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Interferon-induced protein with tetratricopeptide repeats 5 (IFIT-5) (Interferon-induced 58 kDa protein) (Retinoic acid- and interferon-inducible 58 kDa protein) (P58)

 IFIT5_HUMAN             Reviewed;         482 AA.
Q13325; B2R5X9; B4DDV1; Q5T7I9; Q6IAX3;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 159.
RecName: Full=Interferon-induced protein with tetratricopeptide repeats 5;
Short=IFIT-5;
AltName: Full=Interferon-induced 58 kDa protein;
AltName: Full=Retinoic acid- and interferon-inducible 58 kDa protein;
Short=P58;
Name=IFIT5; Synonyms=ISG58, RI58;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9398535; DOI=10.1006/bcmd.1997.0151;
Niikura T., Hirata R., Weil S.C.;
"A novel interferon-inducible gene expressed during myeloid
differentiation.";
Blood Cells Mol. Dis. 23:337-349(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
REVIEW.
PubMed=20950130; DOI=10.1089/jir.2010.0101;
Fensterl V., Sen G.C.;
"The ISG56/IFIT1 gene family.";
J. Interferon Cytokine Res. 31:71-78(2011).
[9]
RNA-BINDING.
PubMed=21642987; DOI=10.1038/ni.2048;
Pichlmair A., Lassnig C., Eberle C.A., Gorna M.W., Baumann C.L.,
Burkard T.R., Buerckstuemmer T., Stefanovic A., Krieger S.,
Bennett K.L., Ruelicke T., Weber F., Colinge J., Mueller M.,
Superti-Furga G.;
"IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA.";
Nat. Immunol. 12:624-630(2011).
[10]
FUNCTION, RNA-BINDING, AND MUTAGENESIS OF GLU-33; THR-37; GLN-41;
LYS-48; LYS-150; TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; GLN-288;
LEU-291; ARG-307; ASP-334; PHE-339; LYS-415 AND LYS-426.
PubMed=25092312; DOI=10.1073/pnas.1412842111;
Katibah G.E., Qin Y., Sidote D.J., Yao J., Lambowitz A.M., Collins K.;
"Broad and adaptable RNA structure recognition by the human
interferon-induced tetratricopeptide repeat protein IFIT5.";
Proc. Natl. Acad. Sci. U.S.A. 111:12025-12030(2014).
[11]
FUNCTION, AND INTERACTION WITH MAP3K7; CHUK; IKBKB AND IKBKG.
PubMed=26334375; DOI=10.1016/j.cellsig.2015.08.018;
Zheng C., Zheng Z., Zhang Z., Meng J., Liu Y., Ke X., Hu Q., Wang H.;
"IFIT5 positively regulates NF-kappaB signaling through synergizing
the recruitment of IkappaB kinase (IKK) to TGF-beta-activated kinase 1
(TAK1).";
Cell. Signal. 27:2343-2354(2015).
[12]
X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS), FUNCTION, RNA-BINDING,
DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF 185-TYR-ARG-186;
253-ARG-TYR-254; LYS-257; PHE-284; ARG-294; 337-PHE--PHE-339; ARG-384;
LYS-415 AND 422-LYS--LYS-426.
PubMed=23774268; DOI=10.1038/cr.2013.80;
Feng F., Yuan L., Wang Y.E., Crowley C., Lv Z., Li J., Liu Y.,
Cheng G., Zeng S., Liang H.;
"Crystal structure and nucleotide selectivity of human IFIT5/ISG58.";
Cell Res. 23:1055-1058(2013).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RNA-BINDING,
SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF LEU-291; LYS-302;
ARG-307; LYS-309; 388-PHE-HIS-389; LYS-415; LYS-422 AND LYS-426.
PubMed=23317505; DOI=10.1016/j.molcel.2012.12.015;
Katibah G.E., Lee H.J., Huizar J.P., Vogan J.M., Alber T., Collins K.;
"tRNA binding, structure, and localization of the human interferon-
induced protein IFIT5.";
Mol. Cell 49:743-750(2013).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP-RNA,
FUNCTION, RNA-BINDING, AND MUTAGENESIS OF GLU-33; GLN-41; LYS-150;
TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; ARG-260; HIS-287 AND
GLN-288.
PubMed=23334420; DOI=10.1038/nature11783;
Abbas Y.M., Pichlmair A., Gorna M.W., Superti-Furga G., Nagar B.;
"Structural basis for viral 5'-PPP-RNA recognition by human IFIT
proteins.";
Nature 494:60-64(2013).
