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Database: UniProt
Entry: A0A452IYT7_9SAUR
LinkDB: A0A452IYT7_9SAUR
Original site: A0A452IYT7_9SAUR 
ID   A0A452IYT7_9SAUR        Unreviewed;       144 AA.
AC   A0A452IYT7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000033248.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000033248.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A452IYT7; -.
DR   SMR; A0A452IYT7; -.
DR   STRING; 38772.ENSGAGP00000033248; -.
DR   Ensembl; ENSGAGT00000037675.1; ENSGAGP00000033248.1; ENSGAGG00000023700.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
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:UP000291020}.
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          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"
SQ   SEQUENCE   144 AA;  16442 MW;  1DE91334F191BEC5 CRC64;
     MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAL CFDGVKRLCH
     IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT
     FGPGDDDEIQ FDDIGDDDED IDDI
//
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