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Interferon-induced protein with tetratricopeptide repeats 3 (IFIT-3) (CIG49) (ISG-60) (Interferon-induced 60 kDa protein) (IFI-60K) (Interferon-induced protein with tetratricopeptide repeats 4) (IFIT-4) (Retinoic acid-induced gene G protein) (P60) (RIG-G)

 IFIT3_HUMAN             Reviewed;         490 AA.
O14879; Q99634; Q9BSK7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 162.
RecName: Full=Interferon-induced protein with tetratricopeptide repeats 3;
Short=IFIT-3;
AltName: Full=CIG49;
AltName: Full=ISG-60;
AltName: Full=Interferon-induced 60 kDa protein;
Short=IFI-60K;
AltName: Full=Interferon-induced protein with tetratricopeptide repeats 4;
Short=IFIT-4;
AltName: Full=Retinoic acid-induced gene G protein;
Short=P60;
Short=RIG-G;
Name=IFIT3; Synonyms=CIG-49, IFI60, IFIT4, ISG60;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Foreskin;
PubMed=9391139; DOI=10.1073/pnas.94.25.13985;
Zhu H., Cong J.-P., Shenk T.;
"Use of differential display analysis to assess the effect of human
cytomegalovirus infection on the accumulation of cellular RNAs:
induction of interferon-responsive RNAs.";
Proc. Natl. Acad. Sci. U.S.A. 94:13985-13990(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9828129; DOI=10.1006/geno.1998.5555;
de Veer M.J., Sim H., Whisstock J.C., Devenish R.J., Ralph S.J.;
"IFI60/ISG60/IFIT4, a new member of the human IFI54/IFIT2 family of
interferon-stimulated genes.";
Genomics 54:267-277(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Yu M., Tong J., Mao M., Chen S., Chen Z.;
"RIG-G, a novel gene induced by ATRA in acute promyelocytic leukemia
cells, is a new member of the ISG family.";
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH COPS5.
PubMed=17050680; DOI=10.1073/pnas.0607830103;
Xiao S., Li D., Zhu H.Q., Song M.G., Pan X.R., Jia P.M., Peng L.L.,
Dou A.X., Chen G.Q., Chen S.J., Chen Z., Tong J.H.;
"RIG-G as a key mediator of the antiproliferative activity of
interferon-related pathways through enhancing p21 and p27 proteins.";
Proc. Natl. Acad. Sci. U.S.A. 103:16448-16453(2006).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18706081; DOI=10.1186/ar2475;
Huang X., Shen N., Bao C., Gu Y., Wu L., Chen S.;
"Interferon-induced protein IFIT4 is associated with systemic lupus
erythematosus and promotes differentiation of monocytes into dendritic
cell-like cells.";
Arthritis Res. Ther. 10:R91-R91(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-237, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-478, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
FUNCTION.
PubMed=20686046; DOI=10.1128/JVI.00818-10;
Schmeisser H., Mejido J., Balinsky C.A., Morrow A.N., Clark C.R.,
Zhao T., Zoon K.C.;
"Identification of alpha interferon-induced genes associated with
antiviral activity in Daudi cells and characterization of IFIT3 as a
novel antiviral gene.";
J. Virol. 84:10671-10680(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION, AND INTERACTION WITH IFIT2.
PubMed=21190939; DOI=10.1074/jbc.M110.207068;
Stawowczyk M., Van Scoy S., Kumar K.P., Reich N.C.;
"The interferon stimulated gene 54 promotes apoptosis.";
J. Biol. Chem. 286:7257-7266(2011).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAVS; TBK1; TRAF6
AND DDX58.
PubMed=21813773; DOI=10.4049/jimmunol.1100963;
Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.;
"IFN-induced TPR protein IFIT3 potentiates antiviral signaling by
bridging MAVS and TBK1.";
J. Immunol. 187:2559-2568(2011).
[15]
REVIEW.
PubMed=20950130; DOI=10.1089/jir.2010.0101;
Fensterl V., Sen G.C.;
"The ISG56/IFIT1 gene family.";
J. Interferon Cytokine Res. 31:71-78(2011).
[16]
FUNCTION, AND INTERACTION WITH IFIT1 AND IFIT2.
