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Database: UniProt
Entry: NAL4C_MOUSE
LinkDB: NAL4C_MOUSE
Original site: NAL4C_MOUSE 
ID   NAL4C_MOUSE             Reviewed;         982 AA.
AC   Q3TKR3; Q66X27;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=NACHT, LRR and PYD domains-containing protein 4C;
DE   AltName: Full=NALP-alpha;
GN   Name=Nlrp4c; Synonyms=Nalp4c;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=15317747; DOI=10.1093/hmg/ddh241;
RA   Hamatani T., Falco G., Carter M.G., Akutsu H., Stagg C.A., Sharov A.A.,
RA   Dudekula D.B., VanBuren V., Ko M.S.H.;
RT   "Age-associated alteration of gene expression patterns in mouse oocytes.";
RL   Hum. Mol. Genet. 13:2263-2278(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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).
CC   -!- FUNCTION: May be involved in inflammation and recognition of cytosolic
CC       pathogen-associated molecular patterns (PAMPs) not intercepted by
CC       membrane-bound receptors. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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DR   EMBL; AY596194; AAU06315.1; -; mRNA.
DR   EMBL; AK166817; BAE39043.1; -; mRNA.
DR   EMBL; AK166869; BAE39081.1; -; mRNA.
DR   CCDS; CCDS51988.1; -.
DR   RefSeq; NP_113566.2; NM_031389.2.
DR   AlphaFoldDB; Q3TKR3; -.
DR   SMR; Q3TKR3; -.
DR   BioGRID; 219949; 1.
DR   STRING; 10090.ENSMUSP00000046503; -.
DR   iPTMnet; Q3TKR3; -.
DR   PhosphoSitePlus; Q3TKR3; -.
DR   MaxQB; Q3TKR3; -.
DR   PaxDb; 10090-ENSMUSP00000046503; -.
DR   ProteomicsDB; 293618; -.
DR   DNASU; 83564; -.
DR   Ensembl; ENSMUST00000037728.13; ENSMUSP00000046503.6; ENSMUSG00000034690.14.
DR   Ensembl; ENSMUST00000121583.2; ENSMUSP00000113824.2; ENSMUSG00000034690.14.
DR   Ensembl; ENSMUST00000208360.2; ENSMUSP00000146613.2; ENSMUSG00000034690.14.
DR   GeneID; 83564; -.
DR   KEGG; mmu:83564; -.
DR   UCSC; uc009fan.2; mouse.
DR   AGR; MGI:1890518; -.
DR   CTD; 83564; -.
DR   MGI; MGI:1890518; Nlrp4c.
DR   VEuPathDB; HostDB:ENSMUSG00000034690; -.
DR   eggNOG; ENOG502SGVH; Eukaryota.
DR   GeneTree; ENSGT00940000162284; -.
DR   HOGENOM; CLU_002274_2_1_1; -.
DR   InParanoid; Q3TKR3; -.
DR   OMA; THPDCRV; -.
DR   OrthoDB; 55870at2759; -.
DR   PhylomeDB; Q3TKR3; -.
DR   Reactome; R-MMU-3134975; Regulation of innate immune responses to cytosolic DNA.
DR   Reactome; R-MMU-3270619; IRF3-mediated induction of type I IFN.
DR   BioGRID-ORCS; 83564; 3 hits in 79 CRISPR screens.
DR   PRO; PR:Q3TKR3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q3TKR3; Protein.
DR   Bgee; ENSMUSG00000034690; Expressed in primary oocyte and 30 other cell types or tissues.
DR   Genevisible; Q3TKR3; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045824; P:negative regulation of innate immune response; ISO:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR   CDD; cd08320; Pyrin_NALPs; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR004020; DAPIN.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR007111; NACHT_NTPase.
DR   InterPro; IPR041267; NLRP_HD2.
DR   InterPro; IPR041075; NOD2_WH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45690; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 12; 1.
DR   PANTHER; PTHR45690:SF6; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 4; 1.
