Full text data of IFIT5
IFIT5
(ISG58, RI58)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Interferon-induced protein with tetratricopeptide repeats 5; IFIT-5 (Interferon-induced 58 kDa protein; Retinoic acid- and interferon-inducible 58 kDa protein; P58)
Interferon-induced protein with tetratricopeptide repeats 5; IFIT-5 (Interferon-induced 58 kDa protein; Retinoic acid- and interferon-inducible 58 kDa protein; P58)
UniProt
Q13325
ID IFIT5_HUMAN Reviewed; 482 AA.
AC Q13325; B2R5X9; Q5T7I9; Q6IAX3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 5;
DE Short=IFIT-5;
DE AltName: Full=Interferon-induced 58 kDa protein;
DE AltName: Full=Retinoic acid- and interferon-inducible 58 kDa protein;
DE Short=P58;
GN Name=IFIT5; Synonyms=ISG58, RI58;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9398535; DOI=10.1006/bcmd.1997.0151;
RA Niikura T., Hirata R., Weil S.C.;
RT "A novel interferon-inducible gene expressed during myeloid
RT differentiation.";
RL Blood Cells Mol. Dis. 23:337-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP REVIEW.
RX PubMed=20950130; DOI=10.1089/jir.2010.0101;
RA Fensterl V., Sen G.C.;
RT "The ISG56/IFIT1 gene family.";
RL J. Interferon Cytokine Res. 31:71-78(2011).
RN [9]
RP RNA-BINDING.
RX PubMed=21642987; DOI=10.1038/ni.2048;
RA Pichlmair A., Lassnig C., Eberle C.A., Gorna M.W., Baumann C.L.,
RA Burkard T.R., Buerckstuemmer T., Stefanovic A., Krieger S.,
RA Bennett K.L., Ruelicke T., Weber F., Colinge J., Mueller M.,
RA Superti-Furga G.;
RT "IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA.";
RL Nat. Immunol. 12:624-630(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RNA-BINDING,
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF LEU-291; LYS-302;
RP ARG-307; LYS-309; 388-PHE-HIS-389; LYS-415; LYS-422 AND LYS-426.
RX PubMed=23317505; DOI=10.1016/j.molcel.2012.12.015;
RA Katibah G.E., Lee H.J., Huizar J.P., Vogan J.M., Alber T., Collins K.;
RT "tRNA binding, structure, and localization of the human interferon-
RT induced protein IFIT5.";
RL Mol. Cell 49:743-750(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP-RNA,
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF GLU-33; GLN-41; LYS-150;
RP TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; ARG-260; HIS-287 AND
RP GLN-288.
RX PubMed=23334420; DOI=10.1038/nature11783;
RA Abbas Y.M., Pichlmair A., Gorna M.W., Superti-Furga G., Nagar B.;
RT "Structural basis for viral 5'-PPP-RNA recognition by human IFIT
RT proteins.";
RL Nature 494:60-64(2013).
CC -!- FUNCTION: Interferon-induced RNA-binding protein that specifically
CC binds single-stranded RNA bearing a 5'-triphosphate group (PPP-
CC RNA), thereby acting as a sensor of viral single-stranded RNAs.
CC Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5'
CC cap and bear a 5'-triphosphate group instead, are specific from
CC viruses, providing a molecular signature to distinguish between
CC self and non-self mRNAs by the host during viral infection.
CC Directly binds PPP-RNA in a non-sequence-specific manner. Also
CC recognizes and binds tRNAs.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane.
CC Note=Colocalized with DDX58/RIG-I at cell surface ruffles.
CC Localizes to actin-rich protrusions from the apical cell surface.
CC -!- INDUCTION: By interferons (IFNs).
CC -!- DOMAIN: RNA recognition is mediated by a convoluted intramolecular
CC fold of the TPR repeats (TPR eddy), which scaffolds unique
CC additional helices that form an RNA binding cleft (PubMed:23317505
CC and PubMed:23334420). Undergoes a conformational change upon RNA-
CC binding: unliganded exists in a more open conformation,
CC facilitating RNA entry (PubMed:23334420).
