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Caspase recruitment domain family, member 15 (Predicted) (Nucleotide-binding oligomerization domain-containing 2)

 D4A5W3_RAT              Unreviewed;       932 AA.
D4A5W3;
20-APR-2010, integrated into UniProtKB/TrEMBL.
20-APR-2010, sequence version 1.
31-JAN-2018, entry version 76.
SubName: Full=Caspase recruitment domain family, member 15 (Predicted) {ECO:0000313|EMBL:EDL87529.1};
SubName: Full=Nucleotide-binding oligomerization domain-containing 2 {ECO:0000313|Ensembl:ENSRNOP00000061463};
Name=Nod2 {ECO:0000313|Ensembl:ENSRNOP00000061463,
ECO:0000313|RGD:1306368};
Synonyms=Card15_predicted {ECO:0000313|EMBL:EDL87529.1};
ORFNames=rCG_63140 {ECO:0000313|EMBL:EDL87529.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000061463, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000061463, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061463,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
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.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDL87529.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL87529.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDL87529.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL87529.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Ensembl:ENSRNOP00000061463}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000061463};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
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EMBL; AABR07043075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07043076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474037; EDL87529.1; -; Genomic_DNA.
RefSeq; NP_001099642.1; NM_001106172.1.
UniGene; Rn.218600; -.
STRING; 10116.ENSRNOP00000061463; -.
Ensembl; ENSRNOT00000065103; ENSRNOP00000061463; ENSRNOG00000014124.
GeneID; 291912; -.
KEGG; rno:291912; -.
CTD; 64127; -.
RGD; 1306368; Nod2.
eggNOG; KOG4308; Eukaryota.
eggNOG; ENOG410ZBX3; LUCA.
GeneTree; ENSGT00860000133673; -.
KO; K10165; -.
Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
Reactome; R-RNO-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-RNO-446652; Interleukin-1 family signaling.
Reactome; R-RNO-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
Proteomes; UP000002494; Chromosome 19.
Bgee; ENSRNOG00000014124; -.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005856; C:cytoskeleton; ISO:RGD.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0043234; C:protein complex; ISO:RGD.
GO; GO:0031982; C:vesicle; ISO:RGD.
GO; GO:0003779; F:actin binding; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0050700; F:CARD domain binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
GO; GO:0032500; F:muramyl dipeptide binding; IDA:RGD.
GO; GO:0042834; F:peptidoglycan binding; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0002253; P:activation of immune response; ISO:RGD.
GO; GO:0071225; P:cellular response to muramyl dipeptide; ISO:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0071224; P:cellular response to peptidoglycan; IEP:RGD.
GO; GO:0002367; P:cytokine production involved in immune response; ISO:RGD.
GO; GO:0002374; P:cytokine secretion involved in immune response; ISO:RGD.
GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
GO; GO:0016045; P:detection of bacterium; ISO:RGD.
GO; GO:0032498; P:detection of muramyl dipeptide; ISO:RGD.
GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISO:RGD.
GO; GO:0045087; P:innate immune response; ISO:RGD.
GO; GO:0002227; P:innate immune response in mucosa; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
GO; GO:0071608; P:macrophage inflammatory protein-1 alpha production; ISO:RGD.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:RGD.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; ISO:RGD.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:RGD.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:RGD.
GO; GO:0032701; P:negative regulation of interleukin-18 production; ISO:RGD.
GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISO:RGD.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
GO; GO:0002710; P:negative regulation of T cell mediated immunity; ISO:RGD.
GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; ISO:RGD.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:RGD.
GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; ISO:RGD.
GO; GO:0050871; P:positive regulation of B cell activation; ISO:RGD.
GO; GO:0006965; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:RGD.
GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; ISO:RGD.
GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IDA:RGD.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; ISO:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
GO; GO:0045089; P:positive regulation of innate immune response; ISO:RGD.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; ISO:RGD.
GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:RGD.
GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:RGD.
GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:RGD.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:RGD.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:RGD.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; ISO:RGD.
GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; ISO:RGD.
GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; ISO:RGD.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
GO; GO:0002830; P:positive regulation of type 2 immune response; ISO:RGD.
GO; GO:1904417; P:positive regulation of xenophagy; ISO:RGD.
GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISO:RGD.
GO; GO:0043330; P:response to exogenous dsRNA; ISO:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
GO; GO:0032495; P:response to muramyl dipeptide; IDA:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0032494; P:response to peptidoglycan; ISO:RGD.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00619; CARD; 2.
Pfam; PF13516; LRR_6; 3.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50209; CARD; 2.
PROSITE; PS50837; NACHT; 1.
4: Predicted;
ATP-binding {ECO:0000256|SAAS:SAAS00074409};
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00074409};
Reference proteome {ECO:0000313|Proteomes:UP000002494}.
DOMAIN 1 82 CARD. {ECO:0000259|PROSITE:PS50209}.
DOMAIN 107 191 CARD. {ECO:0000259|PROSITE:PS50209}.
DOMAIN 266 402 NACHT. {ECO:0000259|PROSITE:PS50837}.
SEQUENCE 932 AA; 103398 MW; C0A7A4271FF7DEA9 CRC64;
MCSQEDFQAQ RSQLVALLVS GSLEGFESIL DWLLSWDVLS REDYEGLSLP GQPLSHSARR
LLDTVCNKGV WGCQKLFEAV QEAQANSHTF ELQGCWDVHS LHPTRDLQSH RPAIVRRLCS
HVEAILELAR DEGFLSQYEC EEIRLPIFTS SQRARRLLDL AAVKANGLAA FLLQHVRKLP
ASLSLPYEAA ECQKFTAKLR TMVSAQSRFL STYDGSENLC LEDIYTENTL ELRTEVGTAG
ALQKSPATLG LEELFGTHGH LNKDADTILV VGEAGSGKST LLQRLHLLWA SGQNFREFLF
IFPFSCRQLQ CMTKPLSLRT LLFEHCCWPD VGQDDVFQFL LDHPDRVLLT FDGLDEFKFR
FTDRERHCSP LDPTSVQTLL FNLLQGNLLK NACKVLTSRP DAVSALLRKF VRTECHLKGF
SEEGIKLYLR KHHREPGVAD RLIHLIQATS ALHGLCHLPV FSWMVSRCHR ELLLQNRGFP
TTSTDMYLLI LQHFLLHASP PDSFPLGLGP GLLQSRLSTL LHLGHLALQG LAMSCYVFSA
QQLQAAQVDS EDISLGFLVR AQSVVPGSKA PLEFLHITFQ CFFAAFYLAV SADTSAASLK
HLFSCGRPGN SLLLRLLPNL CIQGSRVKGG QAALLQKAEP HNLQITAAFL AGLLSQQHRD
LLAACQVPER VLLQRQARAR SCLAHSLREH FHSIPPAVPG ETKSMHAMPG FIWLIRSLYE
MQEVQLAREA VRRLDIGHLK LTFCRVGPAE CAALAFVLQH LQRPVALQLD HNSVGDVGVE
QLLPCLGVCT ALYLRDNNIS DRGARTLVEC ALRCEQLQKL ALFNNKLTDG CASSVAKLLA
HKQNFLSLRV GNNHITAAGA EVLAQGLKSN TSLQFLGFWG NSVGDKGSQA LAEVVADHQR
LKWLSLVGNN IGSVGAHALA LMLEKNKSLE EL


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