ID IFIT1_HUMAN Reviewed; 478 AA. AC P09914; B3KS50; D3DR31; Q5T7J1; Q96QM5; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 1; DE Short=IFIT-1; DE AltName: Full=Interferon-induced 56 kDa protein; DE Short=IFI-56K; DE Short=P56; GN Name=IFIT1; Synonyms=G10P1, IFI56, IFNAI1, ISG56; 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), AND INDUCTION. RX PubMed=3753936; DOI=10.1111/j.1432-1033.1986.tb09452.x; RA Wathelet M., Moutschen S., Defilippi P., Cravador A., Collet M., Huez G., RA Content J.; RT "Molecular cloning, full-length sequence and preliminary characterization RT of a 56-kDa protein induced by human interferons."; RL Eur. J. Biochem. 155:11-17(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Small intestine, and Synovium; 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 [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., 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=Prostate; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 413-478. RX PubMed=6186990; DOI=10.1093/nar/11.5.1213; RA Chebath J., Merlin G., Metz R., Benech P., Revel M.; RT "Interferon-induced 56,000 Mr protein and its mRNA in human cells: RT molecular cloning and partial sequence of the cDNA."; RL Nucleic Acids Res. 11:1213-1226(1983). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2. RX PubMed=3121313; DOI=10.1111/j.1432-1033.1987.tb13614.x; RA Wathelet M.G., Clauss I.M., Nols C.B., Content J., Huez G.A.; RT "New inducers revealed by the promoter sequence analysis of two interferon- RT activated human genes."; RL Eur. J. Biochem. 169:313-321(1987). RN [9] RP SIMILARITY TO IFI-54K. RX PubMed=3360121; DOI=10.1016/0014-5793(88)80724-5; RA Wathelet M.G., Clauss I.M., Content J., Huez G.A.; RT "The IFI-56K and IFI-54K interferon-inducible human genes belong to the RT same gene family."; RL FEBS Lett. 231:164-171(1988). RN [10] RP ISGYLATION. RX PubMed=16009940; DOI=10.1073/pnas.0504754102; RA Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.; RT "Human ISG15 conjugation targets both IFN-induced and constitutively RT expressed proteins functioning in diverse cellular pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005). RN [11] RP INTERACTION WITH EIF3E. RX PubMed=16023166; DOI=10.1016/j.virol.2005.06.011; RA Terenzi F., Pal S., Sen G.C.; RT "Induction and mode of action of the viral stress-inducible murine RT proteins, P56 and P54."; RL Virology 340:116-124(2005). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH E1 PROTEINS OF HPV RP TYPES 11; 18 AND 31 (MICROBIAL INFECTION). RX PubMed=19008854; DOI=10.1038/emboj.2008.241; RA Terenzi F., Saikia P., Sen G.C.; RT "Interferon-inducible protein, P56, inhibits HPV DNA replication by binding RT to the viral protein E1."; RL EMBO J. 27:3311-3321(2008). RN [13] RP FUNCTION, INTERACTION WITH STING1/MITA, AND PHOSPHORYLATION. RX PubMed=19416887; DOI=10.1073/pnas.0900818106; RA Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y., RA Yang F., Shu H.B.; RT "ISG56 is a negative-feedback regulator of virus-triggered signaling and RT cellular antiviral response."; RL Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009). RN [14] 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 [15] RP INTERACTION WITH RPL15. RX PubMed=21612406; DOI=10.1089/dna.2010.1149; RA Hsu Y.A., Lin H.J., Sheu J.J., Shieh F.K., Chen S.Y., Lai C.H., Tsai F.J., RA Wan L., Chen B.H.; RT "A novel interaction between interferon-inducible protein p56 and ribosomal RT protein L15 in gastric cancer cells."; RL DNA Cell Biol. 30:671-679(2011). RN [16] RP INTERACTION WITH IFIT2. RX PubMed=21190939; DOI=10.1074/jbc.m110.207068; RA Stawowczyk M., Van Scoy S., Kumar K.P., Reich N.C.; RT "The interferon stimulated gene 54 promotes apoptosis."; RL J. Biol. Chem. 286:7257-7266(2011). RN [17] 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 [18] RP FUNCTION. RX PubMed=21976647; DOI=10.1128/jvi.05633-11; RA Raychoudhuri A., Shrivastava S., Steele R., Kim H., Ray R., Ray R.B.; RT "ISG56 and IFITM1 proteins inhibit hepatitis C virus replication."; RL J. Virol. 