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Q13325 (IFIT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-induced protein with tetratricopeptide repeats 5

Short name=IFIT-5
Alternative name(s):
Interferon-induced 58 kDa protein
Retinoic acid- and interferon-inducible 58 kDa protein
Short name=P58
Gene names
Name:IFIT5
Synonyms:ISG58, RI58
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs. Ref.10 Ref.11

Subunit structure

Monomer. Ref.10

Subcellular location

Cell projectionruffle membrane. Note: Colocalized with DDX58/RIG-I at cell surface ruffles. Localizes to actin-rich protrusions from the apical cell surface. Ref.10

Induction

By interferons (IFNs).

Domain

RNA recognition is mediated by a convoluted intramolecular fold of the TPR repeats (TPR eddy), which scaffolds unique additional helices that form an RNA binding cleft (Ref.10 and Ref.11). Undergoes a conformational change upon RNA-binding: unliganded exists in a more open conformation, facilitating RNA entry (Ref.11).

Sequence similarities

Belongs to the IFIT family.

Contains 8 TPR repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Interferon-induced protein with tetratricopeptide repeats 5
PRO_0000106351

Regions

Repeat51 – 8434TPR 1
Repeat94 – 12734TPR 2
Repeat138 – 17336TPR 3
Repeat181 – 21434TPR 4
Repeat249 – 28234TPR 5
Repeat338 – 37134TPR 6
Repeat376 – 41035TPR 7
Repeat435 – 46834TPR 8
Region254 – 2607Interaction with the 5'-triphosphate group of PPP-RNA

Sites

Site331Interaction with PPP-RNA
Site371Interaction with PPP-RNA
Site411Interaction with PPP-RNA
Site1501Interaction with PPP-RNA
Site1861Interaction with PPP-RNA
Site2501Interaction with PPP-RNA
Site2881Interaction with the 5'-triphosphate group of PPP-RNA

Experimental info

Mutagenesis331E → A: Reduced PPP-RNA-binding. Ref.11
Mutagenesis371T → V: Abolishes PPP-RNA-binding.
Mutagenesis411Q → E: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis1501K → M: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis1561Y → F: Reduced PPP-RNA-binding. Ref.11
Mutagenesis1861R → H: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis2501Y → F: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis2531R → M: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis2541Y → F: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis2601R → E: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis2871H → A: Reduced PPP-RNA-binding. Ref.11
Mutagenesis2881Q → E: Abolishes PPP-RNA-binding. Ref.11
Mutagenesis2911L → A: Does not affect RNA-binding. Ref.10
Mutagenesis3021K → A: Reduced RNA-binding. Ref.10
Mutagenesis3071R → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. Ref.10
Mutagenesis3091K → A: Reduced RNA-binding. Ref.10
Mutagenesis3371F → A: Abolishes PPP-RNA-binding.
Mutagenesis388 – 3892FH → AA: Reduced RNA-binding.
Mutagenesis4151K → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. Ref.10
Mutagenesis4221K → A: Reduced RNA-binding. Ref.10
Mutagenesis4261K → A: Reduced RNA-binding. 5 fold reduction in tRNA-binding. Ref.10
Sequence conflict2151S → N in CAG33312. Ref.3
Sequence conflict4491G → R in BAG35276. Ref.2

Secondary structure

.................................................................. 482
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13325 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8045BC100384BE05

FASTA48255,847
        10         20         30         40         50         60 
MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR LALYNLLAYV 

        70         80         90        100        110        120 
KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY AWVYYHMDQL EEAQKYTGKI 

       130        140        150        160        170        180 
GNVCKKLSSP SNYKLECPET DCEKGWALLK FGGKYYQKAK AAFEKALEVE PDNPEFNIGY 

       190        200        210        220        230        240 
AITVYRLDDS DREGSVKSFS LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE 

       250        260        270        280        290        300 
ILDQISSQPY VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI 

       310        320        330        340        350        360 
KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE GGQYSNAEDI 

