IF1AX_MOUSE
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 03-AUG-2022, entry version 137.
DE RecName: Full=Eukaryotic translation initiation factor 1A, X-chromosomal;
DE Short=eIF-1A 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 cell,
RC 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: 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 (By similarity). {ECO:0000250}.
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; Q8BMJ3; -.
DR PeptideAtlas; Q8BMJ3; -.
DR PRIDE; Q8BMJ3; -.
DR ProteomicsDB; 267091; -.
DR Antibodypedia; 9819; 102 antibodies from 24 providers.
DR DNASU; 66235; -.
DR Ensembl; ENSMUST00000087143; ENSMUSP00000084387; ENSMUSG00000067194.
DR GeneID; 66235; -.
DR KEGG; mmu:66235; -.
DR UCSC; uc009usl.1; mouse.
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; LGGNHVR; -.
DR OrthoDB; 1426335at2759; -.
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 74 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 261 other tissues.
DR Genevisible; Q8BMJ3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Initiation factor; Protein biosynthesis; Reference proteome.
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