85:12881-12889(2011). RN [19] RP REVIEW ON FUNCTION. RX PubMed=21685951; DOI=10.1038/ni.2061; RA Ablasser A., Hornung V.; RT "Where, in antiviral defense, does IFIT1 fit?"; RL Nat. Immunol. 12:588-590(2011). RN [20] RP SUBCELLULAR LOCATION, INTERACTION WITH IFIT2 AND IFIT3, AND 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 [21] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-279, FUNCTION, RNA-BINDING, AND RP MUTAGENESIS OF ASP-34; ARG-38; GLN-42; LYS-151; TYR-157; ARG-187 AND RP ARG-255. 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 antiviral RNA-binding protein that CC specifically binds single-stranded RNA bearing a 5'-triphosphate group CC (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and CC inhibiting expression of viral messenger RNAs. Single-stranded PPP- CC RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'- CC triphosphate group instead, are specific from viruses, providing a CC molecular signature to distinguish between self and non-self mRNAs by CC the host during viral infection. Directly binds PPP-RNA in a non- CC sequence-specific manner. Viruses evolved several ways to evade this CC restriction system such as encoding their own 2'-O-methylase for their CC mRNAs or by stealing host cap containing the 2'-O-methylation (cap CC snatching mechanism). Exhibits antiviral activity against several CC viruses including human papilloma and hepatitis C viruses. CC {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:19416887, CC ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:23334420}. CC -!- SUBUNIT: Component of an interferon-dependent multiprotein complex, at CC least composed of IFIT1, IFIT2 and IFIT3. Interacts (via TPR repeats 4- CC 7) with EEF1A1 (By similarity). Interacts with EIF3C (By similarity). CC Interacts with IFIT2 and IFIT3. Interacts (via TPR repeats 1-4) with CC RPL15. Interacts with STING1/MITA and disrupts its interaction with CC MAVS or TBK1. Interacts with EIF3E. {ECO:0000250, CC ECO:0000269|PubMed:16023166, ECO:0000269|PubMed:19416887, CC ECO:0000269|PubMed:21190939, ECO:0000269|PubMed:21612406, CC ECO:0000269|PubMed:21642987}. CC -!- SUBUNIT: (Microbial infection) Interacts (via TPR repeat 2) with E1 CC proteins of HPV types 11, 18 and 3; this interaction blocks E1 helicase CC activity and viral replication. {ECO:0000269|PubMed:19008854}. CC -!- INTERACTION: CC P09914; P09913: IFIT2; NbExp=6; IntAct=EBI-745117, EBI-3507167; CC P09914; O14879: IFIT3; NbExp=12; IntAct=EBI-745117, EBI-745127; CC P09914; Q86WV6: STING1; NbExp=3; IntAct=EBI-745117, EBI-2800345; CC P09914; P06789: E1; Xeno; NbExp=8; IntAct=EBI-745117, EBI-7015660; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19008854, CC ECO:0000269|PubMed:21642987}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P09914-1; Sequence=Displayed; CC Name=2; CC IsoId=P09914-2; Sequence=VSP_054831; CC -!- INDUCTION: By type I interferons, dsRNAs and viruses. CC {ECO:0000269|PubMed:3753936}. 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. {ECO:0000250}. CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:19416887}. CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16009940}. 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; X03557; CAA27244.1; -; mRNA. DR EMBL; BT006667; AAP35313.1; -; mRNA. DR EMBL; AK092813; BAG52612.1; -; mRNA. DR EMBL; AK314588; BAG37163.1; -; mRNA. DR EMBL; AL353146; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW50136.1; -; Genomic_DNA. DR EMBL; CH471066; EAW50137.1; -; Genomic_DNA. DR EMBL; CH471066; EAW50138.1; -; Genomic_DNA. DR EMBL; BC007091; AAH07091.1; -; mRNA. DR EMBL; X06559; CAA29802.1; -; Genomic_DNA. DR CCDS; CCDS31243.1; -. [P09914-1] DR CCDS; CCDS59220.1; -. [P09914-2] DR PIR; A25407; A25407. DR RefSeq; NP_001257857.1; NM_001270928.1. [P09914-2] DR RefSeq; NP_001257858.1; NM_001270929.1. [P09914-2] DR RefSeq; NP_001257859.1; NM_001270930.1. [P09914-2] DR