ID A0A2T7P5G5_POMCA Unreviewed; 273 AA.
AC A0A2T7P5G5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN ORFNames=C0Q70_11240 {ECO:0000313|EMBL:PVD28646.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD28646.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD28646.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD28646.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD28646.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- FUNCTION: Seems to be required for maximal rate of protein
CC biosynthesis. Enhances ribosome dissociation into subunits and
CC stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC subunits. {ECO:0000256|ARBA:ARBA00025502}.
CC -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|RuleBase:RU004364}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD28646.1}.
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DR EMBL; PZQS01000006; PVD28646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7P5G5; -.
DR STRING; 400727.A0A2T7P5G5; -.
DR EnsemblMetazoa; XM_025241090.1; XP_025096875.1; LOC112565571.
DR EnsemblMetazoa; XM_025241492.1; XP_025097277.1; LOC112565759.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg6.
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; IPR017245; BLOC-1_complex_su-3.
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:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 4C; 1.
DR Pfam; PF15753; BLOC1S3; 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:UP000245119}.
FT DOMAIN 150..224
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 41..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 30651 MW; 9D742BA8FDEF0564 CRC64;
MEKSKFQTVV QGEASESDDD EVHVSSVNIK PFPSRVLQTS LESKKTAGGQ AVVVEGEASE
SEEEEEVEVD TSLNSTKLPP LKVEPQKKVQ YGSSGDLSDV PTLMSPRMAD LRFNKPKYDT
LGSTPYQMKE NLDRKGGKNR RRGKNENENE KRELVFKEDG QEYAQVTKML GNGRLEAMCF
DGVKRLCHIR GKLRKKVWIN SGDIILLGLR DYQDTKADVI LKYTADEARN LKAYGELPES
AKINENAGME DDLDENITFD NFDDDEDDDD DAA
//