CC -!- SIMILARITY: Belongs to the IFIT family.
CC -!- SIMILARITY: Contains 8 TPR repeats.
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DR EMBL; U34605; AAA84934.1; -; mRNA.
DR EMBL; AK312358; BAG35276.1; -; mRNA.
DR EMBL; CR457031; CAG33312.1; -; mRNA.
DR EMBL; AL353146; CAI12381.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50135.1; -; Genomic_DNA.
DR EMBL; BC025786; AAH25786.1; -; mRNA.
DR PIR; G02058; G02058.
DR RefSeq; NP_036552.1; NM_012420.2.
DR UniGene; Hs.252839; -.
DR PDB; 3ZGQ; X-ray; 2.20 A; A=1-482.
DR PDB; 4HOQ; X-ray; 2.07 A; A=1-482.
DR PDB; 4HOR; X-ray; 1.86 A; A=1-482.
DR PDB; 4HOS; X-ray; 2.00 A; A=1-482.
DR PDB; 4HOT; X-ray; 2.50 A; A=1-482.
DR PDB; 4J0U; X-ray; 1.97 A; A=1-482.
DR PDBsum; 3ZGQ; -.
DR PDBsum; 4HOQ; -.
DR PDBsum; 4HOR; -.
DR PDBsum; 4HOS; -.
DR PDBsum; 4HOT; -.
DR PDBsum; 4J0U; -.
DR ProteinModelPortal; Q13325; -.
DR SMR; Q13325; 1-482.
DR IntAct; Q13325; 13.
DR MINT; MINT-1395756; -.
DR STRING; 9606.ENSP00000360860; -.
DR PhosphoSite; Q13325; -.
DR DMDM; 6831571; -.
DR PaxDb; Q13325; -.
DR PeptideAtlas; Q13325; -.
DR PRIDE; Q13325; -.
DR Ensembl; ENST00000371795; ENSP00000360860; ENSG00000152778.
DR GeneID; 24138; -.
DR KEGG; hsa:24138; -.
DR UCSC; uc010qnh.2; human.
DR CTD; 24138; -.
DR GeneCards; GC10P091164; -.
DR HGNC; HGNC:13328; IFIT5.
DR HPA; HPA037957; -.
DR neXtProt; NX_Q13325; -.
DR PharmGKB; PA134988392; -.
DR eggNOG; NOG311487; -.
DR HOGENOM; HOG000001558; -.
DR HOVERGEN; HBG066330; -.
DR InParanoid; Q13325; -.
DR OMA; NTAIHHY; -.
DR OrthoDB; EOG71K62V; -.
DR PhylomeDB; Q13325; -.
DR GenomeRNAi; 24138; -.
DR NextBio; 35467534; -.
DR PRO; PR:Q13325; -.
DR ArrayExpress; Q13325; -.
DR Bgee; Q13325; -.
DR CleanEx; HS_IFIT5; -.
DR Genevestigator; Q13325; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR024125; Interferon_induced_IFIT5.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10271:SF5; PTHR10271:SF5; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF07719; TPR_2; 2.
DR SMART; SM00028; TPR; 5.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cell membrane; Cell projection;
KW Complete proteome; Immunity; Innate immunity; Membrane;
KW Reference proteome; Repeat; RNA-binding; TPR repeat; tRNA-binding.
FT CHAIN 1 482 Interferon-induced protein with
FT tetratricopeptide repeats 5.
FT /FTId=PRO_0000106351.
FT REPEAT 51 84 TPR 1.
FT REPEAT 94 127 TPR 2.
FT REPEAT 138 173 TPR 3.
FT REPEAT 181 214 TPR 4.
FT REPEAT 249 282 TPR 5.
FT REPEAT 338 371 TPR 6.
FT REPEAT 376 410 TPR 7.
FT REPEAT 435 468 TPR 8.
FT REGION 254 260 Interaction with the 5'-triphosphate
FT group of PPP-RNA.
