ID IFIT5_HUMAN Reviewed; 482 AA. AC Q13325; B2R5X9; B4DDV1; Q5T7I9; Q6IAX3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 5; DE Short=IFIT-5; DE AltName: Full=Interferon-induced 58 kDa protein; DE AltName: Full=Retinoic acid- and interferon-inducible 58 kDa protein; DE Short=P58; GN Name=IFIT5; Synonyms=ISG58, RI58; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9398535; DOI=10.1006/bcmd.1997.0151; RA Niikura T., Hirata R., Weil S.C.; RT "A novel interferon-inducible gene expressed during myeloid RT differentiation."; RL Blood Cells Mol. Dis. 23:337-349(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas, and Spleen; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP REVIEW. RX PubMed=20950130; DOI=10.1089/jir.2010.0101; RA Fensterl V., Sen G.C.; RT "The ISG56/IFIT1 gene family."; RL J. Interferon Cytokine Res. 31:71-78(2011). RN [9] RP RNA-BINDING. RX PubMed=21642987; DOI=10.1038/ni.2048; RA Pichlmair A., Lassnig C., Eberle C.A., Gorna M.W., Baumann C.L., RA Burkard T.R., Buerckstuemmer T., Stefanovic A., Krieger S., Bennett K.L., RA Ruelicke T., Weber F., Colinge J., Mueller M., Superti-Furga G.; RT "IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA."; RL Nat. Immunol. 12:624-630(2011). RN [10] RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF GLU-33; THR-37; GLN-41; LYS-48; RP LYS-150; TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; GLN-288; LEU-291; RP ARG-307; ASP-334; PHE-339; LYS-415 AND LYS-426. RX PubMed=25092312; DOI=10.1073/pnas.1412842111; RA Katibah G.E., Qin Y., Sidote D.J., Yao J., Lambowitz A.M., Collins K.; RT "Broad and adaptable RNA structure recognition by the human interferon- RT induced tetratricopeptide repeat protein IFIT5."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12025-12030(2014). RN [11] RP FUNCTION, AND INTERACTION WITH MAP3K7; CHUK; IKBKB AND IKBKG. RX PubMed=26334375; DOI=10.1016/j.cellsig.2015.08.018; RA Zheng C., Zheng Z., Zhang Z., Meng J., Liu Y., Ke X., Hu Q., Wang H.; RT "IFIT5 positively regulates NF-kappaB signaling through synergizing the RT recruitment of IkappaB kinase (IKK) to TGF-beta-activated kinase 1 RT (TAK1)."; RL Cell. Signal. 27:2343-2354(2015). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS), FUNCTION, RNA-BINDING, DNA-BINDING, RP SUBUNIT, AND MUTAGENESIS OF 185-TYR-ARG-186; 253-ARG-TYR-254; LYS-257; RP PHE-284; ARG-294; 337-PHE--PHE-339; ARG-384; LYS-415 AND 422-LYS--LYS-426. RX PubMed=23774268; DOI=10.1038/cr.2013.80; RA Feng F., Yuan L., Wang Y.E., Crowley C., Lv Z., Li J., Liu Y., Cheng G., RA Zeng S., Liang H.; RT "Crystal structure and nucleotide selectivity of human IFIT5/ISG58."; RL Cell Res. 23:1055-1058(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RNA-BINDING, SUBCELLULAR RP LOCATION, SUBUNIT, AND MUTAGENESIS OF LEU-291; LYS-302; ARG-307; LYS-309; RP 388-PHE-HIS-389; LYS-415; LYS-422 AND LYS-426. RX PubMed=23317505; DOI=10.1016/j.molcel.2012.12.015; RA Katibah G.E., Lee H.J., Huizar J.P., Vogan J.M., Alber T., Collins K.; RT "tRNA binding, structure, and localization of the human interferon-induced RT protein IFIT5."; RL Mol. Cell 49:743-750(2013). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP-RNA, FUNCTION, RP RNA-BINDING, AND MUTAGENESIS OF GLU-33; GLN-41; LYS-150; TYR-156; ARG-186; RP TYR-250; ARG-253; TYR-254; ARG-260; HIS-287 AND GLN-288. RX PubMed=23334420; DOI=10.1038/nature11783; RA Abbas Y.M., Pichlmair A., Gorna M.W., Superti-Furga G., Nagar B.; RT "Structural basis for viral 5'-PPP-RNA recognition by human IFIT RT proteins."; RL Nature 494:60-64(2013). CC -!- FUNCTION: Interferon-induced RNA-binding protein involved in the human CC innate immune response. Has a broad and adaptable RNA structure CC recognition important for RNA recognition specificity in antiviral CC defense. Binds precursor and processed tRNAs as well as poly-U-tailed CC tRNA fragments (PubMed:25092312, PubMed:23317505, PubMed:23774268). CC Specifically binds single-stranded RNA bearing a 5'-triphosphate group CC (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. CC Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and CC bear a 5'-triphosphate group instead, are specific from viruses, CC providing a molecular signature to distinguish between self and non- CC self mRNAs by the host during viral infection. Directly binds PPP-RNA CC in a non-sequence-specific manner (PubMed:23334420). Also recognizes CC and selectively binds AT-rich dsDNA (PubMed:23774268). Additionally, as CC a mediator in innate immunity, positively regulates IKK-NFKB signaling CC by sinergizing the recruitment of IKK to MAP3K7 (PubMed:26334375). CC {ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:23334420, CC ECO:0000269|PubMed:23774268, ECO:0000269|PubMed:25092312, CC ECO:0000269|PubMed:26334375}. CC -!