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Protein

Interferon-induced protein with tetratricopeptide repeats 5

Gene

IFIT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • defense response to virus Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000152778-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:IFIT5
Synonyms:ISG58, RI58
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:13328. IFIT5.

Subcellular locationi

  • Cell projectionruffle membrane 1 Publication

  • Note: Colocalized with DDX58/RIG-I at cell surface ruffles. Localizes to actin-rich protrusions from the apical cell surface.

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • apical part of cell Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • plasma membrane Source: HPA
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi33E → A: Reduced PPP-RNA-binding. 1 Publication1
Mutagenesisi37T → V: Abolishes PPP-RNA-binding. 1
Mutagenesisi41Q → E: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi150K → M: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi156Y → F: Reduced PPP-RNA-binding. 1 Publication1
Mutagenesisi186R → H: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi250Y → F: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi253R → M: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi254Y → F: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi260R → E: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi287H → A: Reduced PPP-RNA-binding. 1 Publication1
Mutagenesisi288Q → E: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi291L → A: Does not affect RNA-binding. 1 Publication1
Mutagenesisi302K → A: Reduced RNA-binding. 1 Publication1
Mutagenesisi307R → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. 1 Publication1
Mutagenesisi309K → A: Reduced RNA-binding. 1 Publication1
Mutagenesisi337F → A: Abolishes PPP-RNA-binding. 1
Mutagenesisi388 – 389FH → AA: Reduced RNA-binding. 1 Publication2
Mutagenesisi415K → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. 1 Publication1
Mutagenesisi422K → A: Reduced RNA-binding. 1 Publication1
Mutagenesisi426K → A: Reduced RNA-binding. 5 fold reduction in tRNA-binding. 1 Publication1

Organism-specific databases

DisGeNETi24138.
OpenTargetsiENSG00000152778.
PharmGKBiPA134988392.

Polymorphism and mutation databases

BioMutaiIFIT5.
DMDMi6831571.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001063511 – 482Interferon-induced protein with tetratricopeptide repeats 5Add BLAST482

Proteomic databases

EPDiQ13325.
MaxQBiQ13325.
PaxDbiQ13325.
PeptideAtlasiQ13325.
PRIDEiQ13325.
TopDownProteomicsiQ13325-1. [Q13325-1]

PTM databases

iPTMnetiQ13325.
PhosphoSitePlusiQ13325.

Expressioni

Inductioni

By interferons (IFNs).

Gene expression databases

BgeeiENSG00000152778.
CleanExiHS_IFIT5.
GenevisibleiQ13325. HS.

Organism-specific databases

HPAiHPA037957.
HPA062180.

Interactioni

Subunit structurei

Monomer.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei33Interaction with PPP-RNA1
Sitei37Interaction with PPP-RNA1
Sitei41Interaction with PPP-RNA1
Sitei150Interaction with PPP-RNA1
Sitei186Interaction with PPP-RNA1
Sitei250Interaction with PPP-RNA1
Sitei288Interaction with the 5'-triphosphate group of PPP-RNA1

Protein-protein interaction databases

BioGridi117289. 24 interactors.
IntActiQ13325. 13 interactors.
MINTiMINT-1395756.
STRINGi9606.ENSP00000360860.

Structurei

Secondary structure

1482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 15Combined sources13
Helixi19 – 21Combined sources3
Helixi26 – 28Combined sources3
Helixi31 – 44Combined sources14
Beta strandi46 – 48Combined sources3
Helixi50 – 63Combined sources14
Helixi67 – 84Combined sources18
Helixi86 – 88Combined sources3
Helixi91 – 93Combined sources3
Helixi94 – 106Combined sources13
Helixi110 – 126Combined sources17
Beta strandi130 – 133Combined sources4
Helixi138 – 150Combined sources13
Helixi153 – 155Combined sources3
Helixi156 – 169Combined sources14
Helixi174 – 189Combined sources16
Beta strandi193 – 195Combined sources3
Helixi201 – 210Combined sources10
Helixi215 – 227Combined sources13
Helixi231 – 244Combined sources14
Helixi249 – 261Combined sources13
Helixi265 – 278Combined sources14
Helixi283 – 303Combined sources21
Turni304 – 306Combined sources3
Helixi310 – 333Combined sources24
Helixi338 – 350Combined sources13
Helixi354 – 365Combined sources12
Helixi372 – 388Combined sources17
Helixi393 – 406Combined sources14
Beta strandi408 – 410Combined sources3
Helixi413 – 430Combined sources18
Helixi435 – 447Combined sources13
Helixi451 – 464Combined sources14
Helixi469 – 480Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ13325.
SMRiQ13325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati51 – 84TPR 1Add BLAST34
Repeati94 – 127TPR 2Add BLAST34
Repeati138 – 173TPR 3Add BLAST36
Repeati181 – 214TPR 4Add BLAST34
Repeati249 – 282TPR 5Add BLAST34
Repeati338 – 371TPR 6Add BLAST34
Repeati376 – 410TPR 7Add BLAST35
Repeati435 – 468TPR 8Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni254 – 260Interaction with the 5'-triphosphate group of PPP-RNA7