FT SITE 33 33 Interaction with PPP-RNA.
FT SITE 37 37 Interaction with PPP-RNA.
FT SITE 41 41 Interaction with PPP-RNA.
FT SITE 150 150 Interaction with PPP-RNA.
FT SITE 186 186 Interaction with PPP-RNA.
FT SITE 250 250 Interaction with PPP-RNA.
FT SITE 288 288 Interaction with the 5'-triphosphate
FT group of PPP-RNA.
FT MUTAGEN 33 33 E->A: Reduced PPP-RNA-binding.
FT MUTAGEN 37 37 T->V: Abolishes PPP-RNA-binding.
FT MUTAGEN 41 41 Q->E: Abolishes PPP-RNA-binding.
FT MUTAGEN 150 150 K->M: Abolishes PPP-RNA-binding.
FT MUTAGEN 156 156 Y->F: Reduced PPP-RNA-binding.
FT MUTAGEN 186 186 R->H: Abolishes PPP-RNA-binding.
FT MUTAGEN 250 250 Y->F: Abolishes PPP-RNA-binding.
FT MUTAGEN 253 253 R->M: Abolishes PPP-RNA-binding.
FT MUTAGEN 254 254 Y->F: Abolishes PPP-RNA-binding.
FT MUTAGEN 260 260 R->E: Abolishes PPP-RNA-binding.
FT MUTAGEN 287 287 H->A: Reduced PPP-RNA-binding.
FT MUTAGEN 288 288 Q->E: Abolishes PPP-RNA-binding.
FT MUTAGEN 291 291 L->A: Does not affect RNA-binding.
FT MUTAGEN 302 302 K->A: Reduced RNA-binding.
FT MUTAGEN 307 307 R->A: Reduced RNA-binding. 25 fold
FT reduction in tRNA-binding.
FT MUTAGEN 309 309 K->A: Reduced RNA-binding.
FT MUTAGEN 337 337 F->A: Abolishes PPP-RNA-binding.
FT MUTAGEN 388 389 FH->AA: Reduced RNA-binding.
FT MUTAGEN 415 415 K->A: Reduced RNA-binding. 25 fold
FT reduction in tRNA-binding.
FT MUTAGEN 422 422 K->A: Reduced RNA-binding.
FT MUTAGEN 426 426 K->A: Reduced RNA-binding. 5 fold
FT reduction in tRNA-binding.
FT CONFLICT 215 215 S -> N (in Ref. 3; CAG33312).
FT CONFLICT 449 449 G -> R (in Ref. 2; BAG35276).
FT HELIX 3 15
FT HELIX 19 21
FT HELIX 26 28
FT HELIX 31 44
FT STRAND 46 48
FT HELIX 50 63
FT HELIX 67 84
FT HELIX 86 88
FT HELIX 91 93
FT HELIX 94 106
FT HELIX 110 126
FT STRAND 130 133
FT HELIX 138 150
FT HELIX 153 155
FT HELIX 156 169
FT HELIX 174 189
FT STRAND 193 195
FT HELIX 201 210
FT HELIX 215 227
FT HELIX 231 244
FT HELIX 249 261
FT HELIX 265 278
FT HELIX 283 303
FT TURN 304 306
FT HELIX 310 333
FT HELIX 338 350
FT HELIX 354 365
FT HELIX 372 388
FT HELIX 393 406
FT STRAND 408 410
FT HELIX 413 430
FT HELIX 435 447
FT HELIX 451 464
FT HELIX 469 480
SQ SEQUENCE 482 AA; 55847 MW; 8045BC100384BE05 CRC64;
MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR LALYNLLAYV
KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY AWVYYHMDQL EEAQKYTGKI
GNVCKKLSSP SNYKLECPET DCEKGWALLK FGGKYYQKAK AAFEKALEVE PDNPEFNIGY
AITVYRLDDS DREGSVKSFS LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE
ILDQISSQPY VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI
KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE GGQYSNAEDI
FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY LEALKVKDRS PLRTKLTSAL
KKLSTKRLCH NALDVQSLSA LGFVYKLEGE KRQAAEYYEK AQKIDPENAE FLTALCELRL
SI
//
ID IFIT5_HUMAN Reviewed; 482 AA.
