IFIT1_MACFA
ID IFIT1_MACFA Reviewed; 478 AA.
AC Q4R5F5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 1;
DE Short=IFIT-1;
GN Name=IFIT1; ORFNames=QnpA-13470;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). {ECO:0000250}.
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 (via TPR repeats 4-7) with EEF1A1 (By
CC similarity). Interacts (via TPR repeats 1-4) with RPL15 (By
CC similarity). Interacts with STING1/MITA and disrupts its interaction
CC with MAVS or TBK1 (By similarity). Interacts with EIF3C and EIF3E (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AB169588; BAE01670.1; -; mRNA.
DR RefSeq; NP_001274655.1; NM_001287726.1.
DR RefSeq; XP_005565966.1; XM_005565909.2.
DR AlphaFoldDB; Q4R5F5; -.
DR SMR; Q4R5F5; -.
DR STRING; 9541.XP_005565966.1; -.
DR Ensembl; ENSMFAT00000097999; ENSMFAP00000063010; ENSMFAG00000040940.
DR Ensembl; ENSMFAT00000098426; ENSMFAP00000062881; ENSMFAG00000040940.
DR GeneID; 102143994; -.
DR KEGG; mcf:102143994; -.
DR CTD; 3434; -.
DR VEuPathDB; HostDB:ENSMFAG00000040940; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00950000182946; -.
DR Proteomes; UP000233100; Chromosome 9.
DR Bgee; ENSMFAG00000040940; Expressed in bone marrow and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:InterPro.
DR GO; GO:0071357; P:cellular response to type I interferon; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR024121; Interferon-induced_IFIT1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10271:SF30; PTHR10271:SF30; 1.
DR Pfam; PF07719; TPR_2; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cytoplasm; 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_0000285729"
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"
SQ SEQUENCE 478 AA; 55348 MW; 558589EAC2DCBBBD CRC64;
MSTNGDNHQV KDSLEQLRCH FTWELFIEDD EMPDLENRVL DQIEFLDTKY NVGIHNLLAY
VKHLKGQNEE ALKSLKEAED LMQKEHANQA SVRSLVTWSN FAWVYYHMGR LAEAQAYLDK
VENICKKPSN PFRYRMECPE IDCEEGWALL KCGGKNYERA KACFEKALEG DHENPEFSTG
YAISAYRLDG FKLATKGYRQ FSLLPLRQAV SLNPDNGYLK VLLALKLQDN GQEAEGEKYL
EEALANMSSQ TYVFRYAAKF YRRKGSVDKA LELLKKALQE TPTSVLLHHQ IGLCYKAQMI
QIKEATKGQP RGQNREKIDK MIRLAIFHFE SAVENKPTFE VAHLDLARMY IEAGNHRKAE
ETFQKLLCMK PVVEETMQDI HLQYARFQEF QKKSEINAII HYLKAIKIEQ TSFIRDKSIN
SLKKLVLKKL QRNALDLESL SLLGFVYKLK GNMNEALEYY ERALRLAADF ENSVRQGP
