PDCD4_MOUSE
ID PDCD4_MOUSE Reviewed; 469 AA.
AC Q61823; P97296; Q3T9A9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Programmed cell death protein 4;
DE AltName: Full=Protein MA-3;
DE AltName: Full=Topoisomerase-inhibitor suppressed protein;
GN Name=Pdcd4; Synonyms=Ma3, Tis;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Thymus;
RX PubMed=8543179; DOI=10.1016/0378-1119(95)00607-9;
RA Shibahara K., Asano M., Ishida Y., Aoki T., Koike T., Honjo T.;
RT "Isolation of a novel mouse gene MA-3 that is induced upon programmed cell
RT death.";
RL Gene 166:297-301(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=8912629; DOI=10.1006/bbrc.1996.1609;
RA Onishi Y., Kizaki H.;
RT "Molecular cloning of the genes suppressed in RVC lymphoma cells by
RT topoisomerase inhibitors.";
RL Biochem. Biophys. Res. Commun. 228:7-13(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=9714845; DOI=10.1016/s0378-1119(98)00313-8;
RA Onishi Y., Hashimoto S., Kizaki H.;
RT "Cloning of the TIS gene suppressed by topoisomerase inhibitors.";
RL Gene 215:453-459(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BTBR T+ tf/J;
RX PubMed=16682971; DOI=10.1038/ng1796;
RA Clee S.M., Yandell B.S., Schueler K.M., Rabaglia M.E., Richards O.C.,
RA Raines S.M., Kabara E.A., Klass D.M., Mui E.T.-K., Stapleton D.S.,
RA Gray-Keller M.P., Young M.B., Stoehr J.P., Lan H., Boronenkov I.,
RA Raess P.W., Flowers M.T., Attie A.D.;
RT "Positional cloning of Sorcs1, a type 2 diabetes quantitative trait
RT locus.";
RL Nat. Genet. 38:688-693(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4A1 AND EIF4A2.
RX PubMed=12482958; DOI=10.1128/mcb.23.1.26-37.2003;
RA Yang H.-S., Jansen A.P., Komar A.A., Zheng X., Merrick W.C., Costes S.,
RA Lockett S.J., Sonenberg N., Colburn N.H.;
RT "The transformation suppressor Pdcd4 is a novel eukaryotic translation
RT initiation factor 4A binding protein that inhibits translation.";
RL Mol. Cell. Biol. 23:26-37(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12894233; DOI=10.1038/sj.onc.1206710;
RA Boehm M., Sawicka K., Siebrasse J.P., Brehmer-Fastnacht A., Peters R.,
RA Klempnauer K.-H.;
RT "The transformation suppressor protein Pdcd4 shuttles between nucleus and
RT cytoplasm and binds RNA.";
RL Oncogene 22:4905-4910(2003).
RN [10]
RP FUNCTION.
RX PubMed=16024603; DOI=10.1158/0008-5472.can-04-2119;
RA Jansen A.P., Camalier C.E., Colburn N.H.;
RT "Epidermal expression of the translation inhibitor programmed cell death 4
RT suppresses tumorigenesis.";
RL Cancer Res. 65:6034-6041(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 320-469, FUNCTION, INTERACTION
RP WITH EIF4A AND EIF4G, SUBUNIT, AND MUTAGENESIS OF ASP-414; ASP-418 AND
RP SER-457.
RX PubMed=17060447; DOI=10.1128/mcb.00867-06;
RA Laronde-Leblanc N., Santhanam A.N., Baker A.R., Wlodawer A., Colburn N.H.;
RT "Structural basis for inhibition of translation by the tumor suppressor
RT pdcd4.";
RL Mol. Cell. Biol. 27:147-156(2007).
RN [13]
RP STRUCTURE BY NMR OF 319-449, AND INTERACTION WITH EIF4A1.
RX PubMed=17310995; DOI=10.1038/sj.onc.1210305;
RA Waters L.C., Veverka V., Bohm M., Schmedt T., Choong P.T., Muskett F.W.,
RA Klempnauer K.H., Carr M.D.;
RT "Structure of the C-terminal MA-3 domain of the tumour suppressor protein
RT Pdcd4 and characterization of its interaction with eIF4A.";
RL Oncogene 26:4941-4950(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 120-469 IN COMPLEX WITH EIF4A1,
RP SUBUNIT, AND DOMAIN.
RX PubMed=19153607; DOI=10.1038/emboj.2008.278;
RA Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D.,
RA Song H.;
RT "Structural basis for translational inhibition by the tumour suppressor
RT Pdcd4.";
RL EMBO J. 28:274-285(2009).
CC -!- FUNCTION: Inhibits translation initiation and cap-dependent
CC translation. May excert its function by hindering the interaction
CC between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A.
CC Modulates the activation of JUN kinase. Down-regulates the expression
CC of MAP4K1, thus inhibiting events important in driving invasion,
CC namely, MAPK85 activation and consequent JUN-dependent transcription.
