Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NLR family CARD domain-containing protein 4

Gene

Nlrc4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. It senses pathogenic proteins of the type III secretion system (T3SS) and type IV secretion system (T4SS) such as flagellin and PrgJ-like rod proteins via the Naip proteins (Naip1, Naip2 or Naip5): specific Naip proteins recognize and bind pathogenic proteins, driving assembly and activation of the NLRC4 inflammasome. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri and fungal pathogen C.albicans. In intestine, the NLRC4 inflammasome is able to discriminate between commensal and pathogenic bacteria and specifically drives production of interleukin-1 beta (IL1B) in response to infection by Salmonella or P.aeruginosa. In case of L.pneumophila infection the inflammasome acts by activating caspase-7.14 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1768ATP

GO - Molecular functioni

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  • activation of innate immune response Source: UniProtKB
  • defense response to bacterium Source: UniProtKB
  • detection of bacterium Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • interleukin-1 beta secretion Source: UniProtKB
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of NF-kappaB transcription factor activity Source: MGI
  • protein homooligomerization Source: UniProtKB
  • pyroptosis Source: UniProtKB
  • regulation of apoptotic process Source: MGI
  • regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
NLR family CARD domain-containing protein 4
Alternative name(s):
Caspase recruitment domain-containing protein 12
Ice protease-activating factor
Short name:
Ipaf
Gene namesi
Name:Nlrc4
Synonyms:Card12, Ipaf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:3036243. Nlrc4.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • IPAF inflammasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice show defects in inflammasome function in response to S.typhimurium (Salmonella) infection. Differences are however observed depending on the strain background: in a C57BL/6J strain background, no striking differences are observed compared to wild-type mice following Salmonella infection. While in a BALB/c strain background, mice are highly susceptible to orogastric but not intraperitoneal infection with Salmonella: enhanced lethality is preceded by impaired expression of endothelial adhesion molecules, lower neutrophil recruitment and poor intestinal pathogen clearance.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi443 – 4431H → L: Constitutively active. 1 Publication
Mutagenesisi533 – 5331S → A: Abolishes phosphorylation and prevents activation of caspase-1 and pyroptosis in response to S.typhimurium. 1 Publication
Mutagenesisi533 – 5331S → D: Mimics phosphorylation; causes rapid macrophage pyroptosis without infection. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10241024NLR family CARD domain-containing protein 4PRO_0000419975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei533 – 5331Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated at Ser-533 following infection of macrophages with S.typhimurium (Salmonella). Phosphorylation is essential for NLRC4 inflammasome function to promote caspase-1 activation and pyroptosis. PRKCD phosphorylates Ser-533 in vitro.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3UP24.
PaxDbiQ3UP24.

PTM databases

iPTMnetiQ3UP24.

Expressioni

Tissue specificityi

Expressed by intestinal mononuclear phagocytes.1 Publication

Gene expression databases

BgeeiQ3UP24.

Interactioni

Subunit structurei

Homooligomer; homooligomerizes following activation of Naip proteins by pathogenic proteins such as S.typhimurium (Salmonella) flagellin or PrgJ. Component of the NLRC4 inflammasome, at least composed of NLRC4, caspase-1 (CASP1) and some NAIP protein (Naip, Naip2 or Naip5). Interacts with Naip5 and Naip6; following Naip5 and Naip6 engagement by Salmonella flagellin. Interacts with Naip2; following Naip2 engagement by Salmonella PrgJ. Interacts with EIF2AK2/PKR (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059637.

