I4A3B_XENLA
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 03-AUG-2022, entry version 105.
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; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Blastula;
RX PubMed=9334272; DOI=10.1242/dev.124.21.4235;
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 splicing as
CC component of the spliceosome. Core component of the splicing-dependent
CC multiprotein exon junction complex (EJC) deposited at splice junctions
CC on mRNAs. The EJC is a dynamic structure consisting of core proteins
CC and several peripheral nuclear and cytoplasmic associated factors that
CC join the complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC junction in the mature mRNA for the gene expression machinery and the
CC core components remain bound to spliced mRNAs throughout all stages of
CC mRNA metabolism thereby influencing downstream processes including
CC nuclear mRNA export, subcellular mRNA localization, translation
CC efficiency and nonsense-mediated mRNA decay (NMD). Binds spliced mRNA
CC in sequence-independent manner, 20-24 nucleotides upstream of mRNA
CC exon-exon junctions (By similarity). Involved in craniofacial
CC development (By similarity). When overexpressed, induces epidermis in
CC dissociated cells that would otherwise adopt a neural fate, a process
CC that requires an active 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}. Nucleus
CC 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 complex
CC (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 region
CC fated to give rise to epidermis and a site of active BMP signaling.
CC {ECO:0000269|PubMed:9334272}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AF020432; AAB71410.1; -; mRNA.
DR RefSeq; NP_001084200.1; NM_001090731.1.
DR AlphaFoldDB; O42226; -.
DR SMR; O42226; -.
DR BioGRID; 100687; 1.
DR GeneID; 399362; -.
DR KEGG; xla:399362; -.
DR CTD; 399362; -.
DR OrthoDB; 726081at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 399362; Expressed in blastula and 19 other tissues.
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: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: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 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; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Spliceosome;
KW Translation regulation; Transport.
FT CHAIN 1..414
FT /note="Eukaryotic initiation factor 4A-III-B"
FT /id="PRO_0000378561"
FT DOMAIN 72..242
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 253..414
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 41..69
FT /note="Q motif"
FT MOTIF 190..193
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 88..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 370..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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
