ID EF1A1_MOUSE Reviewed; 462 AA.
AC P10126; Q61511; Q6ZWN2; Q8BMB8; Q8BVS8; Q99KU5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 3.
DT 01-MAY-2013, entry version 145.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha-1;
DE AltName: Full=Elongation factor Tu;
DE Short=EF-Tu;
DE AltName: Full=Eukaryotic elongation factor 1 A-1;
DE Short=eEF1A-1;
GN Name=Eef1a1; Synonyms=Eef1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3215517; DOI=10.1016/0378-1119(88)90195-3;
RA Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.;
RT "Isolation and mapping of a gene for protein synthesis initiation
RT factor 4A and its expression during differentiation of murine
RT erythroleukemia cells.";
RL Gene 70:231-243(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2911475; DOI=10.1093/nar/17.1.442;
RA Lu X., Werner D.;
RT "The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1
RT alpha) mRNA.";
RL Nucleic Acids Res. 17:442-442(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Testis, and Thymus;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
RX PubMed=3481036;
RA Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N.,
RA Wahba A.J.;
RT "Expression of a gene for mouse eucaryotic elongation factor Tu during
RT murine erythroleukemic cell differentiation.";
RL Mol. Cell. Biol. 7:3929-3936(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
RX PubMed=3960725; DOI=10.1093/nar/14.5.2409;
RA Rao T.R., Slobin L.I.;
RT "Structure of the amino-terminal end of mammalian elongation factor
RT Tu.";
RL Nucleic Acids Res. 14:2409-2409(1986).
RN [7]
RP PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-290 AND
RP 431-439, AND MASS SPECTROMETRY.
RC STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 291-313 AND 372-376, AND ETHANOLAMINYLATION AT
RP GLU-301 AND GLU-374.
RX PubMed=2569467;
RA Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.;
RT "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally
RT modified by novel amide-linked ethanolamine-phosphoglycerol moieties.
RT Addition of ethanolamine-phosphoglycerol to specific glutamic acid
RT residues on EF-1 alpha.";
RL J. Biol. Chem. 264:14334-14341(1989).
RN [9]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH IFIT1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19856081; DOI=10.1007/s11010-009-0289-9;
RA Li H.T., Su Y.P., Cheng T.M., Xu J.M., Liao J., Chen J.C., Ji C.Y.,
RA Ai G.P., Wang J.P.;
RT "The interaction between interferon-induced protein with
RT tetratricopeptide repeats-1 and eukaryotic elongation factor-1A.";
RL Mol. Cell. Biochem. 337:101-110(2010).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis. With PARP1 and TXK, forms a complex that acts as a T
CC helper 1 (Th1) cell-specific transcription factor and binds the
CC promoter of IFN-gamma to directly regulate its transcription, and
CC is thus involved importantly in Th1 cytokine production (By
CC similarity).
CC -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran
CC and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS
CC (By similarity). May interact with ERGIC2 (By similarity).
CC Interacts with DLC1, facilitating distribution to the membrane
CC periphery and ruffles upon growth factor stimulation (By
CC similarity). Interacts with IFIT1 (via TPR repeats 4-7).
CC -!- INTERACTION:
CC Q01534:TSPY1 (xeno); NbExp=5; IntAct=EBI-773865, EBI-1973142;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC Note=Colocalizes with DLC1 at actin-rich regions in the cell
CC periphery (By similarity).
CC -!- PTM: ISGylated.
CC -!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
CC translation efficiency (By similarity).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-Tu/EF-1A subfamily.
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DR EMBL; M22432; AAA50406.1; -; mRNA.
DR EMBL; X13661; CAA31957.1; -; mRNA.
DR EMBL; AK032914; BAC28085.1; -; mRNA.
DR EMBL; AK076696; BAC36446.1; -; mRNA.
DR EMBL; AK081725; BAC38311.1; -; mRNA.
DR EMBL; AK083361; BAC38884.1; -; mRNA.
DR EMBL; BC004005; AAH04005.1; -; mRNA.
DR EMBL; BC004067; AAH04067.1; -; mRNA.
DR EMBL; BC005660; AAH05660.1; -; mRNA.
DR EMBL; BC018223; AAH18223.1; -; mRNA.
DR EMBL; BC018485; AAH18485.1; -; mRNA.
