ID A0A2Y9IL63_ENHLU Unreviewed; 144 AA.
AC A0A2Y9IL63;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN Name=LOC111139969 {ECO:0000313|RefSeq:XP_022348069.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022348069.1};
RN [1] {ECO:0000313|RefSeq:XP_022348069.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022348069.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the 43S pre-initiation complex (43S PIC), which
CC binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated
CC region, and locates the initiation codon. This protein enhances
CC formation of the cap-proximal complex. Together with EIF1, facilitates
CC scanning, start codon recognition, promotion of the assembly of 48S
CC complex at the initiation codon (43S PIC becomes 48S PIC after the
CC start codon is reached), and dissociation of aberrant complexes. After
CC start codon location, together with EIF5B orients the initiator
CC methionine-tRNA in a conformation that allows 60S ribosomal subunit
CC joining to form the 80S initiation complex. Is released after 80S
CC initiation complex formation, just after GTP hydrolysis by EIF5B, and
CC before release of EIF5B. Its globular part is located in the A site of
CC the 40S ribosomal subunit. Its interaction with EIF5 during scanning
CC contribute to the maintenance of EIF1 within the open 43S PIC. In
CC contrast to yeast orthologs, does not bind EIF1.
CC {ECO:0000256|RuleBase:RU004365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|RuleBase:RU004364}.
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DR RefSeq; XP_022348069.1; XM_022492361.1.
DR AlphaFoldDB; A0A2Y9IL63; -.
DR STRING; 391180.A0A2Y9IL63; -.
DR KEGG; elk:111139969; -.
DR OrthoDB; 2919581at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd05793; S1_IF1A; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00216; aIF_1A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR001253; TIF_eIF-1A.
DR InterPro; IPR018104; TIF_eIF-1A_CS.
DR NCBIfam; TIGR00523; eIF-1A; 1.
DR PANTHER; PTHR21668; EIF-1A; 1.
DR PANTHER; PTHR21668:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 1A, X-CHROMOSOMAL; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS01262; IF1A; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181,
KW ECO:0000256|RuleBase:RU004365};
KW Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181,
KW ECO:0000256|RuleBase:RU004365};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT DOMAIN 22..96
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 144 AA; 16474 MW; 5CAC19844B30BFC2 CRC64;
MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH
IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHVKINDTDT
FGPGDDDEIQ FDDIGDDDED IDDI
//