DR   Pfam; PF13516; LRR_6; 3.
DR   Pfam; PF05729; NACHT; 1.
DR   Pfam; PF17776; NLRC4_HD2; 1.
DR   Pfam; PF17779; NOD2_WH; 1.
DR   Pfam; PF02758; PYRIN; 1.
DR   SMART; SM00368; LRR_RI; 9.
DR   SMART; SM01289; PYRIN; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50824; DAPIN; 1.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS50837; NACHT; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Inflammatory response; Leucine-rich repeat;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..982
FT                   /note="NACHT, LRR and PYD domains-containing protein 4C"
FT                   /id="PRO_0000286331"
FT   DOMAIN          1..93
FT                   /note="Pyrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT   DOMAIN          148..471
FT                   /note="NACHT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT   REPEAT          594..617
FT                   /note="LRR 1"
FT   REPEAT          689..716
FT                   /note="LRR 2"
FT   REPEAT          746..773
FT                   /note="LRR 3"
FT   REPEAT          802..825
FT                   /note="LRR 4"
FT   REPEAT          827..844
FT                   /note="LRR 5"
FT   REPEAT          859..882
FT                   /note="LRR 6"
FT   REPEAT          916..940
FT                   /note="LRR 7"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT   CONFLICT        892
FT                   /note="E -> Q (in Ref. 1; AAU06315)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   982 AA;  112674 MW;  612D76CC6F0D4398 CRC64;
     MASFFSDFGL MWYLEELNKK EFMKFKEFLK QEILQLRLKQ ISWTEVKKAS REDLANLLLK
     HYEEKKAWDM TFKIFQKMNR KDLMERAGRE IAGHSKLYQA HLKKKLTHDY ARKFNIKVQD
     FSKQKFTQDD YDRFENFLIS KVTAKKPHMV FLQGAAGIGK SLMLTKLMLA WSEGMVFQNK
     FSYIFYFCCQ DVKKMKRASL AELISKEWPK TSAPIEDILS QPEKLLFVID NLEVMECDMS
     ERESELCDTC TEKQPVRILL SSLLRRKMLP KSSFLISATP ETFEKMEGRV ECTNVKIVTG
     FNESNIKMYF RSLFQDKTKT QEIFSLVKEN QQLFTVCQVP VLCWMVATCL KKEIEKGRDL
     VSVCRRTTSL YTTHIFNLFI PQSAQYPSKE SQAQLQSLCS LAAEGMWTDT FVFGEEALRR
     NGIMDSDIPT LLDVRILEKS KKSEKSYIFL HPSIQEVCAA IFYLLKSHMD HPSQDVKSIE
     ALIFTFLKKV KVQWIFFGSF IFGLLHESEQ KKLEAFFGHQ LSQEIKRQLY QCLETISGNE
     ELQEQVDGMK LFYCLFEMDD EAFLAQAMNC MEQINFVAKD YSDVIVAAHC LQHCSTLKKL
     SLSTQNVLSE GQEHSYTEKL LMCWHHMCSV LISSKDIYIL QVKNTNLNET ASLVLYSHLM
     YPSCTLKALV VNNVTFLCDN RLFFELIQNQ CLQHLDLNLT FLSHGDVKLL CDVLSQEECN
     IEKLMVAACN LSPDDCKVFA SVLISSKMLK HLNLSSNNLD KGISSLSKAL CHPDCVLKNL
     VLVNCSLSEQ CWDYLSEVLR RNKTLNHLDI SSNDLKDEGL KVLCGALSLP DSVLKSLSVR
     YCLITTSGCQ DLAEVLRKNQ NLRNLQVSNN KIEDAGVKLL CDAIKHPNCH LENIGLEACA
     LTGACCEDLA SAFTHCKTLW GINLQENALD HSGLIVLFEA LKQQQCTLHV LGLRITDFDK
     ETQELLMAEE EKNPHLSILS SV
//
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