PubMed=21642987; DOI=10.1038/ni.2048;
Pichlmair A., Lassnig C., Eberle C.A., Gorna M.W., Baumann C.L.,
Burkard T.R., Buerckstuemmer T., Stefanovic A., Krieger S.,
Bennett K.L., Ruelicke T., Weber F., Colinge J., Mueller M.,
Superti-Furga G.;
"IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA.";
Nat. Immunol. 12:624-630(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: IFN-induced antiviral protein which acts as an inhibitor
of cellular as well as viral processes, cell migration,
proliferation, signaling, and viral replication. Enhances MAVS-
mediated host antiviral responses by serving as an adapter
bridging TBK1 to MAVS which leads to the activation of TBK1 and
phosphorylation of IRF3 and phosphorylated IRF3 translocates into
nucleus to promote antiviral gene transcription. Exihibits an
antiproliferative activity via the up-regulation of cell cycle
negative regulators CDKN1A/p21 and CDKN1B/p27. Normally,
CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27
in the nucleus and exports it to the cytoplasm for ubiquitin-
dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm,
thereby increasing nuclear CDKN1B/p27 protein levels. Upregulates
CDKN1A/p21 by downregulating MYC, a repressor of CDKN1A/p21. Can
negatively regulate the apoptotic effects of IFIT2.
{ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20686046,
ECO:0000269|PubMed:21190939, ECO:0000269|PubMed:21642987,
ECO:0000269|PubMed:21813773}.
-!- SUBUNIT: Component of an interferon-dependent multiprotein
complex, at least composed of IFIT1, IFIT2 and IFIT3. Interacts
with IFIT1 and IFIT2. Interacts (via N-terminus) with MAVS, TBK1,
TRAF6 and DDX58. Interacts with COPS5.
{ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:21190939,
ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:21813773}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-745127, EBI-745127;
Q16543:CDC37; NbExp=4; IntAct=EBI-745127, EBI-295634;
Q92905:COPS5; NbExp=4; IntAct=EBI-745127, EBI-594661;
Q05D60:DEUP1; NbExp=4; IntAct=EBI-745127, EBI-748597;
Q0P5U8:FLJ90650; NbExp=3; IntAct=EBI-745127, EBI-10226698;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-745127, EBI-2514791;
P09914:IFIT1; NbExp=10; IntAct=EBI-745127, EBI-745117;
Q5T764:IFIT1B; NbExp=3; IntAct=EBI-745127, EBI-3507164;
P09913:IFIT2; NbExp=4; IntAct=EBI-745127, EBI-3507167;
Q8IZ03:IFIT2; NbExp=5; IntAct=EBI-745127, EBI-746217;
Q8IXX5:TMEM183A; NbExp=5; IntAct=EBI-745127, EBI-2841953;
P09493-10:TPM1; NbExp=4; IntAct=EBI-745127, EBI-12123928;
P06753:TPM3; NbExp=5; IntAct=EBI-745127, EBI-355607;
Q5VU62:TPM3; NbExp=3; IntAct=EBI-745127, EBI-10184033;
-!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
-!- TISSUE SPECIFICITY: Expression significantly higher in peripheral
blood mononuclear cells (PBMCs) and monocytes from systemic lupus
erythematosus (SLE) patients than in those from healthy
individuals (at protein level). Spleen, lung, leukocytes, lymph
nodes, placenta, bone marrow and fetal liver.
{ECO:0000269|PubMed:18706081}.
-!- INDUCTION: By type I interferons, dsRNAs and viruses.
{ECO:0000269|PubMed:17050680}.
-!- SIMILARITY: Belongs to the IFIT family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF026939; AAB95160.1; -; mRNA.
EMBL; AF083470; AAC63524.1; -; mRNA.
EMBL; U52513; AAB40606.1; -; mRNA.
EMBL; BT007284; AAP35948.1; -; mRNA.
EMBL; BC001383; AAH01383.1; -; mRNA.
EMBL; BC004977; AAH04977.1; -; mRNA.
CCDS; CCDS31241.1; -.
CCDS; CCDS7402.1; -.
RefSeq; NP_001026853.1; NM_001031683.3.
RefSeq; NP_001540.2; NM_001549.5.
UniGene; Hs.47338; -.
UniGene; Hs.744072; -.
ProteinModelPortal; O14879; -.
SMR; O14879; -.
BioGrid; 109660; 70.
DIP; DIP-37890N; -.
IntAct; O14879; 56.
