ASC_MOUSE
ID ASC_MOUSE Reviewed; 193 AA.
AC Q9EPB4; Q9D2W9;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Apoptosis-associated speck-like protein containing a CARD;
DE Short=mASC;
DE AltName: Full=PYD and CARD domain-containing protein;
GN Name=Pycard; Synonyms=Asc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=11139337; DOI=10.1006/excr.2000.5078;
RA Masumoto J., Taniguchi S., Nakayama K., Ayukawa K., Sagara J.;
RT "Murine ortholog of ASC, a CARD-containing protein, self-associates and
RT exhibits restricted distribution in developing mouse embryos.";
RL Exp. Cell Res. 262:128-133(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RA Martinon F., Hofmann K., Tschopp J.;
RT "Pycard a PYD and CARD containing molecule.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15507117; DOI=10.1111/j.1365-2443.2004.00789.x;
RA Yamamoto M., Yaginuma K., Tsutsui H., Sagara J., Guan X., Seki E.,
RA Yasuda K., Yamamoto M., Akira S., Nakanishi K., Noda T., Taniguchi S.;
RT "ASC is essential for LPS-induced activation of procaspase-1 independently
RT of TLR-associated signal adaptor molecules.";
RL Genes Cells 9:1055-1067(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15190255; DOI=10.1038/nature02664;
RA Mariathasan S., Newton K., Monack D.M., Vucic D., French D.M., Lee W.P.,
RA Roose-Girma M., Erickson S., Dixit V.M.;
RT "Differential activation of the inflammasome by caspase-1 adaptors ASC and
RT Ipaf.";
RL Nature 430:213-218(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21892172; DOI=10.1038/ni.2095;
RA Ippagunta S.K., Malireddi R.K., Shaw P.J., Neale G.A., Walle L.V.,
RA Green D.R., Fukui Y., Lamkanfi M., Kanneganti T.D.;
RT "The inflammasome adaptor ASC regulates the function of adaptive immune
RT cells by controlling Dock2-mediated Rac activation and actin
RT polymerization.";
RL Nat. Immunol. 12:1010-1016(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CASP8.
RX PubMed=22555457; DOI=10.1038/cdd.2012.51;
RA Pierini R., Juruj C., Perret M., Jones C.L., Mangeot P., Weiss D.S.,
RA Henry T.;
RT "AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected
RT caspase-1-deficient macrophages.";
RL Cell Death Differ. 19:1709-1721(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
RA Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J., Fang R.,
RA Meng G., Su X., Jiang Z.;
RT "Inflammasome activation triggers caspase-1-mediated cleavage of cGAS to
RT regulate responses to DNA virus infection.";
RL Immunity 46:393-404(2017).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NLRP6.
RX PubMed=32424362; DOI=10.1038/s41590-020-0681-x;
RA Mukherjee S., Kumar R., Tsakem Lenou E., Basrur V., Kontoyiannis D.L.,
RA Ioakeimidis F., Mosialos G., Theiss A.L., Flavell R.A., Venuprasad K.;
RT "Deubiquitination of NLRP6 inflammasome by Cyld critically regulates
RT intestinal inflammation.";
RL Nat. Immunol. 21:626-635(2020).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NLRP6.
RX PubMed=34678144; DOI=10.1016/j.cell.2021.09.032;
RA Shen C., Li R., Negro R., Cheng J., Vora S.M., Fu T.M., Wang A., He K.,
RA Andreeva L., Gao P., Tian Z., Flavell R.A., Zhu S., Wu H.;
RT "Phase separation drives RNA virus-induced activation of the NLRP6
RT inflammasome.";
RL Cell 184:5759-5774(2021).
RN [13]
RP IDENTIFICATION IN THE AIM2 PANOPTOSOME COMPLEX.
RX PubMed=34471287; DOI=10.1038/s41586-021-03875-8;
RA Lee S., Karki R., Wang Y., Nguyen L.N., Kalathur R.C., Kanneganti T.D.;
RT "AIM2 forms a complex with pyrin and ZBP1 to drive PANoptosis and host
RT defence.";
RL Nature 597:415-419(2021).
CC -!- FUNCTION: Functions as key mediator in apoptosis and inflammation.