- SUBUNIT: Monomer (PubMed:23317505, PubMed:23334420, PubMed:23774268). CC Interacts with MAP3K7 and the components of the IKK core complex CHUK, CC IKBKB and IKBKG; the interaction synergizes the recruitment of IKK to CC MAP3K7 and enhances IKK phosphorylation (PubMed:26334375). CC {ECO:0000269|PubMed:23317505, ECO:0000269|PubMed:23334420, CC ECO:0000269|PubMed:23774268, ECO:0000269|PubMed:26334375}. CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane CC {ECO:0000269|PubMed:23317505}. Note=Colocalized with RIGI at cell CC surface ruffles. Localizes to actin-rich protrusions from the apical CC cell surface. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13325-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13325-2; Sequence=VSP_056412; CC -!- INDUCTION: By interferons (IFNs). CC -!- DOMAIN: RNA recognition is mediated by a convoluted intramolecular fold CC of the TPR repeats (TPR eddy), which scaffolds unique additional CC helices that form an RNA binding cleft (PubMed:23317505, CC PubMed:23334420). Undergoes a conformational change upon RNA-binding: CC unliganded exists in a more open conformation, facilitating RNA entry CC (PubMed:23334420). {ECO:0000269|PubMed:23334420}. CC -!- SIMILARITY: Belongs to the IFIT family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U34605; AAA84934.1; -; mRNA. DR EMBL; AK293346; BAG56862.1; -; mRNA. DR EMBL; AK312358; BAG35276.1; -; mRNA. DR EMBL; CR457031; CAG33312.1; -; mRNA. DR EMBL; AL353146; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW50135.1; -; Genomic_DNA. DR EMBL; BC025786; AAH25786.1; -; mRNA. DR CCDS; CCDS7403.1; -. [Q13325-1] DR PIR; G02058; G02058. DR RefSeq; NP_036552.1; NM_012420.2. [Q13325-1] DR PDB; 3ZGQ; X-ray; 2.20 A; A=1-482. DR PDB; 4HOQ; X-ray; 2.07 A; A=1-482. DR PDB; 4HOR; X-ray; 1.86 A; A=1-482. DR PDB; 4HOS; X-ray; 2.00 A; A=1-482. DR PDB; 4HOT; X-ray; 2.50 A; A=1-482. DR PDB; 4J0U; X-ray; 1.97 A; A=1-482. DR PDBsum; 3ZGQ; -. DR PDBsum; 4HOQ; -. DR PDBsum; 4HOR; -. DR PDBsum; 4HOS; -. DR PDBsum; 4HOT; -. DR PDBsum; 4J0U; -. DR AlphaFoldDB; Q13325; -. DR SMR; Q13325; -. DR BioGRID; 117289; 100. DR IntAct; Q13325; 19. DR MINT; Q13325; -. DR STRING; 9606.ENSP00000360860; -. DR GlyGen; Q13325; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13325; -. DR PhosphoSitePlus; Q13325; -. DR BioMuta; IFIT5; -. DR DMDM; 6831571; -. DR EPD; Q13325; -. DR jPOST; Q13325; -. DR MassIVE; Q13325; -. DR MaxQB; Q13325; -. DR PaxDb; 9606-ENSP00000360860; -. DR PeptideAtlas; Q13325; -. DR ProteomicsDB; 3893; -. DR ProteomicsDB; 59315; -. [Q13325-1] DR Pumba; Q13325; -. DR TopDownProteomics; Q13325-1; -. [Q13325-1] DR Antibodypedia; 30272; 185 antibodies from 28 providers. DR DNASU; 24138; -. DR Ensembl; ENST00000371795.5; ENSP00000360860.4; ENSG00000152778.10. [Q13325-1] DR Ensembl; ENST00000681348.1; ENSP00000505706.1; ENSG00000152778.10. [Q13325-2] DR GeneID; 24138; -. DR KEGG; hsa:24138; -. DR MANE-Select; ENST00000371795.5; ENSP00000360860.4; NM_012420.3; NP_036552.1. DR UCSC; uc010qnh.3; human. [Q13325-1] DR AGR; HGNC:13328; -. DR CTD; 24138; -. DR DisGeNET; 24138; -. DR GeneCards; IFIT5; -. DR HGNC; HGNC:13328; IFIT5. DR HPA; ENSG00000152778; Low tissue specificity. DR MIM; 616135; gene. DR neXtProt; NX_Q13325; -. DR OpenTargets; ENSG00000152778; -. DR PharmGKB; PA134988392; -. DR VEuPathDB; HostDB:ENSG00000152778; -. DR eggNOG; KOG1124; Eukaryota. DR GeneTree; ENSGT00950000182946; -. DR HOGENOM; CLU_043482_1_0_1; -. DR InParanoid; Q13325; -. DR OMA; VYCEEGW; -. DR OrthoDB; 5401272at2759; -. DR PhylomeDB; Q13325; -. DR TreeFam; TF342671; -. DR PathwayCommons; Q13325; -. