IFIT5_HUMAN
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 03-AUG-2022, entry version 183.
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, regulates positively 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 DDX58/RIG-I at
CC cell surface ruffles. Localizes to actin-rich protrusions from the
CC apical 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 and
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}.
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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; 84.
DR IntAct; Q13325; 18.
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; Q13325; -.
DR PeptideAtlas; Q13325; -.
DR PRIDE; Q13325; -.
DR ProteomicsDB; 3893; -.
DR ProteomicsDB; 59315; -. [Q13325-1]
DR TopDownProteomics; Q13325-1; -. [Q13325-1]
DR Antibodypedia; 30272; 171 antibodies from 27 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 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; GRKYYER; -.
DR OrthoDB; 460948at2759; -.
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; 19 hits in 1068 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 199 other tissues.
DR Genevisible; Q13325; HS.
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 I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR024125; Interferon_induced_IFIT5.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10271:SF28; PTHR10271:SF28; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 3.
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 PPP-RNA-
FT 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 tRNA-
FT 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