CC Promotes caspase-mediated apoptosis involving predominantly caspase-8
CC and also caspase-9 in a probable cell type-specific manner. Involved in
CC activation of the mitochondrial apoptotic pathway, promotes caspase-8-
CC dependent proteolytic maturation of BID independently of FADD in
CC certain cell types and also mediates mitochondrial translocation of BAX
CC and activates BAX-dependent apoptosis coupled to activation of caspase-
CC 9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent
CC inflammatory form of cell death and is the major constituent of the ASC
CC pyroptosome which forms upon potassium depletion and rapidly recruits
CC and activates caspase-1. In innate immune response, acts as integral
CC adapter in the assembly of the inflammasome which activates caspase-1
CC leading to processing and secretion of pro-inflammatory cytokines. The
CC function as activating adapter in different types of inflammasomes is
CC mediated by the pyrin and CARD domains and their homotypic
CC interactions. Required for recruitment of caspase-1 to inflammasomes
CC containing certain pattern recognition receptors, such as NLRP2, NLRP3,
CC NLRP6, AIM2 and probably IFI16 (PubMed:32424362, PubMed:34678144). In
CC the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates
CC the processing of procaspase-1. In cooperation with NOD2 involved in an
CC inflammasome activated by bacterial muramyl dipeptide leading to
CC caspase-1 activation. May be involved in DDX58-triggered pro-
CC inflammatory responses and inflammasome activation. In collaboration
CC with AIM2 which detects cytosolic double-stranded DNA may also be
CC involved in a caspase-1-independent cell death that involves caspase-8.
CC In adaptive immunity may be involved in maturation of dendritic cells
CC to stimulate T-cell immunity and in cytoskeletal rearrangements coupled
CC to chemotaxis and antigen uptake may be involved in post-
CC transcriptional regulation of the guanine nucleotide exchange factor
CC DOCK2; the latter function is proposed to involve the nuclear form.
CC Also involved in transcriptional activation of cytokines and chemokines
CC independent of the inflammasome; this function may involve AP-1, NF-
CC kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-
CC kappa-B activating and inhibiting functions have been reported.
CC Modulates NF-kappa-B induction at the level of the IKK complex by
CC inhibiting kinase activity of CHUK and IKBK. Proposed to compete with
CC RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated
CC RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta
CC processing. Modulates host resistance to DNA virus infection, probably
CC by inducing the cleavage of and inactivating CGAS in presence of
CC cytoplasmic double-stranded DNA (PubMed:28314590).
CC {ECO:0000269|PubMed:15190255, ECO:0000269|PubMed:15507117,
CC ECO:0000269|PubMed:21892172, ECO:0000269|PubMed:22555457,
CC ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:32424362,
CC ECO:0000269|PubMed:34678144}.
CC -!- SUBUNIT: Self-associates; enforced oligomerization induces apoptosis,
CC NF-kappa-B regulation and interleukin-1 beta secretion (By similarity).
CC Homooligomers can form disk-like particles of approximately 12 nm
CC diameter and approximately 1 nm height (By similarity). Component of
CC several inflammasomes containing one pattern recognition
CC receptor/sensor, such as NLRP2, NLRP3, NLRP6, NLRC4, AIM2, MEFV or
CC NOD2, and probably NLRC4, NLRP12 or IFI16 (PubMed:32424362,
CC PubMed:34678144). Major component of the ASC pyroptosome, a 1-2 um
CC supramolecular assembly (one per macrophage cell) which consists of
CC oligomerized PYCARD dimers and CASP1 (By similarity). Interacts with
CC CASP1 (precursor form); the interaction induces activation of CASP1
CC leading to the processing of interleukin-1 beta; PYCARD competes with
CC RIPK2 for binding to CASP1 (By similarity). Interacts with NLRP3; the
CC interaction requires the homooligomerization of NLRP3 (By similarity).
CC Interacts with NLRP2, NLRC4, MEFV, CARD16, AIM2, IFI16, NOD2, DDX58,
CC RIPK2, PYDC1, PYDC2, NLRP10, CHUK, IKBKB and BAX (By similarity).
CC Interacts with CASP8 (PubMed:22555457). Component of the AIM2
CC PANoptosome complex, a multiprotein complex that drives inflammatory
CC cell death (PANoptosis) (PubMed:34471287).
CC {ECO:0000250|UniProtKB:Q9ULZ3, ECO:0000269|PubMed:22555457,
CC ECO:0000269|PubMed:32424362, ECO:0000269|PubMed:34471287,
CC ECO:0000269|PubMed:34678144}.
