korswagen H.C., Niehrs C.;
RT "RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-beta-
RT catenin signaling.";
RL Science 339:1436-1441(2013).
CC -!- FUNCTION: Multifunctional ATP-dependent RNA helicase. The ATPase
CC activity can be stimulated by various ribo-and deoxynucleic acids
CC indicative for a relaxed substrate specificity. In vitro can unwind
CC partially double-stranded DNA with a preference for 5'-single-stranded
CC DNA overhangs. Involved in many cellular processes, which do not
CC necessarily require its ATPase/helicase catalytic activities. Involved
CC in the regulation of transcription and translation initiation. Involved
CC in innate immunity (By similarity). Involved in both stress and
CC inflammatory responses (By similarity). May negatively regulate
CC extrinsic apoptotic signaling pathway via death domain receptors. May
CC be involved in mitotic chromosome segregation (By similarity). Required
CC for canonical Wnt signaling involved in anteroposterior neural
CC patterning (PubMed:23413191). {ECO:0000250|UniProtKB:O00571,
CC ECO:0000250|UniProtKB:Q62167, ECO:0000269|PubMed:23413191}.
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:O00571};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00571}.
CC Nucleus {ECO:0000250|UniProtKB:O00571}. Cytoplasm
CC {ECO:0000250|UniProtKB:O00571}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:O00571}. Inflammasome
CC {ECO:0000250|UniProtKB:Q62167}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O00571}. Note=Shuttles between the nucleus and
CC the cytosol. {ECO:0000250|UniProtKB:O00571}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed throughout embryogenesis. At
CC gastrula stage (st. 10.5), equal expression in ventral and dorsal
CC marginal zones. At neurula stage (st. 18), highest expression levels in
CC ectodermal cells. {ECO:0000269|PubMed:23413191}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC anteriorization of embryos, that exhibit enlarged heads and eyes,
CC shortened tails and defective melanocyte and eye pigmentation.
CC {ECO:0000269|PubMed:23413191}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; X57328; CAA40605.1; -; mRNA.
DR PIR; S13654; S13654.
DR RefSeq; NP_001095245.1; NM_001101775.1.
DR AlphaFoldDB; P24346; -.
DR SMR; P24346; -.
DR BioGRID; 99271; 1.
DR DIP; DIP-59067N; -.
DR IntAct; P24346; 1.
DR GeneID; 397935; -.
DR KEGG; xla:397935; -.
DR CTD; 397935; -.
DR Xenbase; XB-GENE-17330554; ddx3x.S.
DR OrthoDB; 595675at2759; -.
DR SABIO-RK; P24346; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 397935; Expressed in pancreas and 19 other tissues.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0061702; C:inflammasome complex; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; 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; Cell membrane; Cell projection; Cytoplasm; Helicase;
KW Hydrolase; Inflammasome; Membrane; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..697
FT /note="Putative ATP-dependent RNA helicase an3"
FT /id="PRO_0000055015"
FT DOMAIN 252..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 455..616
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 27..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..249
FT /note="Q motif"
FT MOTIF 388..391
FT /note="DEAD box"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 241..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 265..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 697 AA; 77303 MW; F3DD23EB60B2E2EF CRC64;
MSHVAVENVL NLDQQFAGLD LNSADAESGV AGTKGRYIPP HLRNKEASRN DSNWDSGRGG
NGYINGMQDD RDGRMNGYDR GGYGSRGTGR SDRGFYDREN SGWNSGRDKD AYSSFGSRGD
RGKGSLFNER GSGSRRTDDR RQDGFDGMGN RSDKSGFGRF DRGNSRWSDD RNDEDDWSKP
LAPNDRVEQE LFSGSNTGIN FEKYDDIPVE ATGSNCPPHI ESFHDVTMGE IIMGNIQLTR
YTRPTPVQKH AIPIIIEKRD LMACAQTGSG KTAAFLLPIL SQIYADGPGD AMKHLQENGR
YGRRKQFPLS LVLAPTRELA VQIYEEARKF AYRSRVRPCV VYGGADIGQQ IRDLERGCHL
LVATPGRLVD MMERGKIGLD FCKYLVLDEA DRMLDMGFEP QIRRIVEQDT MPPKGVRQTM
MFSATFPKEI QILARDFLDE YIFLAVGRVG STSENITQKV VWVEEMDKRS FLLDLLNATG
KDSLTLVFVE TKKGADALED FLYHEGYACT SIHGDRSQRD REEALHQFRS GKSPILVATA
VAARGLDISN VKHVINFDLP SDIEEYVHRI GRTGRVGNLG LATSFFNEKN INITKDLLDL
LVEAKQEVPS WLENMAYEQH HKSSSRGRSK SRFSGGFGAK DYRQSSGAGS SFGSSRGGRS
SGHGGSRGFG GGYGGFYNSD GYGGNYGGSS QVDWWGN
