ID   IF1A_RABIT              Reviewed;         144 AA.
AC   P47814;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Eukaryotic translation initiation factor 1A;
DE            Short=eIF-1A;
DE   AltName: Full=Eukaryotic translation initiation factor 4C;
DE            Short=eIF-4C;
GN   Name=EIF1A;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-144.
RX   PubMed=8106356; DOI=10.1016/s0021-9258(17)41850-3;
RA   Dever T.E., Wei C.-L., Benkowski L.A., Browning K., Merrick W.C.,
RA   Hershey J.W.B.;
RT   "Determination of the amino acid sequence of rabbit, human, and wheat germ
RT   protein synthesis factor eIF-4C by cloning and chemical sequencing.";
RL   J. Biol. Chem. 269:3212-3218(1994).
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.
CC   -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR   PIR; B53045; B53045.
DR   AlphaFoldDB; P47814; -.
DR   BMRB; P47814; -.
DR   SMR; P47814; -.
DR   STRING; 9986.ENSOCUP00000008779; -.
DR   eggNOG; KOG3403; Eukaryota.
DR   InParanoid; P47814; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd05793; S1_IF1A; 1.
DR   Gene3D; 2.40.50.140; -; 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   PANTHER; PTHR21668; PTHR21668; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00523; eIF-1A; 1.
DR   PROSITE; PS01262; IF1A; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Initiation factor; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8106356"
FT   CHAIN           2..144
FT                   /note="Eukaryotic translation initiation factor 1A"
FT                   /id="PRO_0000145108"
FT   DOMAIN          22..96
FT                   /note="S1-like"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..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"
FT   VARIANT         31
FT                   /note="D -> E"
FT   VARIANT         79
FT                   /note="V -> I"
FT   VARIANT         83
FT                   /note="E -> D"
SQ   SEQUENCE   144 AA;  16528 MW;  743625D0CB29F1DD CRC64;
     MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM LFDGVKRLFH
     IRGKLRKKVW INTSDIILVG LREYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT
     FGPGDDDEIQ FDDIGDDDED IDDI