CC -!- INTERACTION:
CC Q9EPB4; P29452: Casp1; NbExp=2; IntAct=EBI-6253348, EBI-489700;
CC Q9EPB4; Q8R4B8: Nlrp3; NbExp=3; IntAct=EBI-6253348, EBI-6910832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11139337,
CC ECO:0000269|PubMed:21892172, ECO:0000269|PubMed:22555457}. Inflammasome
CC {ECO:0000269|PubMed:32424362, ECO:0000269|PubMed:34678144}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q9ULZ3}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9ULZ3}. Nucleus {ECO:0000250|UniProtKB:Q9ULZ3}.
CC Note=Upstream of caspase activation, a redistribution from the
CC cytoplasm to the aggregates occurs. These appear as hollow, perinuclear
CC spherical, ball-like structures. Upon NLRP3 inflammasome activation
CC redistributes to the perinuclear space localizing to endoplasmic
CC reticulum and mitochondria. Localized primarily to the nucleus in
CC resting monocytes/macrophages and rapidly redistributed to the
CC cytoplasm upon pathogen infection (By similarity). Localized to large
CC cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD,
CC CASP8 and bacterial DNA after infection with Francisella tularensis
CC (PubMed:22555457). {ECO:0000250|UniProtKB:Q9ULZ3,
CC ECO:0000269|PubMed:22555457}.
CC -!- TISSUE SPECIFICITY: Expressed in small intestine, colon, thymus,
CC spleen, brain, heart, skeletal muscle, kidney, lung and liver.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed at 9.5 dpc in the
CC telencephalon, thalamic areas of the diencephalon, heart and liver.
CC -!- DOMAIN: The CARD domain mediates interaction with CASP1 and NLRC4.
CC {ECO:0000250|UniProtKB:Q9ULZ3}.
CC -!- DOMAIN: The pyrin domain mediates homotypic interactions with pyrin
CC domains of proteins such as of NLRP3, PYDC1, PYDC2 and AIM2.
CC {ECO:0000250|UniProtKB:Q9ULZ3}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9ULZ3}.
CC -!- PTM: 'Lys-63'-linked polyubiquitination by TRAF3 is critical for speck
CC formation and inflammasome activation. {ECO:0000250|UniProtKB:Q9ULZ3}.
CC -!- DISRUPTION PHENOTYPE: Increased resistance to endotoxic shock and
CC severe defects in caspase-1 activation and interleukin-1 beta and
CC interleukin-18 production in macrophages in response to several pro-
CC inflammatory molecules (PubMed:15190255, PubMed:15507117). Mutants are
CC resitant to vaccinia virus (VACV) but not vesicular somatitis virus
CC (VSV) infection. They show lower viral loads in the lungs compared to
CC wild type mice, they produce higher levels of type I IFN, IL6 and
CC RSAD2/Viperin after VCAV INFECTION (PubMed:28314590).
CC {ECO:0000269|PubMed:15190255, ECO:0000269|PubMed:15507117,
CC ECO:0000269|PubMed:28314590}.
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DR EMBL; AB032249; BAB16609.1; -; mRNA.
DR EMBL; AF310104; AAG30287.1; -; mRNA.
DR EMBL; AK009852; BAB26543.1; -; mRNA.
DR EMBL; AK007742; BAB25229.1; -; mRNA.
DR EMBL; AK018682; BAB31341.1; -; mRNA.
DR EMBL; BC008252; AAH08252.1; -; mRNA.
DR CCDS; CCDS21888.1; -.
DR RefSeq; NP_075747.3; NM_023258.4.
DR PDB; 2N1F; Other; 4.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-90.
DR PDBsum; 2N1F; -.
DR AlphaFoldDB; Q9EPB4; -.
DR SMR; Q9EPB4; -.
DR BioGRID; 211743; 5.
DR ComplexPortal; CPX-4241; NLRP3 inflammasome.
DR ComplexPortal; CPX-4243; AIM2 inflammasome.
DR ComplexPortal; CPX-4244; Pyrin inflammasome.
DR CORUM; Q9EPB4; -.
DR DIP; DIP-27619N; -.
DR IntAct; Q9EPB4; 11.
DR MINT; Q9EPB4; -.
DR STRING; 10090.ENSMUSP00000033056; -.
DR iPTMnet; Q9EPB4; -.
DR PhosphoSitePlus; Q9EPB4; -.
DR CPTAC; non-CPTAC-3636; -.