MINT; MINT-1448195; -.
STRING; 9606.ENSP00000360876; -.
iPTMnet; O14879; -.
PhosphoSitePlus; O14879; -.
BioMuta; IFIT3; -.
EPD; O14879; -.
PaxDb; O14879; -.
PeptideAtlas; O14879; -.
PRIDE; O14879; -.
DNASU; 3437; -.
Ensembl; ENST00000371811; ENSP00000360876; ENSG00000119917.
Ensembl; ENST00000371818; ENSP00000360883; ENSG00000119917.
GeneID; 3437; -.
KEGG; hsa:3437; -.
CTD; 3437; -.
DisGeNET; 3437; -.
EuPathDB; HostDB:ENSG00000119917.13; -.
GeneCards; IFIT3; -.
HGNC; HGNC:5411; IFIT3.
HPA; HPA059914; -.
MIM; 604650; gene.
neXtProt; NX_O14879; -.
OpenTargets; ENSG00000119917; -.
PharmGKB; PA29651; -.
eggNOG; KOG1124; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00390000013876; -.
HOGENOM; HOG000001558; -.
HOVERGEN; HBG066330; -.
InParanoid; O14879; -.
OMA; NGYLYHQ; -.
OrthoDB; EOG091G06GX; -.
PhylomeDB; O14879; -.
TreeFam; TF342671; -.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
GeneWiki; IFIT3; -.
GenomeRNAi; 3437; -.
PRO; PR:O14879; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000119917; -.
CleanEx; HS_IFIT3; -.
ExpressionAtlas; O14879; baseline and differential.
Genevisible; O14879; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035457; P:cellular response to interferon-alpha; IEA:InterPro.
GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR024122; Interferon-induced_IFIT3.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10271:SF3; PTHR10271:SF3; 1.
Pfam; PF13176; TPR_7; 1.
Pfam; PF13181; TPR_8; 2.
SMART; SM00028; TPR; 5.
SUPFAM; SSF48452; SSF48452; 3.
PROSITE; PS50005; TPR; 5.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Antiviral defense; Complete proteome; Cytoplasm; Immunity;
Innate immunity; Mitochondrion; Phosphoprotein; Reference proteome;
Repeat; TPR repeat.
CHAIN 1 490 Interferon-induced protein with
tetratricopeptide repeats 3.
/FTId=PRO_0000106349.
REPEAT 51 84 TPR 1.
REPEAT 94 127 TPR 2.
REPEAT 136 169 TPR 3.
REPEAT 172 206 TPR 4.
REPEAT 207 240 TPR 5.
REPEAT 241 274 TPR 6.
REPEAT 415 448 TPR 7.
REPEAT 450 481 TPR 8.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
CONFLICT 44 44 F -> S (in Ref. 5; AAH04977).
{ECO:0000305}.
CONFLICT 359 359 Q -> QQ (in Ref. 2; AAB40606).
{ECO:0000305}.
CONFLICT 435 435 Missing (in Ref. 2; AAB40606).
{ECO:0000305}.
SEQUENCE 490 AA; 55985 MW; B9F042D4DF7151D2 CRC64;
MSEVTKNSLE KILPQLKCHF TWNLFKEDSV SRDLEDRVCN QIEFLNTEFK ATMYNLLAYI
KHLDGNNEAA LECLRQAEEL IQQEHADQAE IRSLVTWGNY AWVYYHLGRL SDAQIYVDKV
KQTCKKFSNP YSIEYSELDC EEGWTQLKCG RNERAKVCFE KALEEKPNNP EFSSGLAIAM
YHLDNHPEKQ FSTDVLKQAI ELSPDNQYVK VLLGLKLQKM NKEAEGEQFV EEALEKSPCQ
TDVLRSAAKF YRRKGDLDKA IELFQRVLES TPNNGYLYHQ IGCCYKAKVR QMQNTGESEA
SGNKEMIEAL KQYAMDYSNK ALEKGLNPLN AYSDLAEFLE TECYQTPFNK EVPDAEKQQS
HQRYCNLQKY NGKSEDTAVQ HGLEGLSISK KSTDKEEIKD QPQNVSENLL PQNAPNYWYL
QGLIHKQNGD LLQAAKCYEK ELGRLLRDAP SGIGSIFLSA SELEDGSEEM GQGAVSSSPR
ELLSNSEQLN


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