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Database: UniProt
Entry: O42226
LinkDB: O42226
Original site: O42226 
ID   I4A3B_XENLA             Reviewed;         414 AA.
AC   O42226;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   31-JUL-2019, entry version 97.
DE   RecName: Full=Eukaryotic initiation factor 4A-III-B;
DE            Short=XeIF-4AIII;
DE            Short=eIF-4A-III-B;
DE            Short=eIF4A-III-B;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P38919};
DE   AltName: Full=ATP-dependent RNA helicase DDX48-B;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A-3-B;
DE   AltName: Full=DEAD box protein 48-B;
DE   AltName: Full=Eukaryotic translation initiation factor 4A isoform 3-B;
GN   Name=eif4a3-b; Synonyms=ddx48;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Blastula;
RX   PubMed=9334272;
RA   Weinstein D.C., Honore E., Hemmati-Brivanlou A.;
RT   "Epidermal induction and inhibition of neural fate by translation
RT   initiation factor 4AIII.";
RL   Development 124:4235-4242(1997).
CC   -!- FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA
CC       splicing as component of the spliceosome. Core component of the
CC       splicing-dependent multiprotein exon junction complex (EJC)
CC       deposited at splice junctions on mRNAs. The EJC is a dynamic
CC       structure consisting of core proteins and several peripheral
CC       nuclear and cytoplasmic associated factors that join the complex
CC       only transiently either during EJC assembly or during subsequent
CC       mRNA metabolism. The EJC marks the position of the exon-exon
CC       junction in the mature mRNA for the gene expression machinery and
CC       the core components remain bound to spliced mRNAs throughout all
CC       stages of mRNA metabolism thereby influencing downstream processes
CC       including nuclear mRNA export, subcellular mRNA localization,
CC       translation efficiency and nonsense-mediated mRNA decay (NMD).
CC       Binds spliced mRNA in sequence-independent manner, 20-24
CC       nucleotides upstream of mRNA exon-exon junctions (By similarity).
CC       Involved in craniofacial development (By similarity). When
CC       overexpressed, induces epidermis in dissociated cells that would
CC       otherwise adopt a neural fate, a process that requires an active
CC       BMP signaling pathway (PubMed:9334272).
CC       {ECO:0000250|UniProtKB:P38919, ECO:0000269|PubMed:9334272}.
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:P38919};
CC   -!- SUBUNIT: Identified in the spliceosome C complex. Part of the mRNA
CC       splicing-dependent exon junction complex (EJC) complex; the core
CC       complex contains casc3, eif4a3, magoh and rbm8a.
CC       {ECO:0000250|UniProtKB:P38919}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}.
CC       Nucleus speckle {ECO:0000250|UniProtKB:P38919}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling
CC       protein. Travels to the cytoplasm as part of the exon junction
CC       complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q3B8Q2}.
CC   -!- DEVELOPMENTAL STAGE: Expressed between blastula and neural plate
CC       stages. Detected in the ventral ectoderm of the gastrula, the
CC       region fated to give rise to epidermis and a site of active BMP
CC       signaling. {ECO:0000269|PubMed:9334272}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000305}.
DR   EMBL; AF020432; AAB71410.1; -; mRNA.
DR   RefSeq; NP_001084200.1; NM_001090731.1.
DR   SMR; O42226; -.
DR   PRIDE; O42226; -.
DR   GeneID; 399362; -.
DR   KEGG; xla:399362; -.
DR   CTD; 399362; -.
DR   Xenbase; XB-GENE-5773753; eif4a3.
DR   KO; K13025; -.
DR   OrthoDB; 726081at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; mRNA processing;
KW   mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay;
KW   Nucleotide-binding; Nucleus; RNA-binding; Spliceosome;
KW   Translation regulation; Transport.
FT   CHAIN         1    414       Eukaryotic initiation factor 4A-III-B.
FT                                /FTId=PRO_0000378561.
FT   DOMAIN       72    242       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      253    414       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      85     92       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   NP_BIND      88     93       ATP. {ECO:0000250|UniProtKB:P38919}.
FT   NP_BIND     370    374       ATP. {ECO:0000250|UniProtKB:P38919}.
FT   MOTIF        41     69       Q motif.
FT   MOTIF       190    193       DEAD box. {ECO:0000305}.
FT   BINDING      63     63       ATP; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   BINDING      68     68       ATP. {ECO:0000250|UniProtKB:P38919}.
FT   BINDING     345    345       ATP. {ECO:0000250|UniProtKB:P38919}.
SQ   SEQUENCE   414 AA;  47060 MW;  AF3270D5EF59A693 CRC64;
     MAAAAVAGVA GLTTAHAKRL LREEDMTTVE FQTSEEVDVT PTFDTMGLRE DLLRGIYAYG
     FEKPSAIQQK AIKQIIKGRD VIAQSQSGTG KTATFCVSVL QCLDIQIRET QALILAPTKE
     LARQIQKVLL ALGDYMNVQC HACIGGTNVG EDIRKLDYGQ HVVAGTPGRV FDMIRRRSLR
     TRAIKMLVLD EADEMLNKGF KEQIYDVYRY LPPATQVCLI SATLPHEILE MTNKFMTDPI
     RILVKRDELT LEGIKQFFVA VEREEWKFDT LCDLYDTLTI TQAVIFCNTK RKVDWLTEKM
     REANFTVSSM HGDMPQKERE SIMKEFRSGA SRVLISTDVW ARGLDVPQVS LIINYDLPNN
     RELYIHRIGR SGRYGRKGVA INFVKNDDIR ILRDIEQYYS TQIDEMPMNV ADLI
//
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