Structurei

Secondary structure

1
1024
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi95 – 10915Combined sources
Helixi112 – 1154Combined sources
Turni130 – 1334Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi148 – 1525Combined sources
Helixi154 – 1596Combined sources
Beta strandi163 – 1686Combined sources
Helixi175 – 18814Combined sources
Helixi193 – 1964Combined sources
Beta strandi198 – 2047Combined sources
Helixi205 – 2073Combined sources
Helixi212 – 2209Combined sources
Helixi229 – 23911Combined sources
Helixi240 – 2423Combined sources
Beta strandi243 – 2486Combined sources
Helixi250 – 2523Combined sources
Turni255 – 2573Combined sources
Helixi259 – 2668Combined sources
Turni269 – 2713Combined sources
Beta strandi274 – 2785Combined sources
Helixi284 – 2874Combined sources
Turni288 – 2903Combined sources
Beta strandi292 – 2976Combined sources
Helixi302 – 31211Combined sources
Helixi315 – 32713Combined sources
Helixi329 – 3346Combined sources
Helixi338 – 35013Combined sources
Helixi359 – 37416Combined sources
Helixi375 – 3773Combined sources
Helixi386 – 40318Combined sources
Helixi416 – 4249Combined sources
Beta strandi426 – 4294Combined sources
Helixi444 – 45916Combined sources
Helixi464 – 47512Combined sources
Helixi480 – 4856Combined sources
Helixi488 – 49710Combined sources
Helixi499 – 50911Combined sources
Helixi519 – 5213Combined sources
Helixi534 – 5385Combined sources
Helixi542 – 56524Combined sources
Helixi572 – 5798Combined sources
Beta strandi583 – 5897Combined sources
Helixi593 – 6019Combined sources
Helixi603 – 6086Combined sources
Beta strandi609 – 61810Combined sources
Helixi646 – 6549Combined sources
Beta strandi659 – 66810Combined sources
Helixi674 – 68411Combined sources
Beta strandi687 – 69610Combined sources
Helixi703 – 7075Combined sources
Beta strandi712 – 72110Combined sources
Helixi726 – 7349Combined sources
Beta strandi740 – 7467Combined sources
Turni755 – 7584Combined sources
Beta strandi767 – 7737Combined sources
Helixi777 – 78711Combined sources
Beta strandi794 – 8007Combined sources
Helixi807 – 81610Combined sources
Beta strandi824 – 8307Combined sources
Helixi834 – 84310Combined sources
Helixi844 – 8463Combined sources
Beta strandi852 – 8543Combined sources
Helixi864 – 87310Combined sources
Helixi874 – 8774Combined sources
Beta strandi883 – 8864Combined sources
Helixi892 – 8954Combined sources
Helixi896 – 9027Combined sources
Helixi903 – 9053Combined sources
Beta strandi911 – 9166Combined sources
Helixi921 – 93313Combined sources
Beta strandi941 – 9466Combined sources
Helixi951 – 96111Combined sources
Beta strandi969 – 9713Combined sources
Beta strandi975 – 9773Combined sources
Helixi981 – 99313Combined sources
Beta strandi999 – 10013Combined sources
Beta strandi1008 – 10103Combined sources
Helixi1012 – 10154Combined sources
Beta strandi1018 – 10225Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JBLelectron microscopy4.50A/B/C/D/E/F/G/H/I/J/K93-1024[»]
4KXFX-ray3.20B/D/F/H/K/L/N/P1-1024[»]
5AJ2electron microscopy40.00A1-355[»]
B356-580[»]
C580-1024[»]
ProteinModelPortaliQ3UP24.
SMRiQ3UP24. Positions 1-1024.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8888CARDPROSITE-ProRule annotationAdd
BLAST
Domaini163 – 476314NACHTPROSITE-ProRule annotationAdd
BLAST
Repeati578 – 59821LRR 11 PublicationAdd
BLAST
Repeati656 – 67924LRR 21 PublicationAdd
BLAST
Repeati735 – 75824LRR 31 PublicationAdd
BLAST
Repeati762 – 78524LRR 41 PublicationAdd
BLAST
Repeati787 – 81226LRR 51 PublicationAdd
BLAST
Repeati824 – 84724LRR 61 PublicationAdd
BLAST
Repeati848 – 87023LRR 71 PublicationAdd
BLAST
Repeati878 – 90225LRR 81 PublicationAdd
BLAST
Repeati911 – 93323LRR 91 PublicationAdd
BLAST
Repeati936 – 96328LRR 101 PublicationAdd
BLAST
Repeati965 – 98521LRR 111 PublicationAdd
BLAST
Repeati999 – 102123LRR 121 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 298204Nucleotide-binding domain (NBD)Add
BLAST
Regioni356 – 463108Winged-helix domain (WHD)Add
BLAST

Domaini

In an autoinhibited form the C-terminal leucine-rich repeat (LRR) domain is positioned to sterically occlude one side of the NBD domain and consequently sequester NLRC4 in a monomeric state. An ADP-mediated interaction between the NBD and the WHD also contributes to the autoinhibition (PubMed:23765277).1 Publication

