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Database: UniProt
Entry: IFIT1_MACFA
LinkDB: IFIT1_MACFA
Original site: 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   24-JAN-2024, entry version 82.
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   Ensembl; ENSMFAT00000097999.1; ENSMFAP00000063010.1; ENSMFAG00000040940.2.
DR   Ensembl; ENSMFAT00000098426.1; ENSMFAP00000062881.1; ENSMFAG00000040940.2.
DR   GeneID; 102143994; -.
DR   KEGG; mcf:102143994; -.
DR   CTD; 3434; -.
DR   VEuPathDB; HostDB:ENSMFAG00000040940; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00950000182946; -.
DR   OrthoDB; 5401272at2759; -.
DR   Proteomes; UP000233100; Chromosome 9.
DR   Bgee; ENSMFAG00000040940; Expressed in bone marrow and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
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:0009615; P:response to virus; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR10271; INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS; 1.
DR   PANTHER; PTHR10271:SF16; INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS 1; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; TPR-like; 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
//
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