IFIT1_HUMAN
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 03-AUG-2022, entry version 201.
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; 64.
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; P09914; -.
DR PeptideAtlas; P09914; -.
DR PRIDE; P09914; -.
DR ProteomicsDB; 12754; -.
DR ProteomicsDB; 52277; -. [P09914-1]
DR Antibodypedia; 30269; 263 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 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; HFTWELS; -.
DR OrthoDB; 460948at2759; -.
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; 11 hits in 1077 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 200 other tissues.
DR Genevisible; P09914; HS.
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; IEP:ARUK-UCL.
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:0050688; P:regulation of defense response to virus; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; IDA:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR024121; Interferon-induced_IFIT1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10271:SF30; PTHR10271:SF30; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 3.
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
