IFIT1_MOUSE
ID IFIT1_MOUSE Reviewed; 463 AA.
AC Q64282; Q99L77;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 1;
DE Short=IFIT-1;
DE AltName: Full=Glucocorticoid-attenuated response gene 16 protein;
DE Short=GARG-16;
DE AltName: Full=Interferon-induced 56 kDa protein;
DE Short=IFI-56K;
DE Short=P56;
GN Name=Ifit1; Synonyms=Garg16, Ifi56, Isg56;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7896268; DOI=10.1006/geno.1994.1591;
RA Bluyssen H.A., Vlietstra R.J., Faber P.W., Smit E.M., Hagemeijer A.,
RA Trapman J.;
RT "Structure, chromosome localization, and regulation of expression of the
RT interferon-regulated mouse Ifi54/Ifi56 gene family.";
RL Genomics 24:137-148(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=8660659; DOI=10.1006/abbi.1996.0256;
RA Smith J.B., Herschman H.R.;
RT "The glucocorticoid attenuated response genes GARG-16, GARG-39, and GARG-
RT 49/IRG2 encode inducible proteins containing multiple tetratricopeptide
RT repeat domains.";
RL Arch. Biochem. Biophys. 330:290-300(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 INTERACTION WITH EIF3C.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH EEF1A1, AND SUBCELLULAR LOCATION.
RX PubMed=19856081; DOI=10.1007/s11010-009-0289-9;
RA Li H.T., Su Y.P., Cheng T.M., Xu J.M., Liao J., Chen J.C., Ji C.Y.,
RA Ai G.P., Wang J.P.;
RT "The interaction between interferon-induced protein with tetratricopeptide
RT repeats-1 and eukaryotic elongation factor-1A.";
RL Mol. Cell. Biochem. 337:101-110(2010).
RN [10]
RP FUNCTION.
RX PubMed=21085181; DOI=10.1038/nature09489;
RA Daffis S., Szretter K.J., Schriewer J., Li J., Youn S., Errett J.,
RA Lin T.Y., Schneller S., Zust R., Dong H., Thiel V., Sen G.C., Fensterl V.,
RA Klimstra W.B., Pierson T.C., Buller R.M., Gale M. Jr., Shi P.Y.,
RA Diamond M.S.;
RT "2'-O methylation of the viral mRNA cap evades host restriction by IFIT
RT family members.";
RL Nature 468:452-456(2010).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=22589727; DOI=10.1371/journal.ppat.1002698;
RA Szretter K.J., Daniels B.P., Cho H., Gainey M.D., Yokoyama W.M.,
RA Gale M. Jr., Virgin H.W., Klein R.S., Sen G.C., Diamond M.S.;
RT "2'-o methylation of the viral mRNA cap by west nile virus evades ifit1-
RT dependent and -independent mechanisms of host restriction in vivo.";
RL PLoS Pathog. 8:E1002698-E1002698(2012).
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). {ECO:0000269|PubMed:21085181,
CC ECO:0000269|PubMed:22589727}.
CC -!- SUBUNIT: Component of an interferon-dependent multiprotein complex, at
CC least composed of IFIT1, IFIT2 and IFIT3. Interacts with IFIT2 and
CC IFIT3 (By similarity). Interacts with EIF3E (By similarity). Interacts
CC (via TPR repeats 1-4) with RPL15 (By similarity). Interacts with
CC STING1/MITA and disrupts its interaction with MAVS or TBK1 (By
CC similarity). Interacts with EIF3C. Interacts (via TPR repeats 4-7) with
CC EEF1A1. {ECO:0000250, ECO:0000269|PubMed:16023166,
CC ECO:0000269|PubMed:19856081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}.
CC -!- INDUCTION: By type I interferons, dsRNAs and viruses.
CC {ECO:0000269|PubMed:8660659}.
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:0000250}.
CC -!- PTM: ISGylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IFIT family. {ECO:0000305}.
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DR EMBL; S77715; AAB33831.2; -; Genomic_DNA.
DR EMBL; S77714; AAB33831.2; JOINED; Genomic_DNA.
DR EMBL; U43084; AAC52625.1; -; mRNA.
DR EMBL; AK150352; BAE29489.1; -; mRNA.
DR EMBL; AK150424; BAE29547.1; -; mRNA.
DR EMBL; AK150609; BAE29700.1; -; mRNA.
DR EMBL; AK151125; BAE30133.1; -; mRNA.
DR EMBL; AK151158; BAE30163.1; -; mRNA.
DR EMBL; AK151278; BAE30265.1; -; mRNA.
DR EMBL; AK151298; BAE30281.1; -; mRNA.