CC May play a role in apoptosis. Tumor suppressor. Inhibits tumor
CC promoter-induced neoplastic transformation. Binds RNA.
CC {ECO:0000269|PubMed:12482958, ECO:0000269|PubMed:12894233,
CC ECO:0000269|PubMed:16024603, ECO:0000269|PubMed:17060447}.
CC -!- SUBUNIT: Interacts (via MI domains) with EIF4A1 and EIF4A2 (via N-
CC terminal domain). Heterotrimer with EIF4A1; one molecule of PDCD4 binds
CC two molecules of EIF4A1. Interacts with EIF4G1. May form a complex with
CC EIF4A1 and EIF4G1. The interaction between PDCD4 and EIF4A1 interferes
CC with the interaction between EIF4A1 and EIF4G. When phosphorylated,
CC interacts with BTRC and FBXW11 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q61823; P60843: Eif4a1; NbExp=4; IntAct=EBI-296473, EBI-6665935;
CC Q61823; Q62448: Eif4g2; NbExp=2; IntAct=EBI-296473, EBI-296494;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12894233}. Cytoplasm
CC {ECO:0000269|PubMed:12894233}. Note=Shuttles between the nucleus and
CC cytoplasm (PubMed:12894233). Predominantly nuclear under normal growth
CC conditions, and when phosphorylated at Ser-457 (By similarity).
CC {ECO:0000250|UniProtKB:Q53EL6, ECO:0000269|PubMed:12894233}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Highyly expressed in thymus
CC and liver. Moderately expressed in brain, kidney and spleen; weakly in
CC lung and heart. Expression is up- or down-regulated in response to
CC apoptosis inducers. Regulated by many programmed cell death-inducing
CC stimuli. {ECO:0000269|PubMed:8543179, ECO:0000269|PubMed:9714845}.
CC -!- DOMAIN: Binds EIF4A1 via both MI domains.
CC {ECO:0000269|PubMed:19153607}.
CC -!- PTM: Polyubiquitinated, leading to its proteasomal degradation. Rapidly
CC degraded in response to mitogens. Phosphorylation of the phosphodegron
CC promotes interaction with BTRC and proteasomal degradation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens;
CC phosphorylation promotes proteasomal degradation of PDCD4.
CC {ECO:0000250}.
CC -!- DISEASE: Note=Decreases benign tumor development and malignant
CC progression. {ECO:0000305|PubMed:16024603}.
CC -!- SIMILARITY: Belongs to the PDCD4 family. {ECO:0000305}.
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DR EMBL; D50465; BAA09056.1; -; mRNA.
DR EMBL; D86344; BAA13072.1; -; mRNA.
DR EMBL; AB010139; BAA32356.1; -; Genomic_DNA.
DR EMBL; DQ479921; ABF51670.1; -; Genomic_DNA.
DR EMBL; CT010188; CAJ18396.1; -; mRNA.
DR EMBL; AK134366; BAE22118.1; -; mRNA.
DR EMBL; AK172654; BAE43115.1; -; mRNA.
DR EMBL; BC055739; AAH55739.1; -; mRNA.
DR CCDS; CCDS29903.1; -.
DR PIR; JC4523; JC4523.
DR RefSeq; NP_001161963.1; NM_001168491.1.
DR RefSeq; NP_001161964.1; NM_001168492.1.
DR RefSeq; NP_035180.2; NM_011050.4.
DR RefSeq; XP_006526825.1; XM_006526762.3.
DR PDB; 2HM8; NMR; -; A=319-449.
DR PDB; 2IOL; X-ray; 2.00 A; A/B=320-469.
DR PDB; 2ION; X-ray; 1.57 A; A=320-467.
DR PDB; 2IOS; X-ray; 1.76 A; A=320-469.
DR PDB; 2KZT; NMR; -; B=319-449.
DR PDB; 2NSZ; X-ray; 1.15 A; A=322-450.
DR PDB; 3EIQ; X-ray; 3.50 A; C=120-469.
DR PDBsum; 2HM8; -.
DR PDBsum; 2IOL; -.
DR PDBsum; 2ION; -.
DR PDBsum; 2IOS; -.
DR PDBsum; 2KZT; -.
DR PDBsum; 2NSZ; -.
DR PDBsum; 3EIQ; -.
DR AlphaFoldDB; Q61823; -.
DR BMRB; Q61823; -.
DR SMR; Q61823; -.
DR BioGRID; 202070; 4.
DR IntAct; Q61823; 7.
DR MINT; Q61823; -.
DR STRING; 10090.ENSMUSP00000073975; -.
DR iPTMnet; Q61823; -.
DR PhosphoSitePlus; Q61823; -.
DR SwissPalm; Q61823; -.
DR EPD; Q61823; -.
DR jPOST; Q61823; -.