-!- FUNCTION: Interferon-induced RNA-binding protein involved in the
human innate immune response. Has a broad and adaptable RNA
structure recognition important for RNA recognition specificity in
antiviral defense. Binds precursor and processed tRNAs as well as
poly-U-tailed tRNA fragments (PubMed:25092312, PubMed:23317505,
PubMed:23774268). Specifically binds single-stranded RNA bearing a
5'-triphosphate group (PPP-RNA), thereby acting as a sensor of
viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack
2'-O-methylation of the 5' cap and bear a 5'-triphosphate group
instead, are specific from viruses, providing a molecular
signature to distinguish between self and non-self mRNAs by the
host during viral infection. Directly binds PPP-RNA in a non-
sequence-specific manner (PubMed:23334420). Also recognizes and
selectively binds AT-rich dsDNA (PubMed:23774268). Additionally,
as a mediator in innate immunity, regulates positively IKK-NFKB
signaling by sinergizing the recruitment of IKK to MAP3K7
(PubMed:26334375). {ECO:0000269|PubMed:23317505,
ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:23774268,
ECO:0000269|PubMed:25092312, ECO:0000269|PubMed:26334375}.
-!- SUBUNIT: Monomer (PubMed:23317505, PubMed:23334420,
PubMed:23774268). Interacts with MAP3K7 and the components of the
IKK core complex CHUK, IKBKB and IKBKG; the interaction synergizes
the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation
(PubMed:26334375). {ECO:0000269|PubMed:23317505,
ECO:0000269|PubMed:23334420, ECO:0000269|PubMed:23774268,
ECO:0000269|PubMed:26334375}.
-!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
{ECO:0000269|PubMed:23317505}. Note=Colocalized with DDX58/RIG-I
at cell surface ruffles. Localizes to actin-rich protrusions from
the apical cell surface.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13325-1; Sequence=Displayed;
Name=2;
IsoId=Q13325-2; Sequence=VSP_056412;
Note=No experimental confirmation available.;
-!- INDUCTION: By interferons (IFNs).
-!- DOMAIN: RNA recognition is mediated by a convoluted intramolecular
fold of the TPR repeats (TPR eddy), which scaffolds unique
additional helices that form an RNA binding cleft (PubMed:23317505
and PubMed:23334420). Undergoes a conformational change upon RNA-
binding: unliganded exists in a more open conformation,
facilitating RNA entry (PubMed:23334420).
{ECO:0000269|PubMed:23334420}.
-!- SIMILARITY: Belongs to the IFIT family. {ECO:0000305}.
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EMBL; U34605; AAA84934.1; -; mRNA.
EMBL; AK293346; BAG56862.1; -; mRNA.
EMBL; AK312358; BAG35276.1; -; mRNA.
EMBL; CR457031; CAG33312.1; -; mRNA.
EMBL; AL353146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW50135.1; -; Genomic_DNA.
EMBL; BC025786; AAH25786.1; -; mRNA.
CCDS; CCDS7403.1; -. [Q13325-1]
PIR; G02058; G02058.
RefSeq; NP_036552.1; NM_012420.2. [Q13325-1]
UniGene; Hs.252839; -.
PDB; 3ZGQ; X-ray; 2.20 A; A=1-482.
PDB; 4HOQ; X-ray; 2.07 A; A=1-482.
PDB; 4HOR; X-ray; 1.86 A; A=1-482.
PDB; 4HOS; X-ray; 2.00 A; A=1-482.
PDB; 4HOT; X-ray; 2.50 A; A=1-482.
PDB; 4J0U; X-ray; 1.97 A; A=1-482.
PDBsum; 3ZGQ; -.
PDBsum; 4HOQ; -.
PDBsum; 4HOR; -.
PDBsum; 4HOS; -.
PDBsum; 4HOT; -.
PDBsum; 4J0U; -.
ProteinModelPortal; Q13325; -.
SMR; Q13325; -.
BioGrid; 117289; 28.
IntAct; Q13325; 13.
STRING; 9606.ENSP00000360860; -.
iPTMnet; Q13325; -.
PhosphoSitePlus; Q13325; -.
BioMuta; IFIT5; -.
DMDM; 6831571; -.
EPD; Q13325; -.
MaxQB; Q13325; -.
PaxDb; Q13325; -.
PeptideAtlas; Q13325; -.
PRIDE; Q13325; -.
TopDownProteomics; Q13325-1; -. [Q13325-1]
Ensembl; ENST00000371795; ENSP00000360860; ENSG00000152778. [Q13325-1]
GeneID; 24138; -.
KEGG; hsa:24138; -.
UCSC; uc010qnh.3; human. [Q13325-1]
CTD; 24138; -.
DisGeNET; 24138; -.
EuPathDB; HostDB:ENSG00000152778.8; -.
GeneCards; IFIT5; -.