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SignaLink; Q13325; -. DR BioGRID-ORCS; 24138; 20 hits in 1146 CRISPR screens. DR GenomeRNAi; 24138; -. DR Pharos; Q13325; Tbio. DR PRO; PR:Q13325; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q13325; Protein. DR Bgee; ENSG00000152778; Expressed in calcaneal tendon and 201 other cell types or tissues. DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB. DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0000339; F:RNA cap binding; IDA:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR013105; TPR_2. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR10271; INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS; 1. DR PANTHER; PTHR10271:SF28; INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS 5; 1. DR Pfam; PF13374; TPR_10; 1. DR Pfam; PF13424; TPR_12; 1. DR Pfam; PF07719; TPR_2; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 5. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 3. DR Genevisible; Q13325; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; Cell membrane; KW Cell projection; Immunity; Innate immunity; Membrane; Reference proteome; KW Repeat; RNA-binding; TPR repeat; tRNA-binding. FT CHAIN 1..482 FT /note="Interferon-induced protein with tetratricopeptide FT repeats 5" FT /id="PRO_0000106351" FT REPEAT 51..84 FT /note="TPR 1" FT REPEAT 94..127 FT /note="TPR 2" FT REPEAT 138..173 FT /note="TPR 3" FT REPEAT 181..214 FT /note="TPR 4" FT REPEAT 249..282 FT /note="TPR 5" FT REPEAT 338..371 FT /note="TPR 6" FT REPEAT 376..410 FT /note="TPR 7" FT REPEAT 435..468 FT /note="TPR 8" FT REGION 254..260 FT /note="Interaction with the 5'-triphosphate group of PPP- FT RNA" FT SITE 33 FT /note="Interaction with PPP-RNA" FT SITE 37 FT /note="Interaction with PPP-RNA" FT SITE 41 FT /note="Interaction with PPP-RNA" FT SITE 150 FT /note="Interaction with PPP-RNA" FT SITE 186 FT /note="Interaction with PPP-RNA" FT SITE 250 FT /note="Interaction with PPP-RNA" FT SITE 288 FT /note="Interaction with the 5'-triphosphate group of PPP- FT RNA" FT VAR_SEQ 158..205 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056412" FT MUTAGEN 33 FT /note="E->A: No effect on RNA-binding but changes size FT profile of RNA bound. Reduces PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 37 FT /note="T->A,V: No effect on RNA-binding but changes size FT profile of RNA bound." FT /evidence="ECO:0000269|PubMed:25092312" FT MUTAGEN 37 FT /note="T->V: Abolishes PPP-RNA-binding." FT MUTAGEN 41 FT /note="Q->E: No effect on RNA-binding but changes size FT profile of RNA bound. Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 48 FT /note="K->A,E: Inhibits RNA-binding." FT /evidence="ECO:0000269|PubMed:25092312" FT MUTAGEN 150 FT /note="K->M: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 150 FT /note="K->N,E: Inhibits RNA-binding." FT /evidence="ECO:0000269|PubMed:25092312" FT MUTAGEN 150 FT /note="K->R: Reduces RNA-binding." FT /evidence="ECO:0000269|PubMed:25092312" FT MUTAGEN 156 FT /note="Y->F,A: No effect on RNA-binding. Reduces FT PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 185..186 FT /note="YR->AE: Reduces binding to RNA and DNA." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 186 FT /note="R->H,A: Abolishes RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 250 FT /note="Y->F: No effect on RNA-binding but changes size FT profile of RNA bound. Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 253..254 FT /note="RY->EA: Reduces binding to RNA and DNA." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 253 FT /note="R->M: Abolishes RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 254 FT /note="Y->F: Abolishes RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 257 FT /note="K->E: Reduces binding to RNA and DNA." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 260 FT /note="R->E: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 284 FT /note="F->A: Strongly reduces binding to dsDNA. No effect FT on ssRNA binding." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 287 FT /note="H->A: Reduces PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 288 FT /note="Q->E: Abolishes RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 291 FT /note="L->A: No effect RNA-binding." FT /evidence="ECO:0000269|PubMed:23317505, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 294 FT /note="R->E: Strongly reduces binding to dsDNA. No effect FT on ssRNA binding." