ID   IF1AX_MOUSE             Reviewed;         144 AA.
AC   Q8BMJ3; Q3UY50; Q6ZWL8; Q8BJZ2; Q8BMH8; Q9CSL9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Eukaryotic translation initiation factor 1A, X-chromosomal;
DE            Short=eIF-1A X isoform;
DE            Short=eIF1A X isoform;
DE   AltName: Full=Eukaryotic translation initiation factor 4C;
DE            Short=eIF-4C;
GN   Name=Eif1ax; Synonyms=Eif1ay;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Blastocyst, Cerebellum, Embryo, Embryonic eye, Embryonic stem
RC   cell, Forelimb, Medulla oblongata, Olfactory bulb, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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:0000250|UniProtKB:P47813}.
CC   -!- SUBUNIT: Component of the 43S pre-initiation complex (43S PIC), which
CC       is composed of the 40S ribosomal subunit, EIF1, eIF1A (EIF1AX), eIF3
CC       complex, EIF5 and eIF2-GTP-initiator tRNA complex (eIF2 ternary
CC       complex). Interacts with EIF5; this interaction contributes to the
CC       maintenance of EIF1 within the open 43S PIC. Interacts through its C-
CC       terminal domain (CTD) with the CTD of EIF5B; from the location of the
CC       start codon by the 43S complex until the formation of the 80S complex.
CC       {ECO:0000250|UniProtKB:P47813}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR   EMBL; AK005185; BAB23869.1; -; mRNA.
DR   EMBL; AK007301; BAB24942.1; -; mRNA.
DR   EMBL; AK012233; BAB28110.1; -; mRNA.
DR   EMBL; AK012464; BAB28259.3; -; mRNA.
DR   EMBL; AK012714; BAB28428.1; -; mRNA.
DR   EMBL; AK021283; BAB32361.1; -; mRNA.
DR   EMBL; AK030774; BAC27130.1; -; mRNA.
DR   EMBL; AK031113; BAC27259.1; -; mRNA.
DR   EMBL; AK077710; BAC36971.1; -; mRNA.
DR   EMBL; AK090053; BAC41069.1; -; mRNA.
DR   EMBL; AK134827; BAE22301.1; -; mRNA.
DR   EMBL; AK134969; BAE22363.1; -; mRNA.
DR   EMBL; AK165574; BAE38266.1; -; mRNA.
DR   EMBL; AK166629; BAE38904.1; -; mRNA.
DR   EMBL; AK166852; BAE39071.1; -; mRNA.
DR   EMBL; BC027284; AAH27284.1; -; mRNA.
DR   CCDS; CCDS41192.1; -.
DR   RefSeq; NP_079713.2; NM_025437.4.
DR   AlphaFoldDB; Q8BMJ3; -.
DR   SMR; Q8BMJ3; -.
DR   BioGRID; 211316; 3.
DR   IntAct; Q8BMJ3; 1.
DR   STRING; 10090.ENSMUSP00000084387; -.
DR   iPTMnet; Q8BMJ3; -.
DR   PhosphoSitePlus; Q8BMJ3; -.
DR   REPRODUCTION-2DPAGE; Q8BMJ3; -.
DR   EPD; Q8BMJ3; -.
DR   jPOST; Q8BMJ3; -.
DR   MaxQB; Q8BMJ3; -.
DR   PaxDb; 10090-ENSMUSP00000084387; -.
DR   PeptideAtlas; Q8BMJ3; -.
DR   ProteomicsDB; 267091; -.
DR   Pumba; Q8BMJ3; -.
DR   Antibodypedia; 9819; 130 antibodies from 24 providers.
DR   DNASU; 66235; -.
DR   Ensembl; ENSMUST00000087143.7; ENSMUSP00000084387.7; ENSMUSG00000067194.7.
DR   GeneID; 66235; -.
DR   KEGG; mmu:66235; -.
DR   UCSC; uc009usl.1; mouse.
DR   AGR; MGI:1913485; -.
DR   CTD; 1964; -.
DR   MGI; MGI:1913485; Eif1ax.
DR   VEuPathDB; HostDB:ENSMUSG00000067194; -.
DR   eggNOG; KOG3403; Eukaryota.
DR   GeneTree; ENSGT00390000008256; -.
DR   HOGENOM; CLU_109098_0_1_1; -.
DR   InParanoid; Q8BMJ3; -.
DR   OMA; WRYTRTE; -.
DR   OrthoDB; 2919581at2759; -.
DR   PhylomeDB; Q8BMJ3; -.
DR   TreeFam; TF350394; -.
DR   Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-MMU-72649; Translation initiation complex formation.
DR   Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   BioGRID-ORCS; 66235; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Eif1ax; mouse.
DR   PRO; PR:Q8BMJ3; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8BMJ3; Protein.
DR   Bgee; ENSMUSG00000067194; Expressed in otic placode and 264 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; ISO:MGI.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; ISO:MGI.
DR   GO; GO:0043614; C:multi-eIF complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042255; P:ribosome assembly; IEA:Ensembl.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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.
DR   Genevisible; Q8BMJ3; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   RNA-binding; tRNA-binding.
FT   CHAIN           1..144
FT                   /note="Eukaryotic translation initiation factor 1A, X-
FT                   chromosomal"
FT                   /id="PRO_0000145107"
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   CONFLICT        46
FT                   /note="R -> G (in Ref. 1; BAC36971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="G -> R (in Ref. 1; BAB23869)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="Y -> N (in Ref. 1; BAC27259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="D -> E (in Ref. 1; BAC27130)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   144 AA;  16460 MW;  1C4209855B21BFD4 CRC64;
     MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH
     IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT
     FGPGDDDEIQ FDDIGDDDED IDDI
//