HGNC; HGNC:13328; IFIT5.
HPA; HPA037957; -.
HPA; HPA062180; -.
MIM; 616135; gene.
neXtProt; NX_Q13325; -.
OpenTargets; ENSG00000152778; -.
PharmGKB; PA134988392; -.
eggNOG; KOG1124; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00390000013876; -.
HOGENOM; HOG000001558; -.
HOVERGEN; HBG066330; -.
InParanoid; Q13325; -.
OMA; DHKHQIH; -.
OrthoDB; EOG091G06GX; -.
PhylomeDB; Q13325; -.
TreeFam; TF342671; -.
ChiTaRS; IFIT5; human.
GenomeRNAi; 24138; -.
PRO; PR:Q13325; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000152778; -.
CleanEx; HS_IFIT5; -.
Genevisible; Q13325; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000339; F:RNA cap binding; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR024125; Interferon_induced_IFIT5.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR013105; TPR_2.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10271:SF24; PTHR10271:SF24; 1.
Pfam; PF07719; TPR_2; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 5.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50005; TPR; 5.
PROSITE; PS50293; TPR_REGION; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense; Cell membrane;
Cell projection; Complete proteome; Immunity; Innate immunity;
Membrane; Reference proteome; Repeat; RNA-binding; TPR repeat;
tRNA-binding.
CHAIN 1 482 Interferon-induced protein with
tetratricopeptide repeats 5.
/FTId=PRO_0000106351.
REPEAT 51 84 TPR 1.
REPEAT 94 127 TPR 2.
REPEAT 138 173 TPR 3.
REPEAT 181 214 TPR 4.
REPEAT 249 282 TPR 5.
REPEAT 338 371 TPR 6.
REPEAT 376 410 TPR 7.
REPEAT 435 468 TPR 8.
REGION 254 260 Interaction with the 5'-triphosphate
group of PPP-RNA.
SITE 33 33 Interaction with PPP-RNA.
SITE 37 37 Interaction with PPP-RNA.
SITE 41 41 Interaction with PPP-RNA.
SITE 150 150 Interaction with PPP-RNA.
SITE 186 186 Interaction with PPP-RNA.
SITE 250 250 Interaction with PPP-RNA.
SITE 288 288 Interaction with the 5'-triphosphate
group of PPP-RNA.
VAR_SEQ 158 205 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056412.
MUTAGEN 33 33 E->A: No effect on RNA-binding but
changes size profile of RNA bound.
Reduces PPP-RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 37 37 T->A,V: No effect on RNA-binding but
changes size profile of RNA bound.
{ECO:0000269|PubMed:25092312}.
MUTAGEN 37 37 T->V: Abolishes PPP-RNA-binding.
MUTAGEN 41 41 Q->E: No effect on RNA-binding but
changes size profile of RNA bound.
Abolishes PPP-RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 48 48 K->A,E: Inhibits RNA-binding.
{ECO:0000269|PubMed:25092312}.
MUTAGEN 150 150 K->M: Abolishes PPP-RNA-binding.
{ECO:0000269|PubMed:23334420}.
MUTAGEN 150 150 K->N,E: Inhibits RNA-binding.
{ECO:0000269|PubMed:25092312}.
MUTAGEN 150 150 K->R: Reduces RNA-binding.
{ECO:0000269|PubMed:25092312}.
MUTAGEN 156 156 Y->F,A: No effect on RNA-binding. Reduces
PPP-RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 185 186 YR->AE: Reduces binding to RNA and DNA.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 186 186 R->H,A: Abolishes RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 250 250 Y->F: No effect on RNA-binding but
changes size profile of RNA bound.
Abolishes PPP-RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 253 254 RY->EA: Reduces binding to RNA and DNA.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 253 253 R->M: Abolishes RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 254 254 Y->F: Abolishes RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 257 257 K->E: Reduces binding to RNA and DNA.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 260 260 R->E: Abolishes PPP-RNA-binding.
{ECO:0000269|PubMed:23334420}.
MUTAGEN 284 284 F->A: Strongly reduces binding to dsDNA.
No effect on ssRNA binding.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 287 287 H->A: Reduces PPP-RNA-binding.
{ECO:0000269|PubMed:23334420}.
MUTAGEN 288 288 Q->E: Abolishes RNA-binding.
{ECO:0000269|PubMed:23334420,
ECO:0000269|PubMed:25092312}.
MUTAGEN 291 291 L->A: No effect RNA-binding.
{ECO:0000269|PubMed:23317505,
ECO:0000269|PubMed:25092312}.
MUTAGEN 294 294 R->E: Strongly reduces binding to dsDNA.
No effect on ssRNA binding.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 302 302 K->A: Reduces RNA-binding.