DR EPD; Q9EPB4; -.
DR jPOST; Q9EPB4; -.
DR MaxQB; Q9EPB4; -.
DR PaxDb; Q9EPB4; -.
DR PRIDE; Q9EPB4; -.
DR ProteomicsDB; 277076; -.
DR Antibodypedia; 3375; 744 antibodies from 45 providers.
DR DNASU; 66824; -.
DR Ensembl; ENSMUST00000033056; ENSMUSP00000033056; ENSMUSG00000030793.
DR GeneID; 66824; -.
DR KEGG; mmu:66824; -.
DR UCSC; uc009jxu.2; mouse.
DR CTD; 29108; -.
DR MGI; MGI:1931465; Pycard.
DR VEuPathDB; HostDB:ENSMUSG00000030793; -.
DR eggNOG; ENOG502S3G5; Eukaryota.
DR GeneTree; ENSGT00940000161873; -.
DR HOGENOM; CLU_113553_1_0_1; -.
DR InParanoid; Q9EPB4; -.
DR OMA; NPAKMRK; -.
DR OrthoDB; 1494108at2759; -.
DR PhylomeDB; Q9EPB4; -.
DR TreeFam; TF337882; -.
DR Reactome; R-MMU-5660668; CLEC7A/inflammasome pathway.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-844456; The NLRP3 inflammasome.
DR BioGRID-ORCS; 66824; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q9EPB4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9EPB4; protein.
DR Bgee; ENSMUSG00000030793; Expressed in paneth cell and 214 other tissues.
DR ExpressionAtlas; Q9EPB4; baseline and differential.
DR Genevisible; Q9EPB4; MM.
DR GO; GO:0097169; C:AIM2 inflammasome complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0008385; C:IkappaB kinase complex; ISO:MGI.
DR GO; GO:0061702; C:inflammasome complex; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0072558; C:NLRP1 inflammasome complex; ISO:MGI.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; ISS:UniProtKB.
DR GO; GO:0140738; C:NLRP6 inflammasome complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070700; F:BMP receptor binding; ISO:MGI.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005138; F:interleukin-6 receptor binding; ISO:MGI.
DR GO; GO:0017024; F:myosin I binding; ISO:MGI.
DR GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IMP:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR GO; GO:0032090; F:Pyrin domain binding; ISS:HGNC-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005523; F:tropomyosin binding; ISO:MGI.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IMP:CACAO.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0002218; P:activation of innate immune response; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0044351; P:macropinocytosis; IMP:UniProtKB.
DR GO; GO:0001773; P:myeloid dendritic cell activation; ISO:MGI.
DR GO; GO:0002277; P:myeloid dendritic cell activation involved in immune response; IMP:UniProtKB.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0007231; P:osmosensory signaling pathway; IC:ComplexPortal.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; ISO:MGI.
DR GO; GO:0002588; P:positive regulation of antigen processing and presentation of peptide antigen via MHC class II; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:UniProtKB.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:HGNC-UCL.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:ComplexPortal.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:ComplexPortal.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IGI:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISO:MGI.
DR GO; GO:2000406; P:positive regulation of T cell migration; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0070269; P:pyroptosis; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010506; P:regulation of autophagy; IMP:MGI.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR CDD; cd08330; CARD_ASC_NALP1; 1.
DR Gene3D; 1.10.533.10; -; 2.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR033516; CARD8/ASC/NALP1_CARD.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR002398; Pept_C14.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; SSF47986; 2.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50824; DAPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Endoplasmic reticulum; Immunity;
KW Inflammasome; Inflammatory response; Innate immunity; Isopeptide bond;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..193
FT /note="Apoptosis-associated speck-like protein containing a
FT CARD"
FT /id="PRO_0000064693"
FT DOMAIN 1..91
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 105..193
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULZ3"
FT CONFLICT 159
FT /note="K -> E (in Ref. 3; BAB31341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 21459 MW; 2A4EA40194870B31 CRC64;
MGRARDAILD ALENLSGDEL KKFKMKLLTV QLREGYGRIP RGALLQMDAI DLTDKLVSYY
LESYGLELTM TVLRDMGLQE LAEQLQTTKE ESGAVAAAAS VPAQSTARTG HFVDQHRQAL
IARVTEVDGV LDALHGSVLT EGQYQAVRAE TTSQDKMRKL FSFVPSWNLT CKDSLLQALK
EIHPYLVMDL EQS