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation
Contains 12 LRR (leucine-rich) repeats.Curated
Contains 1 NACHT domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiENOG410IHIG. Eukaryota.
ENOG410YI2E. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000059630.
HOVERGENiHBG050790.
InParanoidiQ3UP24.
KOiK12805.
OMAiDLFVWNV.
OrthoDBiEOG73BVBV.
PhylomeDBiQ3UP24.
TreeFamiTF336864.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR032675. L_dom-like.
IPR007111. NACHT_NTPase.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UP24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFIRNNRRA LIQRMGLTVT KQICDDLFAL NVLNNQEANV IYCEPLEQEA
60 70 80 90 100
ARKIIHMTMQ KGSAACNLFL KSLENWDYFV YQDLTGQNLS YQVTEEDLNV
110 120 130 140 150
LAQNLKDLYN SPAFLNFYPL GEDIDIIFNL EKTFTEPIMW KKDHRHHRVE
160 170 180 190 200
QLTLGSLLEA LKSPCLIEGE SGKGKSTLLQ RIAMLWASGG CRALKGFRLV
210 220 230 240 250
FFIHLRSARG GLFETLYDQL LNIPDFISKP TFKALLLKLH KEVLFLLDGY
260 270 280 290 300
NEFHPQNCPE IEALIKENHR FKNMVIVTTT TECLRHIRHV GALTAEVGDM
310 320 330 340 350
TEDSAKDLIE AVLVPDQVER LWAQIQESRC LRNLMKTPLF VVITCAIQMG
360 370 380 390 400
RQEFQAHTQT MLFQTFYDLL IQKNSHRYRG GASGDFARSL DYCGDLALEG
410 420 430 440 450
VFAHKFDFEP EHGSSMNEDV LVTIGLLCKY TAQRLKPTYK FFHKSFQEYT
460 470 480 490 500
AGRRLSSLLT SKEPEEVSKG NSYLNKMVSI SDITSLYGNL LLYTCGSSTE
510 520 530 540 550
ATRAVMRHLA MVYQHGSLQG LSVTKRPLWR QESIQSLRNT TEQDVLKAIN
560 570 580 590 600
VNSFVECGIN LFSESMSKSD LSQEFEAFFQ GKSLYINSEN IPDYLFDFFE
610 620 630 640 650
YLPNCASALD FVKLDFYERA TESQDKAEEN VPGVHTEGPS ETYIPPRAVS
660 670 680 690 700
LFFNWKQEFK TLEVTLRDIN KLNKQDIKYL GKIFSSATNL RLHIKRCAAM
710 720 730 740 750
AGRLSSVLRT CKNMHTLMVE ASPLTTDDEQ YITSVTGLQN LSIHRLHTQQ
760 770 780 790 800
LPGGLIDSLG NLKNLERLIL DDIRMNEEDA KNLAEGLRSL KKMRLLHLTH
810 820 830 840 850
LSDIGEGMDY IVKSLSEESC DLQEMKLVAC CLTANSVKVL AQNLHNLIKL
860 870 880 890 900
SILDISENYL EKDGNEALQE LIGRLGVLGE LTTLMLPWCW DVHTSLPKLL
910 920 930 940 950
KQLEGTPGLA KLGLKNWRLR DEEIKSLGEF LEMNPLRDLQ QLDLAGHCVS
960 970 980 990 1000
SDGWLYFMNV FENLKQLVFF DFSTEEFLPD AALVRKLSQV LSKLTLLQEV
1010 1020
KLTGWEFDDY DISAIKGTFK LVTA
Length:1,024
Mass (Da):116,749
Last modified:October 11, 2005 - v1
Checksum:i15F192E8F00FF017
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991N → S in BAE42570 (PubMed:16141072).Curated
Sequence conflicti385 – 3851D → N in BAE42570 (PubMed:16141072).Curated
Sequence conflicti515 – 5151H → Y in BAE42570 (PubMed:16141072).Curated
Sequence conflicti670 – 6701N → S in BAE42570 (PubMed:16141072).Curated
Sequence conflicti756 – 7561I → V in BAE42570 (PubMed:16141072).Curated
Sequence conflicti782 – 7821N → S in BAE42570 (PubMed:16141072).Curated
Sequence conflicti799 – 7991T → I in BAE42570 (PubMed:16141072).Curated
Sequence conflicti948 – 9481C → R in BAE42570 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK143864 mRNA. Translation: BAE25573.1.
AK171624 mRNA. Translation: BAE42570.1.
CT033749 Genomic DNA. No translation available.
CCDSiCCDS37692.1.
RefSeqiNP_001028539.1. NM_001033367.3.
XP_006524408.1. XM_006524345.2.
XP_006524409.1. XM_006524346.2.
UniGeneiMm.311884.

Genome annotation databases

EnsembliENSMUST00000052124; ENSMUSP00000059637; ENSMUSG00000039193.
GeneIDi268973.
KEGGimmu:268973.
UCSCiuc008doc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK143864 mRNA. Translation: BAE25573.1.
AK171624 mRNA. Translation: BAE42570.1.
CT033749 Genomic DNA. No translation available.
CCDSiCCDS37692.1.
RefSeqiNP_001028539.1. NM_001033367.3.
XP_006524408.1. XM_006524345.2.
XP_006524409.1. XM_006524346.2.
UniGeneiMm.311884.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JBLelectron microscopy4.50A/B/C/D/E/F/G/H/I/J/K93-1024[»]
4KXFX-ray3.20B/D/F/H/K/L/N/P1-1024[»]
5AJ2electron microscopy40.00A1-355[»]
B356-580[»]
C580-1024[»]
ProteinModelPortaliQ3UP24.
SMRiQ3UP24. Positions 1-1024.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059637.