{ECO:0000269|PubMed:23317505}.
MUTAGEN 307 307 R->A: Reduces RNA-binding. 25 fold
reduction in tRNA-binding.
{ECO:0000269|PubMed:23317505,
ECO:0000269|PubMed:25092312}.
MUTAGEN 309 309 K->A: Reduces RNA-binding.
{ECO:0000269|PubMed:23317505}.
MUTAGEN 334 334 D->A: No effect on RNA-binding but
changes size profile of RNA bound.
{ECO:0000269|PubMed:25092312}.
MUTAGEN 337 339 FAF->AAA: Reduces binding to RNA and DNA.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 337 337 F->A: Abolishes PPP-RNA-binding.
{ECO:0000269|PubMed:23334420}.
MUTAGEN 339 339 F->A: Reduces RNA-binding.
{ECO:0000269|PubMed:25092312}.
MUTAGEN 384 384 R->E: Reduces binding to RNA and DNA and
impairs antiviral activity; when
associated with E-415.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 388 389 FH->AA: Reduces RNA-binding.
{ECO:0000269|PubMed:23317505}.
MUTAGEN 415 415 K->A: Reduces RNA-binding. 25 fold
reduction in tRNA-binding.
{ECO:0000269|PubMed:23317505,
ECO:0000269|PubMed:25092312}.
MUTAGEN 415 415 K->E: Reduces binding to RNA and DNA and
impairs antiviral activity; when
associated with E-384.
{ECO:0000269|PubMed:23774268}.
MUTAGEN 422 426 KLSTK->ELSTE: Reduces binding to RNA and
DNA. {ECO:0000269|PubMed:23774268}.
MUTAGEN 422 422 K->A: Reduced RNA-binding.
{ECO:0000269|PubMed:23317505,
ECO:0000269|PubMed:25092312}.
MUTAGEN 426 426 K->A: Reduces RNA-binding. 5 fold
reduction in tRNA-binding.
{ECO:0000269|PubMed:23317505}.
CONFLICT 215 215 S -> N (in Ref. 3; CAG33312).
{ECO:0000305}.
CONFLICT 449 449 G -> R (in Ref. 2; BAG35276).
{ECO:0000305}.
HELIX 3 15 {ECO:0000244|PDB:4HOR}.
HELIX 19 21 {ECO:0000244|PDB:4HOR}.
HELIX 26 28 {ECO:0000244|PDB:4HOR}.
HELIX 31 44 {ECO:0000244|PDB:4HOR}.
STRAND 46 48 {ECO:0000244|PDB:4HOQ}.
HELIX 50 63 {ECO:0000244|PDB:4HOR}.
HELIX 67 84 {ECO:0000244|PDB:4HOR}.
HELIX 86 88 {ECO:0000244|PDB:4HOR}.
HELIX 91 93 {ECO:0000244|PDB:4HOR}.
HELIX 94 106 {ECO:0000244|PDB:4HOR}.
HELIX 110 126 {ECO:0000244|PDB:4HOR}.
STRAND 130 133 {ECO:0000244|PDB:4HOR}.
HELIX 138 150 {ECO:0000244|PDB:4HOR}.
HELIX 153 155 {ECO:0000244|PDB:4HOR}.
HELIX 156 169 {ECO:0000244|PDB:4HOR}.
HELIX 174 189 {ECO:0000244|PDB:4HOR}.
STRAND 193 195 {ECO:0000244|PDB:4HOR}.
HELIX 201 210 {ECO:0000244|PDB:4HOR}.
HELIX 215 227 {ECO:0000244|PDB:4HOR}.
HELIX 231 244 {ECO:0000244|PDB:4HOR}.
HELIX 249 261 {ECO:0000244|PDB:4HOR}.
HELIX 265 278 {ECO:0000244|PDB:4HOR}.
HELIX 283 303 {ECO:0000244|PDB:4HOR}.
TURN 304 306 {ECO:0000244|PDB:4HOR}.
HELIX 310 333 {ECO:0000244|PDB:4HOR}.
HELIX 338 350 {ECO:0000244|PDB:4HOR}.
HELIX 354 365 {ECO:0000244|PDB:4HOR}.
HELIX 372 388 {ECO:0000244|PDB:4HOR}.
HELIX 393 406 {ECO:0000244|PDB:4HOR}.
STRAND 408 410 {ECO:0000244|PDB:4HOR}.
HELIX 413 430 {ECO:0000244|PDB:4HOR}.
HELIX 435 447 {ECO:0000244|PDB:4HOR}.
HELIX 451 464 {ECO:0000244|PDB:4HOR}.
HELIX 469 480 {ECO:0000244|PDB:4HOR}.
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


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