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 302 FT /note="K->A: Reduces RNA-binding." FT /evidence="ECO:0000269|PubMed:23317505" FT MUTAGEN 307 FT /note="R->A: Reduces RNA-binding. 25 fold reduction in FT tRNA-binding." FT /evidence="ECO:0000269|PubMed:23317505, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 309 FT /note="K->A: Reduces RNA-binding." FT /evidence="ECO:0000269|PubMed:23317505" FT MUTAGEN 334 FT /note="D->A: No effect on RNA-binding but changes size FT profile of RNA bound." FT /evidence="ECO:0000269|PubMed:25092312" FT MUTAGEN 337..339 FT /note="FAF->AAA: Reduces binding to RNA and DNA." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 337 FT /note="F->A: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 339 FT /note="F->A: Reduces RNA-binding." FT /evidence="ECO:0000269|PubMed:25092312" FT MUTAGEN 384 FT /note="R->E: Reduces binding to RNA and DNA and impairs FT antiviral activity; when associated with E-415." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 388..389 FT /note="FH->AA: Reduces RNA-binding." FT /evidence="ECO:0000269|PubMed:23317505" FT MUTAGEN 415 FT /note="K->A: Reduces RNA-binding. 25 fold reduction in FT tRNA-binding." FT /evidence="ECO:0000269|PubMed:23317505, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 415 FT /note="K->E: Reduces binding to RNA and DNA and impairs FT antiviral activity; when associated with E-384." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 422..426 FT /note="KLSTK->ELSTE: Reduces binding to RNA and DNA." FT /evidence="ECO:0000269|PubMed:23774268" FT MUTAGEN 422 FT /note="K->A: Reduced RNA-binding." FT /evidence="ECO:0000269|PubMed:23317505, FT ECO:0000269|PubMed:25092312" FT MUTAGEN 426 FT /note="K->A: Reduces RNA-binding. 5 fold reduction in FT tRNA-binding." FT /evidence="ECO:0000269|PubMed:23317505" FT CONFLICT 215 FT /note="S -> N (in Ref. 3; CAG33312)" FT /evidence="ECO:0000305" FT CONFLICT 449 FT /note="G -> R (in Ref. 2; BAG35276)" FT /evidence="ECO:0000305" FT HELIX 3..15 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 31..44 FT /evidence="ECO:0007829|PDB:4HOR" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:4HOQ" FT HELIX 50..63 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 67..84 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 94..106 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 110..126 FT /evidence="ECO:0007829|PDB:4HOR" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 138..150 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 156..169 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 174..189 FT /evidence="ECO:0007829|PDB:4HOR" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 201..210 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 215..227 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 231..244 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 249..261 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 265..278 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 283..303 FT /evidence="ECO:0007829|PDB:4HOR" FT TURN 304..306 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 310..333 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 338..350 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 354..365 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 372..388 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 393..406 FT /evidence="ECO:0007829|PDB:4HOR" FT STRAND 408..410 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 413..430 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 435..447 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 451..464 FT /evidence="ECO:0007829|PDB:4HOR" FT HELIX 469..480 FT /evidence="ECO:0007829|PDB:4HOR" SQ SEQUENCE 482 AA; 55847 MW; 8045BC100384BE05 CRC64; MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR LALYNLLAYV KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY AWVYYHMDQL EEAQKYTGKI GNVCKKLSSP SNYKLECPET DCEKGWALLK FGGKYYQKAK AAFEKALEVE PDNPEFNIGY AITVYRLDDS DREGSVKSFS LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE ILDQISSQPY VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE GGQYSNAEDI FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY LEALKVKDRS PLRTKLTSAL KKLSTKRLCH NALDVQSLSA LGFVYKLEGE KRQAAEYYEK AQKIDPENAE FLTALCELRL SI //