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Protein
Submitted name:

Interferon regulatory factor 3

Gene

Irf3

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_275282. TRAF3-dependent IRF activation pathway.
REACT_275619. Factors involved in megakaryocyte development and platelet production.
REACT_297663. IRF3-mediated induction of type I IFN.
REACT_301576. TRAF6 mediated IRF7 activation.
REACT_312372. IRF3 mediated activation of type 1 IFN.
REACT_316967. Negative regulators of RIG-I/MDA5 signaling.
REACT_325676. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_336188. Regulation of innate immune responses to cytosolic DNA.
REACT_344709. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_348632. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Submitted name:
Interferon regulatory factor 3Imported
Submitted name:
Interferon regulatory factor 3, isoform CRA_cImported
Submitted name:
Protein Irf3Imported
Gene namesi
Name:Irf3Imported
ORF Names:rCG_54412Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1549774. Irf3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027786.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG42868.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000033705.
HOVERGENiHBG105601.
KOiK05411.
OMAiCHTYWAV.
OrthoDBiEOG7CCBR1.
TreeFamiTF328512.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProiIPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR019471. Interferon_reg_factor-3.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5XIB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTPKPLILP WLVSQLDLGQ LKGVAWLDES RTKFRIPWKH GLRQDAQMAD
60 70 80 90 100
FGIFQAWAEA SGAYTPGKDK PDLSTWKRNF RSALNRKEVL RLAEDRSKDP
110 120 130 140 150
FDPHKVYEFV TPGGARDFVH LDTSPDTNGK SSLSDHQEDL LELLDHMALG
160 170 180 190 200
PLPDEGSSDL PIASDPSQPP LSPIVNNFPN PAPQENPLRQ LLAEEQWEFE
210 220 230 240 250
VTAFYRGRQV FQQTLFCPGG LRLVGSTSDN GTLPWQPVTL PDPEEFLTDR
260 270 280 290 300
LVREYVRQVL KGLGKGLVLW RAGQCLWAQR LGHSHSFWAL GEELLPDSGR
310 320 330 340 350
GPDGEVPKDK NGVVFDLRPF VADLIAFMEG SRHSPRYTLW FCVGESWPQD
360 370 380 390 400
QPWVKRLVMV KVVPTCLKEL LEMAREGGAS SLKTVDLHIS NSQPISLTSD
410 420
QYKACLQDLV EDMDFQATGE T
Length:421
Mass (Da):47,279
Last modified:November 23, 2004 - v1
Checksum:i4ECD3290804EF09F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC127719 Genomic DNA. No translation available.
BC083776 mRNA. Translation: AAH83776.1.
CH473979 Genomic DNA. Translation: EDM07431.1.
CH473979 Genomic DNA. Translation: EDM07432.1.
RefSeqiNP_001006970.1. NM_001006969.1.
XP_006229085.1. XM_006229023.2.
XP_006229086.1. XM_006229024.2.
UniGeneiRn.1499.

Genome annotation databases

EnsembliENSRNOT00000027786; ENSRNOP00000027786; ENSRNOG00000043388.
GeneIDi292892.
KEGGirno:292892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC127719 Genomic DNA. No translation available.
BC083776 mRNA. Translation: AAH83776.1.
CH473979 Genomic DNA. Translation: EDM07431.1.
CH473979 Genomic DNA. Translation: EDM07432.1.
RefSeqiNP_001006970.1. NM_001006969.1.
XP_006229085.1. XM_006229023.2.
XP_006229086.1. XM_006229024.2.
UniGeneiRn.1499.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027786; ENSRNOP00000027786; ENSRNOG00000043388.
GeneIDi292892.
KEGGirno:292892.

Organism-specific databases

CTDi3661.
RGDi1549774. Irf3.

Phylogenomic databases

eggNOGiNOG42868.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000033705.
HOVERGENiHBG105601.
KOiK05411.
OMAiCHTYWAV.
OrthoDBiEOG7CCBR1.
TreeFamiTF328512.

Enzyme and pathway databases

ReactomeiREACT_275282. TRAF3-dependent IRF activation pathway.
REACT_275619. Factors involved in megakaryocyte development and platelet production.
REACT_297663. IRF3-mediated induction of type I IFN.
REACT_301576. TRAF6 mediated IRF7 activation.
REACT_312372. IRF3 mediated activation of type 1 IFN.
REACT_316967. Negative regulators of RIG-I/MDA5 signaling.
REACT_325676. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_336188. Regulation of innate immune responses to cytosolic DNA.
REACT_344709. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_348632. ISG15 antiviral mechanism.

Miscellaneous databases

NextBioi635016.
PROiQ5XIB0.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProiIPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR019471. Interferon_reg_factor-3.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: HeartImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ5XIB0_RAT
AccessioniPrimary (citable) accession number: Q5XIB0
Entry historyi
Integrated into UniProtKB/TrEMBL: November 23, 2004
Last sequence update: November 23, 2004
Last modified: July 22, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

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 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.