DR EMBL; AK153184; BAE31785.1; -; mRNA.
DR EMBL; AK157848; BAE34228.1; -; mRNA.
DR EMBL; CT010226; CAJ18434.1; -; mRNA.
DR EMBL; CH466534; EDL41756.1; -; Genomic_DNA.
DR EMBL; BC003768; AAH03768.1; -; mRNA.
DR CCDS; CCDS29766.1; -.
DR PIR; B55508; B55508.
DR RefSeq; NP_032357.2; NM_008331.3.
DR AlphaFoldDB; Q64282; -.
DR SMR; Q64282; -.
DR BioGRID; 200525; 8.
DR IntAct; Q64282; 1.
DR STRING; 10090.ENSMUSP00000099888; -.
DR iPTMnet; Q64282; -.
DR PhosphoSitePlus; Q64282; -.
DR SwissPalm; Q64282; -.
DR EPD; Q64282; -.
DR MaxQB; Q64282; -.
DR PaxDb; Q64282; -.
DR PRIDE; Q64282; -.
DR ProteomicsDB; 267274; -.
DR DNASU; 15957; -.
DR Ensembl; ENSMUST00000102824; ENSMUSP00000099888; ENSMUSG00000034459.
DR GeneID; 15957; -.
DR KEGG; mmu:15957; -.
DR UCSC; uc008hgt.1; mouse.
DR CTD; 3434; -.
DR MGI; MGI:99450; Ifit1.
DR VEuPathDB; HostDB:ENSMUSG00000034459; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00950000182946; -.
DR HOGENOM; CLU_043482_1_0_1; -.
DR InParanoid; Q64282; -.
DR OMA; ANPSRYR; -.
DR OrthoDB; 460948at2759; -.
DR PhylomeDB; Q64282; -.
DR TreeFam; TF342671; -.
DR BioGRID-ORCS; 15957; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ifit1; mouse.
DR PRO; PR:Q64282; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q64282; protein.
DR Bgee; ENSMUSG00000034459; Expressed in small intestine Peyer's patch and 140 other tissues.
DR Genevisible; Q64282; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IDA:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Immunity; Innate immunity; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; TPR repeat; Ubl conjugation.
FT CHAIN 1..463
FT /note="Interferon-induced protein with tetratricopeptide
FT repeats 1"
FT /id="PRO_0000106345"
FT REPEAT 52..85
FT /note="TPR 1"
FT REPEAT 92..126
FT /note="TPR 2"
FT REPEAT 136..171
FT /note="TPR 3"
FT REPEAT 174..207
FT /note="TPR 4"
FT REPEAT 209..241
FT /note="TPR 5"
FT REPEAT 242..275
FT /note="TPR 6"
FT REPEAT 294..328
FT /note="TPR 7"
FT REPEAT 329..362
FT /note="TPR 8"
FT REPEAT 367..401
FT /note="TPR 9"
FT REPEAT 426..459
FT /note="TPR 10"
FT REGION 247..253
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 148
FT /note="Interaction with PPP-RNA"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Interaction with PPP-RNA"
FT /evidence="ECO:0000250"
FT SITE 243
FT /note="Interaction with PPP-RNA"
FT /evidence="ECO:0000250"
FT SITE 281
FT /note="Interaction with the 5'-triphosphate group of PPP-
FT RNA"
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="I -> V (in Ref. 1; AAB33831 and 2; AAC52625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 53737 MW; 166FAB371F7B6D2A CRC64;
MGENADGDQV MENLLQLRCH FTWKLLFENN DIPDLEVRIS EQVQFLDIKN PLGMHNLLAY
VRHLKGQQDE ALQSLKEAEA LIQSEQLSKR SLATWGNCAW LHYHRGSLAE AQIYLDKVEK
VCKEFSSPFR YRLECAEMDC EEGWALLKCG GGNYKQAMAC FAKALKVEPE NPEYNTGYAV
VAYRQDLDDN FISLEPLRKA VRLNPEDPYL KVLLALKLQD LGEHVEAEAH IEEALSSTSC
QSYVIRYAAK YFRRKHRVDK ALHLLNRALQ ASPSSGYLHY QKGLCYKQQI SQLRTSRNRQ
PRRQDNVQEL AQQAIHEFQE TLKLRPTFEM AYVCMAEVQA EIHQYEEAER NFQKALNNKT
LVAHIEQDIH LRYGRFLQFH KQSEDKAITL YLKGLKVEEK SFAWRKLLTA LEKVAERRVC
QNVHLVESTS LLGLVYKLKG QEKNALFYYE KALRLTGEMN PAF