RefSeq; NP_001539.3; NM_001548.4. [P09914-1] DR PDB; 4HOU; X-ray; 1.95 A; A/B=7-279. DR PDB; 5UDI; X-ray; 1.58 A; A=1-478. DR PDB; 5UDJ; X-ray; 1.69 A; A=1-478. DR PDB; 5UDK; X-ray; 1.65 A; A=1-478. DR PDB; 5UDL; X-ray; 1.65 A; A=1-478. DR PDB; 5W5H; X-ray; 2.79 A; A/C=1-478. DR PDB; 5W5I; X-ray; 2.65 A; A/C=1-478. DR PDB; 6C6K; X-ray; 2.54 A; A/B=7-471. DR PDBsum; 4HOU; -. DR PDBsum; 5UDI; -. DR PDBsum; 5UDJ; -. DR PDBsum; 5UDK; -. DR PDBsum; 5UDL; -. DR PDBsum; 5W5H; -. DR PDBsum; 5W5I; -. DR PDBsum; 6C6K; -. DR AlphaFoldDB; P09914; -. DR SMR; P09914; -. DR BioGRID; 109659; 70. DR DIP; DIP-37898N; -. DR IntAct; P09914; 48. DR MINT; P09914; -. DR STRING; 9606.ENSP00000360869; -. DR iPTMnet; P09914; -. DR PhosphoSitePlus; P09914; -. DR BioMuta; IFIT1; -. DR DMDM; 116242522; -. DR EPD; P09914; -. DR jPOST; P09914; -. DR MassIVE; P09914; -. DR MaxQB; P09914; -. DR PaxDb; 9606-ENSP00000360869; -. DR PeptideAtlas; P09914; -. DR ProteomicsDB; 12754; -. DR ProteomicsDB; 52277; -. [P09914-1] DR Pumba; P09914; -. DR Antibodypedia; 30269; 289 antibodies from 31 providers. DR CPTC; P09914; 1 antibody. DR DNASU; 3434; -. DR Ensembl; ENST00000371804.4; ENSP00000360869.3; ENSG00000185745.10. [P09914-1] DR Ensembl; ENST00000546318.2; ENSP00000441968.1; ENSG00000185745.10. [P09914-2] DR GeneID; 3434; -. DR KEGG; hsa:3434; -. DR MANE-Select; ENST00000371804.4; ENSP00000360869.3; NM_001548.5; NP_001539.3. DR UCSC; uc001kgi.5; human. [P09914-1] DR AGR; HGNC:5407; -. DR CTD; 3434; -. DR DisGeNET; 3434; -. DR GeneCards; IFIT1; -. DR HGNC; HGNC:5407; IFIT1. DR HPA; ENSG00000185745; Low tissue specificity. DR MIM; 147690; gene. DR neXtProt; NX_P09914; -. DR OpenTargets; ENSG00000185745; -. DR PharmGKB; PA29648; -. DR VEuPathDB; HostDB:ENSG00000185745; -. DR eggNOG; KOG1124; Eukaryota. DR GeneTree; ENSGT00950000182946; -. DR HOGENOM; CLU_043482_1_0_1; -. DR InParanoid; P09914; -. DR OMA; DHQVKDS; -. DR OrthoDB; 5401272at2759; -. DR PhylomeDB; P09914; -. DR TreeFam; TF342671; -. DR PathwayCommons; P09914; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SignaLink; P09914; -. DR BioGRID-ORCS; 3434; 12 hits in 1155 CRISPR screens. DR ChiTaRS; IFIT1; human. DR GeneWiki; IFIT1; -. DR GenomeRNAi; 3434; -. DR Pharos; P09914; Tbio. DR PRO; PR:P09914; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P09914; Protein. DR Bgee; ENSG00000185745; Expressed in pons and 202 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043657; C:host cell; IEA:GOC. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProt. DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IDA:BHF-UCL. DR GO; GO:0071357; P:cellular response to type I interferon; IDA:BHF-UCL. DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central. DR GO; GO:0019060; P:intracellular transport of viral protein in host cell; IDA:BHF-UCL. DR GO; GO:0051097; P:negative regulation of helicase activity; IDA:BHF-UCL. DR GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL. DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB. DR GO; GO:0045070; P:positive regulation of viral genome replication; IDA:BHF-UCL. DR GO; GO:0009615; P:response to virus; IDA:BHF-UCL. 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:SF16; INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS 1; 1. DR Pfam; PF13424; TPR_12; 1. DR Pfam; PF14559; TPR_19; 1. DR Pfam; PF07719; TPR_2; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 6. DR SUPFAM; SSF48452; TPR-like; 3. DR PROSITE; PS50005; TPR; 6. DR PROSITE; PS50293; TPR_REGION; 3. DR Genevisible; P09914; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; Cytoplasm; KW Host-virus interaction; Immunity; Innate immunity; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; TPR repeat; Ubl conjugation. FT CHAIN 1..478 FT /note="Interferon-induced protein with tetratricopeptide FT repeats 1" FT /id="PRO_0000106344" FT REPEAT 52..85 FT /note="TPR 1" FT REPEAT 95..128 FT /note="TPR 2" FT REPEAT 139..174 FT /note="TPR 3" FT REPEAT 183..216 FT /note="TPR 