AC Q13325; B2R5X9; Q5T7I9; Q6IAX3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Interferon-induced protein with tetratricopeptide repeats 5;
DE Short=IFIT-5;
DE AltName: Full=Interferon-induced 58 kDa protein;
DE AltName: Full=Retinoic acid- and interferon-inducible 58 kDa protein;
DE Short=P58;
GN Name=IFIT5; Synonyms=ISG58, RI58;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9398535; DOI=10.1006/bcmd.1997.0151;
RA Niikura T., Hirata R., Weil S.C.;
RT "A novel interferon-inducible gene expressed during myeloid
RT differentiation.";
RL Blood Cells Mol. Dis. 23:337-349(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP REVIEW.
RX PubMed=20950130; DOI=10.1089/jir.2010.0101;
RA Fensterl V., Sen G.C.;
RT "The ISG56/IFIT1 gene family.";
RL J. Interferon Cytokine Res. 31:71-78(2011).
RN [9]
RP RNA-BINDING.
RX PubMed=21642987; DOI=10.1038/ni.2048;
RA Pichlmair A., Lassnig C., Eberle C.A., Gorna M.W., Baumann C.L.,
RA Burkard T.R., Buerckstuemmer T., Stefanovic A., Krieger S.,
RA Bennett K.L., Ruelicke T., Weber F., Colinge J., Mueller M.,
RA Superti-Furga G.;
RT "IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA.";
RL Nat. Immunol. 12:624-630(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RNA-BINDING,
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF LEU-291; LYS-302;
RP ARG-307; LYS-309; 388-PHE-HIS-389; LYS-415; LYS-422 AND LYS-426.
RX PubMed=23317505; DOI=10.1016/j.molcel.2012.12.015;
RA Katibah G.E., Lee H.J., Huizar J.P., Vogan J.M., Alber T., Collins K.;
RT "tRNA binding, structure, and localization of the human interferon-
RT induced protein IFIT5.";
RL Mol. Cell 49:743-750(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP-RNA,
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF GLU-33; GLN-41; LYS-150;
RP TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; ARG-260; HIS-287 AND
RP GLN-288.
RX PubMed=23334420; DOI=10.1038/nature11783;
RA Abbas Y.M., Pichlmair A., Gorna M.W., Superti-Furga G., Nagar B.;
RT "Structural basis for viral 5'-PPP-RNA recognition by human IFIT
RT proteins.";
RL Nature 494:60-64(2013).
CC -!- FUNCTION: Interferon-induced RNA-binding protein that specifically
CC binds single-stranded RNA bearing a 5'-triphosphate group (PPP-
CC RNA), thereby acting as a sensor of viral single-stranded RNAs.
CC Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5'
CC cap and bear a 5'-triphosphate group instead, are specific from
CC viruses, providing a molecular signature to distinguish between
CC self and non-self mRNAs by the host during viral infection.
CC Directly binds PPP-RNA in a non-sequence-specific manner. Also
CC recognizes and binds tRNAs.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane.
CC Note=Colocalized with DDX58/RIG-I at cell surface ruffles.
CC Localizes to actin-rich protrusions from the apical cell surface.
CC -!- INDUCTION: By interferons (IFNs).
CC -!- DOMAIN: RNA recognition is mediated by a convoluted intramolecular
CC fold of the TPR repeats (TPR eddy), which scaffolds unique
CC additional helices that form an RNA binding cleft (PubMed:23317505
CC and PubMed:23334420). Undergoes a conformational change upon RNA-
CC binding: unliganded exists in a more open conformation,
CC facilitating RNA entry (PubMed:23334420).
CC -!- SIMILARITY: Belongs to the IFIT family.
CC -!- SIMILARITY: Contains 8 TPR repeats.
