ID IFIT3_PANTR Reviewed; 490 AA.
AC A5A6J9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 3;
DE Short=IFIT-3;
GN Name=IFIT3;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
CC -!- FUNCTION: IFN-induced antiviral protein which acts as an inhibitor of
CC cellular as well as viral processes, cell migration, proliferation,
CC signaling, and viral replication. Enhances MAVS-mediated host antiviral
CC responses by serving as an adapter bridging TBK1 to MAVS which leads to
CC the activation of TBK1 and phosphorylation of IRF3 and phosphorylated
CC IRF3 translocates into nucleus to promote antiviral gene transcription.
CC Exhibits an antiproliferative activity via the up-regulation of cell
CC cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally,
CC CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in
CC the nucleus and exports it to the cytoplasm for ubiquitin-dependent
CC degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby
CC increasing nuclear CDKN1B/p27 protein levels. Up-regulates CDKN1A/p21
CC by down-regulating MYC, a repressor of CDKN1A/p21. Can negatively
CC regulate the apoptotic effects of IFIT2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of an interferon-dependent multiprotein complex, at
CC least composed of IFIT1, IFIT2 and IFIT3 (By similarity). Interacts
CC with IFIT1 and IFIT2 (By similarity). Interacts (via N-terminus) with
CC MAVS, TBK1, TRAF6 and RIGI (By similarity). Interacts with COPS5 (By
CC similarity). {ECO:0000250|UniProtKB:O14879}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14879}.
CC Mitochondrion {ECO:0000250|UniProtKB:O14879}.
CC -!- SIMILARITY: Belongs to the IFIT family. {ECO:0000305}.
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DR EMBL; AB222127; BAF62372.1; -; mRNA.
DR RefSeq; NP_001182075.1; NM_001195146.1.
DR AlphaFoldDB; A5A6J9; -.
DR SMR; A5A6J9; -.
DR STRING; 9598.ENSPTRP00000088943; -.
DR GeneID; 738542; -.
DR KEGG; ptr:738542; -.
DR CTD; 3437; -.
DR InParanoid; A5A6J9; -.
DR OrthoDB; 5401272at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
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; IPR019734; TPR_repeat.
DR PANTHER; PTHR10271; INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS; 1.
DR PANTHER; PTHR10271:SF3; INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS 3; 1.
DR Pfam; PF13176; TPR_7; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cytoplasm; Immunity; Innate immunity; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..490
FT /note="Interferon-induced protein with tetratricopeptide
FT repeats 3"
FT /id="PRO_0000295305"
FT REPEAT 51..84
FT /note="TPR 1"
FT REPEAT 94..127
FT /note="TPR 2"
FT REPEAT 136..169
FT /note="TPR 3"
FT REPEAT 172..206
FT /note="TPR 4"
FT REPEAT 207..240
FT /note="TPR 5"
FT REPEAT 241..274
FT /note="TPR 6"
FT REPEAT 415..448
FT /note="TPR 7"
FT REPEAT 450..481
FT /note="TPR 8"
FT REGION 386..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14879"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14879"
SQ SEQUENCE 490 AA; 55978 MW; 96D0B4FCBD7F7CFC CRC64;
MSEVTKNSLE KILPQLKCHF TWNLFKEESV SRDLEDRVCN QIEFLNTEFK ATMYNLLAYI
KHLDGNNEAA LECLRQAEEL IQQEHADQAE IRSLVTWGNY VWVYYHLGRL SDAQIYVDKV
KQTCKKFSNP YSIEYSELDC EEGWTQLKCG RNERAKVCFE KALEEKPNNP EFSSGLAIAM
YHLDNNPEKQ FSTDVLKQAI ELSPDNQYVK VLLGLKLQKM NKEAEGEQFV EEALEKAPCQ
TDVLRSAAKF YRRKGDLDKA IELFQRVLES TPNNGYLYHQ IGCCYKAKVR QMQNTGESEA
SGNKEMIEAL KQYAMDYSNK ALEKGLNPLN AYSDCAEFLE TECYQTPFNK EVPDAEKQQS
HQRYCNLQKY NGKSEDTAVQ HGLEGLSISK KSTDKEEIKD QPQNVSENLL PQNAPNYWYL
QGLIHKQNGD LLQAAKCYEK ELGRLLRDAP SGIGSIFLSA SELEDGSEEM GQGAVSSSPR
ELLSNSEQLN
//