DR MaxQB; Q61823; -.
DR PaxDb; Q61823; -.
DR PeptideAtlas; Q61823; -.
DR PRIDE; Q61823; -.
DR ProteomicsDB; 287901; -.
DR Antibodypedia; 616; 866 antibodies from 43 providers.
DR DNASU; 18569; -.
DR Ensembl; ENSMUST00000025931; ENSMUSP00000025931; ENSMUSG00000024975.
DR Ensembl; ENSMUST00000074371; ENSMUSP00000073975; ENSMUSG00000024975.
DR Ensembl; ENSMUST00000165617; ENSMUSP00000133135; ENSMUSG00000024975.
DR GeneID; 18569; -.
DR KEGG; mmu:18569; -.
DR UCSC; uc008hxb.2; mouse.
DR CTD; 27250; -.
DR MGI; MGI:107490; Pdcd4.
DR VEuPathDB; HostDB:ENSMUSG00000024975; -.
DR eggNOG; KOG0403; Eukaryota.
DR GeneTree; ENSGT00390000015948; -.
DR HOGENOM; CLU_025354_1_0_1; -.
DR InParanoid; Q61823; -.
DR OMA; HHELIYE; -.
DR OrthoDB; 434771at2759; -.
DR PhylomeDB; Q61823; -.
DR TreeFam; TF323207; -.
DR BioGRID-ORCS; 18569; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Pdcd4; mouse.
DR EvolutionaryTrace; Q61823; -.
DR PRO; PR:Q61823; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q61823; protein.
DR Bgee; ENSMUSG00000024975; Expressed in lacrimal gland and 275 other tissues.
DR ExpressionAtlas; Q61823; baseline and differential.
DR Genevisible; Q61823; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0060940; P:epithelial to mesenchymal transition involved in cardiac fibroblast development; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:BHF-UCL.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:UniProtKB.
DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:BHF-UCL.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; ISO:MGI.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0051246; P:regulation of protein metabolic process; ISO:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR039778; PDCD4.
DR PANTHER; PTHR12626; PTHR12626; 1.
DR Pfam; PF02847; MA3; 2.
DR SMART; SM00544; MA3; 2.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS51366; MI; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..469
FT /note="Programmed cell death protein 4"
FT /id="PRO_0000256520"
FT DOMAIN 163..284
FT /note="MI 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 326..449
FT /note="MI 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..64
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 70..76
FT /note="Phosphodegron"
FT /evidence="ECO:0000250"
FT MOTIF 448..454
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JID1"
FT MOD_RES 67
FT /note="Phosphoserine; by PKB and RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 152
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MOD_RES 457
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:Q53EL6"
FT MUTAGEN 414
FT /note="D->A: Strongly reduced interaction with EIF4A1."
FT /evidence="ECO:0000269|PubMed:17060447"
FT MUTAGEN 418
FT /note="D->A: Strongly reduced interaction with EIF4A1."
FT /evidence="ECO:0000269|PubMed:17060447"
FT MUTAGEN 457
FT /note="S->A,D: No effect on interaction with EIF4A1."
FT /evidence="ECO:0000269|PubMed:17060447"
FT CONFLICT 232
FT /note="S -> I (in Ref. 2; BAA32356 and 3; BAA13072)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="V -> I (in Ref. 2; BAA32356 and 3; BAA13072)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="D -> G (in Ref. 5; BAE43115)"
FT /evidence="ECO:0000305"
FT HELIX 162..178
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:3EIQ"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:3EIQ"
FT TURN 225..229
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:3EIQ"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3EIQ"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:2NSZ"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:2NSZ"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2NSZ"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:2NSZ"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:2IOL"
FT HELIX 378..392
FT /evidence="ECO:0007829|PDB:2NSZ"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:2NSZ"
FT HELIX 422..435
FT /evidence="ECO:0007829|PDB:2NSZ"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:2NSZ"
SQ SEQUENCE 469 AA; 51702 MW; 6883BCE5011692F1 CRC64;
MDIENEQTLN VNPTDPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASTI NEARINAKAK
RRLRKNSSRD SGRGDSVSDN GSEAVRSGVA VPTSPKGRLL DRRSRSGKGR GLPKKGGAGG
KGVWGTPGQV YDVEEVDVKD PNYDDDQENC VYETVVLPLD ETAFEKTLTP IIQEYFEHGD
TNEVAEMLRD LNLGEMKSGV PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTNDVEKSF
DKLLKDLPEL ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV
LLSMSKGGKR KDSVWGSGGG QQPVNHLVKE IDMLLKEYLL SGDISEAEHC LKELEVPHFH
HELVYEAIVM VLESTGESAF KMILDLLKSL WKSSTITIDQ MKRGYERIYN EIPDINLDVP
HSYSVLERFV EECFQAGIIS KQLRDLCPSR GRKRFVSEGD GGRLKPESY