4" FT REPEAT 218..249 FT /note="TPR 5" FT REPEAT 251..284 FT /note="TPR 6" FT REPEAT 305..339 FT /note="TPR 7" FT REPEAT 340..373 FT /note="TPR 8" FT REPEAT 378..412 FT /note="TPR 9" FT REPEAT 437..470 FT /note="TPR 10" FT REGION 256..262 FT /note="Interaction with the 5'-triphosphate group of PPP- FT RNA" FT /evidence="ECO:0000250" FT SITE 34 FT /note="Interaction with PPP-RNA" FT /evidence="ECO:0000250" FT SITE 42 FT /note="Interaction with PPP-RNA" FT /evidence="ECO:0000250" FT SITE 151 FT /note="Interaction with PPP-RNA" FT /evidence="ECO:0000250" FT SITE 187 FT /note="Interaction with PPP-RNA" FT /evidence="ECO:0000250" FT SITE 252 FT /note="Interaction with PPP-RNA" FT /evidence="ECO:0000250" FT SITE 290 FT /note="Interaction with the 5'-triphosphate group of PPP- FT RNA" FT /evidence="ECO:0000250" FT VAR_SEQ 1..31 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054831" FT VARIANT 131 FT /note="P -> H (in dbSNP:rs11553019)" FT /id="VAR_052614" FT MUTAGEN 34 FT /note="D->A: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 38 FT /note="R->M: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 42 FT /note="Q->E: Reduced PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 151 FT /note="K->M: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 157 FT /note="Y->F: Reduced PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 187 FT /note="R->H: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT MUTAGEN 255 FT /note="R->M: Abolishes PPP-RNA-binding." FT /evidence="ECO:0000269|PubMed:23334420" FT CONFLICT 198 FT /note="H -> Y (in Ref. 3; BAG52612)" FT /evidence="ECO:0000305" FT CONFLICT 383 FT /note="H -> Y (in Ref. 1; CAA27244)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="H -> R (in Ref. 3; BAG52612)" FT /evidence="ECO:0000305" FT HELIX 9..16 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 32..45 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 52..64 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 68..85 FT /evidence="ECO:0007829|PDB:5UDI" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:6C6K" FT HELIX 94..108 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 111..127 FT /evidence="ECO:0007829|PDB:5UDI" FT STRAND 131..134 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 139..151 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 157..168 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 175..191 FT /evidence="ECO:0007829|PDB:5UDI" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 203..212 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 217..229 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 233..244 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 250..264 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 267..280 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 285..305 FT /evidence="ECO:0007829|PDB:5UDI" FT TURN 306..308 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 312..335 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 340..352 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 356..367 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 376..390 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 395..407 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 413..432 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 437..449 FT /evidence="ECO:0007829|PDB:5UDI" FT HELIX 453..466 FT /evidence="ECO:0007829|PDB:5UDI" SQ SEQUENCE 478 AA; 55360 MW; EF46E652A366E721 CRC64; MSTNGDDHQV KDSLEQLRCH FTWELSIDDD EMPDLENRVL DQIEFLDTKY SVGIHNLLAY VKHLKGQNEE ALKSLKEAEN LMQEEHDNQA NVRSLVTWGN FAWMYYHMGR LAEAQTYLDK VENICKKLSN PFRYRMECPE IDCEEGWALL KCGGKNYERA KACFEKVLEV DPENPESSAG YAISAYRLDG FKLATKNHKP FSLLPLRQAV RLNPDNGYIK VLLALKLQDE GQEAEGEKYI EEALANMSSQ TYVFRYAAKF YRRKGSVDKA LELLKKALQE TPTSVLLHHQ IGLCYKAQMI QIKEATKGQP RGQNREKLDK MIRSAIFHFE SAVEKKPTFE VAHLDLARMY IEAGNHRKAE ENFQKLLCMK PVVEETMQDI HFHYGRFQEF QKKSDVNAII HYLKAIKIEQ ASLTRDKSIN SLKKLVLRKL RRKALDLESL SLLGFVYKLE GNMNEALEYY ERALRLAADF ENSVRQGP //