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DR EMBL; U34605; AAA84934.1; -; mRNA.
DR EMBL; AK312358; BAG35276.1; -; mRNA.
DR EMBL; CR457031; CAG33312.1; -; mRNA.
DR EMBL; AL353146; CAI12381.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50135.1; -; Genomic_DNA.
DR EMBL; BC025786; AAH25786.1; -; mRNA.
DR PIR; G02058; G02058.
DR RefSeq; NP_036552.1; NM_012420.2.
DR UniGene; Hs.252839; -.
DR PDB; 3ZGQ; X-ray; 2.20 A; A=1-482.
DR PDB; 4HOQ; X-ray; 2.07 A; A=1-482.
DR PDB; 4HOR; X-ray; 1.86 A; A=1-482.
DR PDB; 4HOS; X-ray; 2.00 A; A=1-482.
DR PDB; 4HOT; X-ray; 2.50 A; A=1-482.
DR PDB; 4J0U; X-ray; 1.97 A; A=1-482.
DR PDBsum; 3ZGQ; -.
DR PDBsum; 4HOQ; -.
DR PDBsum; 4HOR; -.
DR PDBsum; 4HOS; -.
DR PDBsum; 4HOT; -.
DR PDBsum; 4J0U; -.
DR ProteinModelPortal; Q13325; -.
DR SMR; Q13325; 1-482.
DR IntAct; Q13325; 13.
DR MINT; MINT-1395756; -.
DR STRING; 9606.ENSP00000360860; -.
DR PhosphoSite; Q13325; -.
DR DMDM; 6831571; -.
DR PaxDb; Q13325; -.
DR PeptideAtlas; Q13325; -.
DR PRIDE; Q13325; -.
DR Ensembl; ENST00000371795; ENSP00000360860; ENSG00000152778.
DR GeneID; 24138; -.
DR KEGG; hsa:24138; -.
DR UCSC; uc010qnh.2; human.
DR CTD; 24138; -.
DR GeneCards; GC10P091164; -.
DR HGNC; HGNC:13328; IFIT5.
DR HPA; HPA037957; -.
DR neXtProt; NX_Q13325; -.
DR PharmGKB; PA134988392; -.
DR eggNOG; NOG311487; -.
DR HOGENOM; HOG000001558; -.
DR HOVERGEN; HBG066330; -.
DR InParanoid; Q13325; -.
DR OMA; NTAIHHY; -.
DR OrthoDB; EOG71K62V; -.
DR PhylomeDB; Q13325; -.
DR GenomeRNAi; 24138; -.
DR NextBio; 35467534; -.
DR PRO; PR:Q13325; -.
DR ArrayExpress; Q13325; -.
DR Bgee; Q13325; -.
DR CleanEx; HS_IFIT5; -.
DR Genevestigator; Q13325; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR024125; Interferon_induced_IFIT5.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10271:SF5; PTHR10271:SF5; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF07719; TPR_2; 2.
DR SMART; SM00028; TPR; 5.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cell membrane; Cell projection;
KW Complete proteome; Immunity; Innate immunity; Membrane;
KW Reference proteome; Repeat; RNA-binding; TPR repeat; tRNA-binding.
FT CHAIN 1 482 Interferon-induced protein with
FT tetratricopeptide repeats 5.
FT /FTId=PRO_0000106351.
FT REPEAT 51 84 TPR 1.
FT REPEAT 94 127 TPR 2.
FT REPEAT 138 173 TPR 3.
FT REPEAT 181 214 TPR 4.
FT REPEAT 249 282 TPR 5.
FT REPEAT 338 371 TPR 6.
FT REPEAT 376 410 TPR 7.
FT REPEAT 435 468 TPR 8.
FT REGION 254 260 Interaction with the 5'-triphosphate
FT group of PPP-RNA.
FT SITE 33 33 Interaction with PPP-RNA.
FT SITE 37 37 Interaction with PPP-RNA.
FT SITE 41 41 Interaction with PPP-RNA.