Domaini

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 (PubMed:23317505 and PubMed:23334420). Undergoes a conformational change upon RNA-binding: unliganded exists in a more open conformation, facilitating RNA entry (PubMed:23334420).1 Publication

Sequence similaritiesi

Belongs to the IFIT family.Curated
Contains 8 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1124. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000013876.
HOGENOMiHOG000001558.
HOVERGENiHBG066330.
InParanoidiQ13325.
OMAiNTAIHHY.
OrthoDBiEOG091G06GX.
PhylomeDBiQ13325.
TreeFamiTF342671.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024125. Interferon_induced_IFIT5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10271:SF17. PTHR10271:SF17. 1 hit.
PfamiPF13374. TPR_10. 1 hit.
PF07719. TPR_2. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13325-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR
60 70 80 90 100
LALYNLLAYV KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY
110 120 130 140 150
AWVYYHMDQL EEAQKYTGKI GNVCKKLSSP SNYKLECPET DCEKGWALLK
160 170 180 190 200
FGGKYYQKAK AAFEKALEVE PDNPEFNIGY AITVYRLDDS DREGSVKSFS
210 220 230 240 250
LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE ILDQISSQPY
260 270 280 290 300
VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI
310 320 330 340 350
KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE
360 370 380 390 400
GGQYSNAEDI FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY
410 420 430 440 450
LEALKVKDRS PLRTKLTSAL KKLSTKRLCH NALDVQSLSA LGFVYKLEGE
460 470 480
KRQAAEYYEK AQKIDPENAE FLTALCELRL SI
Length:482
Mass (Da):55,847
Last modified:November 1, 1996 - v1
Checksum:i8045BC100384BE05
GO
Isoform 2 (identifier: Q13325-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     158-205: Missing.

Note: No experimental confirmation available.
Show »
Length:434
Mass (Da):50,520
Checksum:i6CA739D6614569C8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti215S → N in CAG33312 (Ref. 3) Curated1
Sequence conflicti449G → R in BAG35276 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056412158 – 205Missing in isoform 2. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34605 mRNA. Translation: AAA84934.1.
AK293346 mRNA. Translation: BAG56862.1.
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.
CCDSiCCDS7403.1. [Q13325-1]
PIRiG02058.
RefSeqiNP_036552.1. NM_012420.2. [Q13325-1]
UniGeneiHs.252839.

Genome annotation databases

EnsembliENST00000371795; ENSP00000360860; ENSG00000152778. [Q13325-1]
GeneIDi24138.
KEGGihsa:24138.
UCSCiuc010qnh.3. human. [Q13325-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34605 mRNA. Translation: AAA84934.1.
AK293346 mRNA. Translation: BAG56862.1.
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.
CCDSiCCDS7403.1. [Q13325-1]
PIRiG02058.
RefSeqiNP_036552.1. NM_012420.2. [Q13325-1]
UniGeneiHs.252839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ13325.
SMRiQ13325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117289. 24 interactors.
IntActiQ13325. 13 interactors.
MINTiMINT-1395756.
STRINGi9606.ENSP00000360860.

PTM databases

iPTMnetiQ13325.
PhosphoSitePlusiQ13325.

Polymorphism and mutation databases

BioMutaiIFIT5.
DMDMi6831571.

Proteomic databases

EPDiQ13325.
MaxQBiQ13325.
PaxDbiQ13325.
PeptideAtlasiQ13325.
PRIDEiQ13325.
TopDownProteomicsiQ13325-1. [Q13325-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371795; ENSP00000360860; ENSG00000152778. [Q13325-1]
GeneIDi24138.
KEGGihsa:24138.
UCSCiuc010qnh.3. human. [Q13325-1]

Organism-specific databases

CTDi24138.
DisGeNETi24138.
GeneCardsiIFIT5.
HGNCiHGNC:13328. IFIT5.
HPAiHPA037957.
HPA062180.
MIMi616135. gene.
neXtProtiNX_Q13325.
OpenTargetsiENSG00000152778.
PharmGKBiPA134988392.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1124. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000013876.
HOGENOMiHOG000001558.
HOVERGENiHBG066330.
InParanoidiQ13325.
OMAiNTAIHHY.
OrthoDBiEOG091G06GX.
PhylomeDBiQ13325.
TreeFamiTF342671.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000152778-MONOMER.

Miscellaneous databases

GenomeRNAii24138.
PROiQ13325.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000152778.
CleanExiHS_IFIT5.
GenevisibleiQ13325. HS.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024125. Interferon_induced_IFIT5.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10271:SF17. PTHR10271:SF17. 1 hit.
PfamiPF13374. TPR_10. 1 hit.
PF07719. TPR_2. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIFIT5_HUMAN
AccessioniPrimary (citable) accession number: Q13325
Secondary accession number(s): B2R5X9
, B4DDV1, Q5T7I9, Q6IAX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.