ID   IFIT2_CRIGR             Reviewed;         468 AA.
AC   Q60462;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Interferon-induced protein with tetratricopeptide repeats 2;
DE            Short=IFIT-2;
DE   AltName: Full=CL-54 K;
DE   AltName: Full=Interferon-induced 54 kDa protein;
DE            Short=IFI-54K;
GN   Name=IFIT2; Synonyms=IFI54;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   TISSUE=Ovary;
RX   PubMed=8125096; DOI=10.1111/j.1432-1033.1994.tb18636.x;
RA   Bluyssen J.A.R., Vlietstra R.J., van der Made A., Trapman J.;
RT   "The interferon-stimulated gene 54 K promoter contains two adjacent
RT   functional interferon-stimulated response elements of different strength,
RT   which act synergistically for maximal interferon-alpha inducibility.";
RL   Eur. J. Biochem. 220:395-402(1994).
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 (By
CC       similarity). {ECO:0000250}.
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 (By similarity). Interacts with
CC       STING1/MITA and disrupts its interaction with MAVS or TBK1 (By
CC       similarity). Interacts with EIF3E and EIF3C (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- INDUCTION: By interferons. {ECO:0000269|PubMed:8125096}.
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; X77259; CAA54477.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q60462; -.
DR   SMR; Q60462; -.
DR   STRING; 10029.XP_007625629.1; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0035457; P:cellular response to interferon-alpha; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; ISS: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   2: Evidence at transcript level;
KW   Acetylation; Antiviral defense; Apoptosis; Cytoplasm;
KW   Endoplasmic reticulum; Immunity; Innate immunity; Repeat; RNA-binding;
KW   TPR repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09913"
FT   CHAIN           2..468
FT                   /note="Interferon-induced protein with tetratricopeptide
FT                   repeats 2"
FT                   /id="PRO_0000106346"
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          242..275
FT                   /note="TPR 5"
FT   REPEAT          276..328
FT                   /note="TPR 6"
FT   REPEAT          329..359
FT                   /note="TPR 7"
FT   REPEAT          360..398
FT                   /note="TPR 8"
FT   REPEAT          399..441
FT                   /note="TPR 9"
FT   REGION          441..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09913"
SQ   SEQUENCE   468 AA;  55046 MW;  9D92B878F81B1E27 CRC64;
     MSTTTKKSLE SKLQQLKCHF TWNLMAGDES LDEFEDKVFN KDEFQKRECK ATMCNILAFV
     KHRRGQNASA LKELEKAEQF IQQQHPDHVE IRNIVTWGNY AWVYYHMGQL EKAQAYLDKV
     RQVCEKFSSP YRIESPELDC EEGWARLKCT RNQNERVKVC FEKALEKDPK NPEFTSGWAI
     SNYRLDFWPA QQNAVDSLKQ AIRMSPNSPY VKVLLALKLE MNQENQGKEL VEEALREAPG
     ETDVLRSAAR FYYKTHDKDR AIQLLSQALE LLPNNAYVYY YIGCFYRSKV LQIDSRRETS
     QNENREQLLK QAIYYLKKAE ETKEMIKDSC SYLAHLYVLA EQYKEADYYF QKGFKKELTP
     GLKQLLHLRY GNFQFFQMKC EDKAIHQYLE GVKIRQKTKP KEKMTNKLRF IAERRRSQNG
     FDSKALHILA FLQELNKESQ QAAKVSERGQ DSERPVFSPS LHEGGNEQ