DR EMBL; BC083069; AAH83069.1; -; mRNA.
DR EMBL; M17878; AAA37538.1; -; Genomic_DNA.
DR EMBL; X03688; CAA27324.1; -; mRNA.
DR IPI; IPI00307837; -.
DR PIR; S02114; EFMS1.
DR RefSeq; NP_034236.2; NM_010106.2.
DR RefSeq; XP_003946341.1; XM_003946292.1.
DR RefSeq; XP_003946342.1; XM_003946293.1.
DR RefSeq; XP_003946345.1; XM_003946296.1.
DR RefSeq; XP_003946346.1; XM_003946297.1.
DR RefSeq; XP_003946347.1; XM_003946298.1.
DR RefSeq; XP_003946348.1; XM_003946299.1.
DR RefSeq; XP_003946349.1; XM_003946300.1.
DR RefSeq; XP_003946350.1; XM_003946301.1.
DR UniGene; Mm.138471; -.
DR UniGene; Mm.335315; -.
DR UniGene; Mm.360075; -.
DR UniGene; Mm.391071; -.
DR UniGene; Mm.485669; -.
DR UniGene; Mm.486931; -.
DR ProteinModelPortal; P10126; -.
DR SMR; P10126; 2-443.
DR IntAct; P10126; 14.
DR PhosphoSite; P10126; -.
DR SWISS-2DPAGE; P10126; -.
DR PaxDb; P10126; -.
DR PRIDE; P10126; -.
DR Ensembl; ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
DR GeneID; 101056619; -.
DR GeneID; 13627; -.
DR KEGG; mmu:101056619; -.
DR KEGG; mmu:13627; -.
DR CTD; 1915; -.
DR MGI; MGI:1096881; Eef1a1.
DR eggNOG; COG5256; -.
DR HOGENOM; HOG000229291; -.
DR HOVERGEN; HBG000179; -.
DR InParanoid; P10126; -.
DR KO; K03231; -.
DR OMA; IEMHHES; -.
DR OrthoDB; EOG40K7ZP; -.
DR NextBio; 284304; -.
DR ArrayExpress; P10126; -.
DR Bgee; P10126; -.
DR Genevestigator; P10126; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; Elong_init_C; 1.
DR SUPFAM; SSF50447; Translat_factor; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1 462 Elongation factor 1-alpha 1.
FT /FTId=PRO_0000090886.
FT NP_BIND 14 21 GTP (By similarity).
FT NP_BIND 91 95 GTP (By similarity).
FT NP_BIND 153 156 GTP (By similarity).
FT MOD_RES 36 36 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 55 55 N6,N6-dimethyllysine (By similarity).
FT MOD_RES 79 79 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 165 165 N6,N6-dimethyllysine (By similarity).
FT MOD_RES 300 300 Phosphoserine; by TGFBR1 (By similarity).
FT MOD_RES 301 301 5-glutamyl
FT glycerylphosphorylethanolamine.
FT MOD_RES 318 318 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 374 374 5-glutamyl
FT glycerylphosphorylethanolamine.
FT MOD_RES 432 432 Phosphothreonine; by PASK (By
FT similarity).
FT CONFLICT 7 7 H -> R (in Ref. 5; AAA37538).
FT CONFLICT 15 15 H -> L (in Ref. 5; AAA37538).
FT CONFLICT 23 23 T -> S (in Ref. 5; AAA37538).
FT CONFLICT 77 78 LW -> QR (in Ref. 2; CAA31957).
FT CONFLICT 83 83 S -> A (in Ref. 6; CAA27324).
FT CONFLICT 91 92 DA -> ES (in Ref. 2; CAA31957).
FT CONFLICT 108 108 Q -> R (in Ref. 5; AAA37538).
FT CONFLICT 156 156 D -> G (in Ref. 3; BAC28085).
FT CONFLICT 222 222 S -> H (in Ref. 1; AAA50406).
FT CONFLICT 224 226 SGT -> VAP (in Ref. 2; CAA31957).
FT CONFLICT 225 225 G -> D (in Ref. 4; AAH04005).
FT CONFLICT 239 239 Missing (in Ref. 2; CAA31957).
FT CONFLICT 350 350 P -> T (in Ref. 3; BAC36446).
SQ SEQUENCE 462 AA; 50114 MW; 71072871DE7405DC CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
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