IFIT2_MOUSE
ID IFIT2_MOUSE Reviewed; 472 AA.
AC Q64112; Q62385;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 2;
DE Short=IFIT-2;
DE AltName: Full=Glucocorticoid-attenuated response gene 39 protein;
DE Short=GARG-39;
DE AltName: Full=Interferon-induced 54 kDa protein;
DE Short=IFI-54K;
DE Short=P54;
GN Name=Ifit2; Synonyms=Garg39, Ifi54, Isg54;
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].
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 INDUCTION, AND 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
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 [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=22615570; DOI=10.1371/journal.ppat.1002712;
RA Fensterl V., Wetzel J.L., Ramachandran S., Ogino T., Stohlman S.A.,
RA Bergmann C.C., Diamond M.S., Virgin H.W., Sen G.C.;
RT "Interferon-induced Ifit2/ISG54 protects mice from lethal VSV
RT neuropathogenesis.";
RL PLoS Pathog. 8:E1002712-E1002712(2012).
CC -!- FUNCTION: IFN-induced antiviral protein which inhibits expression of
CC viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose
CC 2'-O-methylation would provide a molecular signature to distinguish
CC between self and non-self mRNAs by the host during viral infection.
CC Viruses evolved several ways to evade this restriction system such as
CC encoding their own 2'-O-methylase for their mRNAs or by stealing host
CC cap containing the 2'-O-methylation (cap snatching mechanism). Binds
CC AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding
CC is required for antiviral activity. Can promote apoptosis.
CC {ECO:0000269|PubMed:21085181, ECO:0000269|PubMed:22615570}.
CC -!- SUBUNIT: Domain-swapped homodimer. Component of an interferon-dependent
CC multiprotein complex, at least composed of IFIT1, IFIT2 and IFIT3.
CC Interacts with IFIT1 and IFIT3. Interacts with STING1/MITA and disrupts
CC its interaction with MAVS or TBK1 (By similarity). Interacts with
CC EIF3C. {ECO:0000250, ECO:0000269|PubMed:16023166}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}.
CC -!- INDUCTION: By type I interferons, dsRNAs and viruses.
CC {ECO:0000269|PubMed:16023166}.
CC -!- DOMAIN: The C-terminal part folds into a super-helical structure and
CC has an extensively positively-charged nucleotide-binding channel on its
CC inner surface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IFIT family. {ECO:0000305}.
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DR EMBL; S77713; AAB33830.1; -; Genomic_DNA.
DR EMBL; S77710; AAB33830.1; JOINED; Genomic_DNA.
DR EMBL; U43085; AAC52626.1; -; mRNA.
DR PIR; A55508; A55508.
DR PIR; S71355; S71355.
DR RefSeq; NP_032358.1; NM_008332.3.
DR RefSeq; XP_006526768.1; XM_006526705.2.
DR RefSeq; XP_006526769.1; XM_006526706.3.
DR AlphaFoldDB; Q64112; -.
DR SMR; Q64112; -.
DR BioGRID; 200526; 4.
DR STRING; 10090.ENSMUSP00000099890; -.
DR PhosphoSitePlus; Q64112; -.
DR MaxQB; Q64112; -.
DR PaxDb; Q64112; -.
DR PeptideAtlas; Q64112; -.
DR PRIDE; Q64112; -.
DR ProteomicsDB; 267275; -.
DR DNASU; 15958; -.
DR GeneID; 15958; -.
DR KEGG; mmu:15958; -.
DR CTD; 3433; -.
DR MGI; MGI:99449; Ifit2.
DR eggNOG; KOG1124; Eukaryota.
DR InParanoid; Q64112; -.
DR OrthoDB; 460948at2759; -.
DR PhylomeDB; Q64112; -.
DR BioGRID-ORCS; 15958; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ifit2; mouse.
DR PRO; PR:Q64112; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64112; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035457; P:cellular response to interferon-alpha; 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:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR024124; Interferon-induced_IFIT2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10271:SF4; PTHR10271:SF4; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antiviral defense; Apoptosis; Cytoplasm;
KW Endoplasmic reticulum; Immunity; Innate immunity; Reference proteome;
KW Repeat; RNA-binding; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09913"
FT CHAIN 2..472
FT /note="Interferon-induced protein with tetratricopeptide
FT repeats 2"
FT /id="PRO_0000106348"
FT REPEAT 51..89
FT /note="TPR 1"
FT REPEAT 90..135
FT /note="TPR 2"
FT REPEAT 136..171
FT /note="TPR 3"
FT REPEAT 172..208
FT /note="TPR 4"
FT REPEAT 244..277
FT /note="TPR 5"
FT REPEAT 278..333
FT /note="TPR 6"
FT REPEAT 334..364
FT /note="TPR 7"
FT REPEAT 365..403
FT /note="TPR 8"
FT REPEAT 404..445
FT /note="TPR 9"
FT REGION 441..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P09913"
FT CONFLICT 10..11
FT /note="VC -> ES (in Ref. 2; AAC52626)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="F -> N (in Ref. 2; AAC52626)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..224
FT /note="Missing (in Ref. 2; AAC52626)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="D -> A (in Ref. 2; AAC52626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 55021 MW; 0C76034B1C0B2C41 CRC64;
MSTTSKESLV CNLRQLKCHF TWNLIAEDES LDEFEDRVFN KDEFQNSEFK ATMCNILAYV
KHCRGLNEAA LQCLGEAEGF IQQQHPDQVE IRSLVTWGNY AWVYYHMGQF SKAQAYLDKV
KQVCKKFSSP YRIENPALDC EEGWARLKCT KNQNERVKVC FQKALEKDPK NPEFTSGWAI
AFYRLDDWPA RNYCIDSLEQ AIQLSPDNTY VKVLLALKLD AVHVHKNQAM ALVEEALKKD
PSAIDTLLRA ARFYCKVYDT DRAIQLLRKA LEKLPNNAYV HYYMGCCYRS KVHHMLNRRE
MVFSGDRKKL EELIQLAVNH LRKAEEIKEM LEYSCSFLAD LYIIAKKYDE ADYYFQKELS
KDLPPGPKQL LHLRYGNFQF FQMKRQDKAI YHYMEGVKIK KKTIPQKKMR EKLQRIALRR
LHEDESDSEA LHILAFLQEN GGGQQADKDS ERGVDSANQV PSASLDEDGA EY
