ID   DDX6_XENLA              Reviewed;         481 AA.
AC   P54824; B7ZRN4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=ATP-dependent RNA helicase ddx6;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P26196};
DE   AltName: Full=ATP-dependent RNA helicase p54;
DE            Short=P54H;
DE            Short=Xp54;
DE   AltName: Full=DEAD box protein 6;
GN   Name=ddx6; Synonyms=p54h;
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], PROTEIN SEQUENCE OF 114-122 AND 368-377,
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A RIBONUCLEOPROTEIN
RP   COMPLEX WITH YBX2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Oocyte;
RX   PubMed=9023105; DOI=10.1093/nar/25.5.965;
RA   Ladomery M.R., Wade E., Sommerville J.;
RT   "Xp54, the Xenopus homologue of human RNA helicase p54, is an integral
RT   component of stored mRNP particles in oocytes.";
RL   Nucleic Acids Res. 25:965-973(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH LSM14A; YBX2 AND
RP   EIF4ENIF1, AND INTERACTION WITH LSM14A.
RX   PubMed=17074753; DOI=10.1074/jbc.m609059200;
RA   Tanaka K.J., Ogawa K., Takagi M., Imamoto N., Matsumoto K., Tsujimoto M.;
RT   "RAP55, a cytoplasmic mRNP component, represses translation in Xenopus
RT   oocytes.";
RL   J. Biol. Chem. 281:40096-40106(2006).
RN   [4]
RP   IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH CPEB1; PAT1; LSM14B;
RP   EIF4ENIF1; EIF4E1B AND YBX2, AND DEVELOPMENTAL STAGE.
RX   PubMed=17942399; DOI=10.1074/jbc.m704629200;
RA   Minshall N., Reiter M.H., Weil D., Standart N.;
RT   "CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus
RT   oocytes.";
RL   J. Biol. Chem. 282:37389-37401(2007).
RN   [5]
RP   IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH ELAVL1; ELAVL2; IGF2BP3;
RP   STAU1; LSM14B AND YBX2.
RX   PubMed=19458392; DOI=10.1074/jbc.m109.009928;
RA   Arthur P.K., Claussen M., Koch S., Tarbashevich K., Jahn O., Pieler T.;
RT   "Participation of Xenopus Elr-type proteins in vegetal mRNA localization
RT   during oogenesis.";
RL   J. Biol. Chem. 284:19982-19992(2009).
CC   -!- FUNCTION: ATP-dependent RNA helicase that is an integral component of
CC       messenger ribonucleoprotein complexes (mRNPs), storage particles that
CC       mask maternal mRNAs from the translational apparatus during oocyte
CC       maturation. {ECO:0000269|PubMed:9023105}.
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: Component of a ribonucleoprotein (RNP) complex, composed at
CC       least of cpeb1, lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100,
CC       eif4enif1/4E-T and eif4e1b. Component of a ribonucleoprotein (RNP)
CC       complex, composed at least of elavl1/elrA and/or elavl2/elrB,
CC       igf2bp3/vg1RBP, ddx6/Xp54, ybx2/frgy2, lsm14b/rap55b and, in a subset
CC       of RNP complexes, stau1/staufen. Component of a ribonucleoprotein (RNP)
CC       complex, composed at least of lsm14a/rap55a, ybx2/frgy2, ddx6/Xp54 and
CC       eif4enif1/4E-T. Interacts with lsm14a/rap55a.
CC       {ECO:0000269|PubMed:17074753, ECO:0000269|PubMed:17942399,
CC       ECO:0000269|PubMed:19458392, ECO:0000269|PubMed:9023105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P26196}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P26196}. Nucleus
CC       {ECO:0000250|UniProtKB:P26196}. Note=Mostly cytoplasmic. Upon cellular
CC       stress, relocalizes to stress granules. {ECO:0000250|UniProtKB:P26196}.
CC   -!- TISSUE SPECIFICITY: In adults, expression is restricted to the germline
CC       cells of the ovary. {ECO:0000269|PubMed:9023105}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally. Expression peaks at stage I
CC       of oogenesis and remains fairly constant through to the end of
CC       oogenesis and, after fertilization, up to blastula. From blastula,
CC       through gastrula and neurula, expression declines significantly. May
CC       also be expressed zygotically since a low level of expression is
CC       detected up to the free-feeding tadpole stage (embryonic stage 42) (at
CC       protein level). {ECO:0000269|PubMed:17942399,
CC       ECO:0000269|PubMed:9023105}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X92421; CAA63149.1; -; mRNA.
DR   EMBL; BC170228; AAI70228.1; -; mRNA.
DR   EMBL; BC170230; AAI70230.1; -; mRNA.
DR   RefSeq; NP_001083721.1; NM_001090252.1.
DR   RefSeq; XP_018079874.1; XM_018224385.1.
DR   RefSeq; XP_018079875.1; XM_018224386.1.
DR   RefSeq; XP_018079876.1; XM_018224387.1.
DR   RefSeq; XP_018079877.1; XM_018224388.1.
DR   RefSeq; XP_018079879.1; XM_018224390.1.
DR   AlphaFoldDB; P54824; -.
DR   SMR; P54824; -.
DR   BioGRID; 100406; 2.
DR   IntAct; P54824; 3.
DR   GeneID; 399080; -.
DR   KEGG; xla:399080; -.
DR   CTD; 399080; -.
DR   Xenbase; XB-GENE-922237; ddx6.L.
DR   OMA; VCADEAP; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 399080; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IPI: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; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Developmental protein; Direct protein sequencing;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Ribonucleoprotein; RNA-binding.
FT   CHAIN           1..481
FT                   /note="ATP-dependent RNA helicase ddx6"
FT                   /id="PRO_0000054985"
FT   DOMAIN          126..297
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          307..467
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           95..123
FT                   /note="Q motif"
FT   MOTIF           245..248
FT                   /note="DEAD box"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        146
FT                   /note="S -> T (in Ref. 1; CAA63149)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   481 AA;  54074 MW;  3CB5516F707C7C3D CRC64;
     MSTARTENPV LMGMSSQNGQ LRGPLKPSAG PGGGGTQTQQ INQLKNASTI NSGSQQQAQS
     MSSIIKPGDD WKKTLKLPPK DLRIKTSDVT STKGNEFEDY CLKRELLMGI FEMGWEKPSP
     IQEESIPIAL SGRDILARAK NGTGKSGAYL IPLLERLDLK KDCIQAMVIV PTRELALQVS
     QICIQVSKHM GGAKVMATTG GTNLRDDIMR LDDTVHVVIA TPGRILDLIK KGVAKVDHIQ
     MIVLDEADKL LSQDFMQIME DIIMTLPKNR QILLYSATFP LSVQKFMTLH LQKPYEINLM
     EELTLKGVTQ YYAYVTERQK VHCLNTLFSR LQINQSIIFC NSSQRVELLA KKISQLGYSC
     FYIHAKMRQE HRNRVFHDFR NGLCRNLVCT DLFTRGIDIQ AVNVVINFDF PKLAETYLHR
     IGRSGRFGHL GLAINLITYD DRFNLKSIEE QLGTEIKPIP SSIDKNLYVA EYHSESGEDK
     P