FT SITE 150 150 Interaction with PPP-RNA.
FT SITE 186 186 Interaction with PPP-RNA.
FT SITE 250 250 Interaction with PPP-RNA.
FT SITE 288 288 Interaction with the 5'-triphosphate
FT group of PPP-RNA.
FT MUTAGEN 33 33 E->A: Reduced PPP-RNA-binding.
FT MUTAGEN 37 37 T->V: Abolishes PPP-RNA-binding.
FT MUTAGEN 41 41 Q->E: Abolishes PPP-RNA-binding.
FT MUTAGEN 150 150 K->M: Abolishes PPP-RNA-binding.
FT MUTAGEN 156 156 Y->F: Reduced PPP-RNA-binding.
FT MUTAGEN 186 186 R->H: Abolishes PPP-RNA-binding.
FT MUTAGEN 250 250 Y->F: Abolishes PPP-RNA-binding.
FT MUTAGEN 253 253 R->M: Abolishes PPP-RNA-binding.
FT MUTAGEN 254 254 Y->F: Abolishes PPP-RNA-binding.
FT MUTAGEN 260 260 R->E: Abolishes PPP-RNA-binding.
FT MUTAGEN 287 287 H->A: Reduced PPP-RNA-binding.
FT MUTAGEN 288 288 Q->E: Abolishes PPP-RNA-binding.
FT MUTAGEN 291 291 L->A: Does not affect RNA-binding.
FT MUTAGEN 302 302 K->A: Reduced RNA-binding.
FT MUTAGEN 307 307 R->A: Reduced RNA-binding. 25 fold
FT reduction in tRNA-binding.
FT MUTAGEN 309 309 K->A: Reduced RNA-binding.
FT MUTAGEN 337 337 F->A: Abolishes PPP-RNA-binding.
FT MUTAGEN 388 389 FH->AA: Reduced RNA-binding.
FT MUTAGEN 415 415 K->A: Reduced RNA-binding. 25 fold
FT reduction in tRNA-binding.
FT MUTAGEN 422 422 K->A: Reduced RNA-binding.
FT MUTAGEN 426 426 K->A: Reduced RNA-binding. 5 fold
FT reduction in tRNA-binding.
FT CONFLICT 215 215 S -> N (in Ref. 3; CAG33312).
FT CONFLICT 449 449 G -> R (in Ref. 2; BAG35276).
FT HELIX 3 15
FT HELIX 19 21
FT HELIX 26 28
FT HELIX 31 44
FT STRAND 46 48
FT HELIX 50 63
FT HELIX 67 84
FT HELIX 86 88
FT HELIX 91 93
FT HELIX 94 106
FT HELIX 110 126
FT STRAND 130 133
FT HELIX 138 150
FT HELIX 153 155
FT HELIX 156 169
FT HELIX 174 189
FT STRAND 193 195
FT HELIX 201 210
FT HELIX 215 227
FT HELIX 231 244
FT HELIX 249 261
FT HELIX 265 278
FT HELIX 283 303
FT TURN 304 306
FT HELIX 310 333
FT HELIX 338 350
FT HELIX 354 365
FT HELIX 372 388
FT HELIX 393 406
FT STRAND 408 410
FT HELIX 413 430
FT HELIX 435 447
FT HELIX 451 464
FT HELIX 469 480
SQ SEQUENCE 482 AA; 55847 MW; 8045BC100384BE05 CRC64;
MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR LALYNLLAYV
KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY AWVYYHMDQL EEAQKYTGKI
GNVCKKLSSP SNYKLECPET DCEKGWALLK FGGKYYQKAK AAFEKALEVE PDNPEFNIGY
AITVYRLDDS DREGSVKSFS LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE
ILDQISSQPY VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI
KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE GGQYSNAEDI
FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY LEALKVKDRS PLRTKLTSAL
KKLSTKRLCH NALDVQSLSA LGFVYKLEGE KRQAAEYYEK AQKIDPENAE FLTALCELRL
SI
//