IF4E_XENLA
ID IF4E_XENLA Reviewed; 213 AA.
AC P48597;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Eukaryotic translation initiation factor 4E;
DE Short=eIF-4E;
DE Short=eIF4E;
DE AltName: Full=eIF-4F 25 kDa subunit;
DE AltName: Full=mRNA cap-binding protein;
GN Name=eif4e;
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], AND DEVELOPMENTAL STAGE.
RX PubMed=7875328; DOI=10.1016/0014-5793(95)00081-j;
RA Wakiyama M., Saigoh M., Shiokawa K., Miura K.I.;
RT "mRNA encoding the translation initiation factor eIF-4E is expressed early
RT in Xenopus embryogenesis.";
RL FEBS Lett. 360:191-193(1995).
RN [2]
RP FUNCTION, INTERACTION WITH TACC3, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10635326; DOI=10.1016/s1097-2765(00)80230-0;
RA Stebbins-Boaz B., Cao Q., de Moor C.H., Mendez R., Richter J.D.;
RT "Maskin is a CPEB-associated factor that transiently interacts with eIF-
RT 4E.";
RL Mol. Cell 4:1017-1027(1999).
CC -!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation of protein synthesis and
CC facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structures (PubMed:10635326). In addition to its role in
CC translation initiation, also acts as a regulator of translation and
CC stability in the cytoplasm (By similarity). Maternal RNA in oocytes
CC remain in a dormant state as tacc3/maskin outcompetes eif4g to bind
CC eif4e, thereby preventing translation (PubMed:10635326). During oocyte
CC maturation this complex dissolves and eif4g binds eif4e to allow
CC translation of maternal RNAs (PubMed:10635326).
CC {ECO:0000250|UniProtKB:P06730, ECO:0000269|PubMed:10635326}.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least eif4a, eif4e and eif4g. eif4e is also known to
CC interact with other partners (By similarity). tacc3/maskin competes
CC with eif4g for binding to eif4e (PubMed:10635326).
CC {ECO:0000250|UniProtKB:P06730, ECO:0000269|PubMed:10635326}.
CC -!- INTERACTION:
CC P48597; Q9PTG8: tacc3; NbExp=3; IntAct=EBI-65739, EBI-65726;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10635326}.
CC Note=When interacting with tacc3/maskin. {ECO:0000269|PubMed:10635326}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:10635326, ECO:0000269|PubMed:7875328}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; D31837; BAA06623.1; -; mRNA.
DR PIR; I51413; I51413.
DR RefSeq; XP_018090600.1; XM_018235111.1.
DR AlphaFoldDB; P48597; -.
DR SMR; P48597; -.
DR DIP; DIP-29251N; -.
DR IntAct; P48597; 2.
DR MINT; P48597; -.
DR DNASU; 399255; -.
DR GeneID; 399255; -.
DR CTD; 399255; -.
DR Xenbase; XB-GENE-6254191; eif4e1b.S.
DR OrthoDB; 1394271at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 399255; Expressed in gastrula and 19 other tissues.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR InterPro; IPR019770; TIF_eIF_4E_CS.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
DR PROSITE; PS00813; IF4E; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..213
FT /note="Eukaryotic translation initiation factor 4E"
FT /id="PRO_0000193640"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52..53
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT BINDING 98..99
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT BINDING 153..158
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT BINDING 201..203
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
SQ SEQUENCE 213 AA; 24635 MW; E9412DFF235AE9E8 CRC64;
MAAVEPENTN PQSTEEEKET GQEIVSPDQY IKHPLQNRWA LWFFKNDKSK TWQANLRLIS
KFDTVEDFWA LYNHIQLSSN LMSGCDYSLF KDGIEPMWED EKNKRGGRWL ITLNKQQRRN
DLDRFWLETL MCLIGESFDE HSDDVCGAVV NVRAKGDKIA IWTTEFENKD AVTHIGRVYK
ERLGLPAKVV IGYQSHADTA TKSGSTTKNR FVV