PTM databases

iPTMnetiQ3UP24.

Proteomic databases

MaxQBiQ3UP24.
PaxDbiQ3UP24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052124; ENSMUSP00000059637; ENSMUSG00000039193.
GeneIDi268973.
KEGGimmu:268973.
UCSCiuc008doc.1. mouse.

Organism-specific databases

CTDi58484.
MGIiMGI:3036243. Nlrc4.

Phylogenomic databases

eggNOGiENOG410IHIG. Eukaryota.
ENOG410YI2E. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000059630.
HOVERGENiHBG050790.
InParanoidiQ3UP24.
KOiK12805.
OMAiDLFVWNV.
OrthoDBiEOG73BVBV.
PhylomeDBiQ3UP24.
TreeFamiTF336864.

Miscellaneous databases

NextBioi392615.
PROiQ3UP24.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UP24.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR032675. L_dom-like.
IPR007111. NACHT_NTPase.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS50837. NACHT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis."
    Lara-Tejero M., Sutterwala F.S., Ogura Y., Grant E.P., Bertin J., Coyle A.J., Flavell R.A., Galan J.E.
    J. Exp. Med. 203:1407-1412(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  4. "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf."
    Mariathasan S., Newton K., Monack D.M., Vucic D., French D.M., Lee W.P., Roose-Girma M., Erickson S., Dixit V.M.
    Nature 430:213-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf."
    Miao E.A., Alpuche-Aranda C.M., Dors M., Clark A.E., Bader M.W., Miller S.I., Aderem A.
    Nat. Immunol. 7:569-575(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages."
    Franchi L., Amer A., Body-Malapel M., Kanneganti T.D., Ozoren N., Jagirdar R., Inohara N., Vandenabeele P., Bertin J., Coyle A., Grant E.P., Nunez G.
    Nat. Immunol. 7:576-582(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome."
    Sutterwala F.S., Mijares L.A., Li L., Ogura Y., Kazmierczak B.I., Flavell R.A.
    J. Exp. Med. 204:3235-3245(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: FUNCTION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  10. "Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella."
    Broz P., Newton K., Lamkanfi M., Mariathasan S., Dixit V.M., Monack D.M.
    J. Exp. Med. 207:1745-1755(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome."
    Miao E.A., Mao D.P., Yudkovsky N., Bonneau R., Lorang C.G., Warren S.E., Leaf I.A., Aderem A.
    Proc. Natl. Acad. Sci. U.S.A. 107:3076-3080(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity."
    Kofoed E.M., Vance R.E.
    Nature 477:592-595(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH NAIP2; NAIP5 AND NAIP6.
  13. "The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus."
    Zhao Y., Yang J., Shi J., Gong Y.N., Lu Q., Xu H., Liu L., Shao F.
    Nature 477:596-600(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NAIP2 AND NAIP5.
  14. "A novel role for the NLRC4 inflammasome in mucosal defenses against the fungal pathogen Candida albicans."
    Tomalka J., Ganesan S., Azodi E., Patel K., Majmudar P., Hall B.A., Fitzgerald K.A., Hise A.G.
    PLoS Pathog. 7:E1002379-E1002379(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "NLRC4 inflammasome-mediated production of IL-1beta modulates mucosal immunity in the lung against gram-negative bacterial infection."
    Cai S., Batra S., Wakamatsu N., Pacher P., Jeyaseelan S.
    J. Immunol. 188:5623-5635(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: FUNCTION.
  17. "NLRC4-driven production of IL-1beta discriminates between pathogenic and commensal bacteria and promotes host intestinal defense."
    Franchi L., Kamada N., Nakamura Y., Burberry A., Kuffa P., Suzuki S., Shaw M.H., Kim Y.G., Nunez G.
    Nat. Immunol. 13:449-456(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  18. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-533, MUTAGENESIS OF SER-533.
  19. "Crystal structure of NLRC4 reveals its autoinhibition mechanism."
    Hu Z., Yan C., Liu P., Huang Z., Ma R., Zhang C., Wang R., Zhang Y., Martinon F., Miao D., Deng H., Wang J., Chang J., Chai J.
    Science 341:172-175(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 93-1024 IN COMPLEX WITH ADP, NBD DOMAIN, WHD DOMAIN, LRR REPEATS, PHOSPHORYLATION AT SER-533, MUTAGENESIS OF HIS-443.

Entry informationi

Entry nameiNLRC4_MOUSE
AccessioniPrimary (citable) accession number: Q3UP24
Secondary accession number(s): Q3TAU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: October 11, 2005
Last modified: May 11, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.