       370        380        390        400        410        420 
FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY LEALKVKDRS PLRTKLTSAL 

       430        440        450        460        470        480 
KKLSTKRLCH NALDVQSLSA LGFVYKLEGE KRQAAEYYEK AQKIDPENAE FLTALCELRL 


SI 

« Hide

References

« Hide 'large scale' references
[1]"A novel interferon-inducible gene expressed during myeloid differentiation."
Niikura T., Hirata R., Weil S.C.
Blood Cells Mol. Dis. 23:337-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas and Spleen.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"The ISG56/IFIT1 gene family."
Fensterl V., Sen G.C.
J. Interferon Cytokine Res. 31:71-78(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[9]"IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA."
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.
Nat. Immunol. 12:624-630(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[10]"tRNA binding, structure, and localization of the human interferon-induced protein IFIT5."
Katibah G.E., Lee H.J., Huizar J.P., Vogan J.M., Alber T., Collins K.
Mol. Cell 49:743-750(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-291; LYS-302; ARG-307; LYS-309; 388-PHE-HIS-389; LYS-415; LYS-422 AND LYS-426.
[11]"Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins."
Abbas Y.M., Pichlmair A., Gorna M.W., Superti-Furga G., Nagar B.
Nature 494:60-64(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP-RNA, FUNCTION, RNA-BINDING, MUTAGENESIS OF GLU-33; GLN-41; LYS-150; TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; ARG-260; HIS-287 AND GLN-288.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U34605 mRNA. Translation: AAA84934.1.
AK312358 mRNA. Translation: BAG35276.1.
CR457031 mRNA. Translation: CAG33312.1.
AL353146 Genomic DNA. Translation: CAI12381.1.
CH471066 Genomic DNA. Translation: EAW50135.1.
BC025786 mRNA. Translation: AAH25786.1.
PIRG02058.
RefSeqNP_036552.1. NM_012420.2.
UniGeneHs.252839.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZGQX-ray2.20A1-482[»]
4HOQX-ray2.07A1-482[»]
4HORX-ray1.86A1-482[»]
4HOSX-ray2.00A1-482[»]
4HOTX-ray2.50A1-482[»]
4J0UX-ray1.97A1-482[»]
ProteinModelPortalQ13325.
SMRQ13325. Positions 1-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117289. 19 interactions.
IntActQ13325. 13 interactions.
MINTMINT-1395756.
STRING9606.ENSP00000360860.

PTM databases

PhosphoSiteQ13325.

Polymorphism databases

DMDM6831571.

Proteomic databases

PaxDbQ13325.
PeptideAtlasQ13325.
PRIDEQ13325.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371795; ENSP00000360860; ENSG00000152778.
GeneID24138.
KEGGhsa:24138.
UCSCuc010qnh.2. human.

Organism-specific databases

CTD24138.
GeneCardsGC10P091164.
HGNCHGNC:13328. IFIT5.
HPAHPA037957.
neXtProtNX_Q13325.
PharmGKBPA134988392.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311487.
HOGENOMHOG000001558.
HOVERGENHBG066330.
InParanoidQ13325.
OMANTAIHHY.
OrthoDBEOG71K62V.
PhylomeDBQ13325.
TreeFamTF342671.

Gene expression databases

ArrayExpressQ13325.
BgeeQ13325.
CleanExHS_IFIT5.
GenevestigatorQ13325.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR024125. Interferon_induced_IFIT5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10271:SF5. PTHR10271:SF5. 1 hit.
PfamPF00515. TPR_1. 1 hit.
PF07719. TPR_2. 2 hits.
[Graphical view]
SMARTSM00028. TPR. 5 hits.
[Graphical view]
PROSITEPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi24138.
NextBio35467534.
PROQ13325.

Entry information

Entry nameIFIT5_HUMAN
AccessionPrimary (citable) accession number: Q13325
Secondary accession number(s): B2R5X9, Q5T7I9, Q6IAX3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM