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NACHT, LRR and PYD domains-containing protein 1a (EC 3.4.-.-) (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]

 NLR1A_MOUSE             Reviewed;        1182 AA.
Q2LKU9; M4T3K8; M4T4C8; M4T632; M4TJP5; Q3U0B5; Q67EY4;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
21-FEB-2006, sequence version 1.
02-JUN-2021, entry version 133.
RecName: Full=NACHT, LRR and PYD domains-containing protein 1a;
EC=3.4.-.- {ECO:0000250|UniProtKB:Q9C000};
AltName: Full=Caspase recruitment domain-containing protein 7;
AltName: Full=Death effector filament-forming ced-4-like apoptosis protein;
AltName: Full=Nucleotide-binding domain and caspase recruitment domain;
Contains:
RecName: Full=NACHT, LRR and PYD domains-containing protein 1a, C-terminus {ECO:0000305};
Short=Nlrp1a-CT {ECO:0000250|UniProtKB:Q9C000};
Contains:
RecName: Full=NACHT, LRR and PYD domains-containing protein 1a, N-terminus {ECO:0000305};
Short=Nlrp1a-NT {ECO:0000250|UniProtKB:Q9C000};
Name=Nlrp1a {ECO:0000312|MGI:MGI:2684861};
Synonyms=Card7, Nalp1, Nalp1a {ECO:0000303|PubMed:16429160}, Nlrp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=16429160; DOI=10.1038/ng1724;
Boyden E.D., Dietrich W.F.;
"Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin.";
Nat. Genet. 38:240-244(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LYS-3; TYR-88; GLY-112;
ARG-227; GLU-256; GLN-291; ASN-337; GLY-484; MET-541; HIS-660; ILE-664;
ASP-705; ASN-857; SER-975; GLN-1030; PHE-1043; SER-1110 AND ARG-1181, AND
TISSUE SPECIFICITY.
STRAIN=A/J, AKR/J, CAST/EiJ, DBA/2J, I/LnJ, and PWK/PhJ;
PubMed=23506131; DOI=10.1186/1471-2164-14-188;
Sastalla I., Crown D., Masters S.L., McKenzie A., Leppla S.H., Moayeri M.;
"Transcriptional analysis of the three Nlrp1 paralogs in mice.";
BMC Genomics 14:188-188(2013).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J;
Martinon F., Hofmann K., Tschopp J.;
"Murine NALPs: a family of proteins involved in inflammation.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-488.
STRAIN=NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
FUNCTION, INVOLVEMENT IN INFLAMMASOME, TISSUE SPECIFICITY, AND MUTAGENESIS
OF GLN-593.
PubMed=23219391; DOI=10.1016/j.immuni.2012.08.027;
Masters S.L., Gerlic M., Metcalf D., Preston S., Pellegrini M.,
O'Donnell J.A., McArthur K., Baldwin T.M., Chevrier S., Nowell C.J.,
Cengia L.H., Henley K.J., Collinge J.E., Kastner D.L., Feigenbaum L.,
Hilton D.J., Alexander W.S., Kile B.T., Croker B.A.;
"NLRP1 inflammasome activation induces pyroptosis of hematopoietic
progenitor cells.";
Immunity 37:1009-1023(2012).
[7]
ACTIVITY REGULATION, AND PROTEOLYTIC CLEAVAGE.
PubMed=31383852; DOI=10.1038/s41419-019-1817-5;
Gai K., Okondo M.C., Rao S.D., Chui A.J., Ball D.P., Johnson D.C.,
Bachovchin D.A.;
"DPP8/9 inhibitors are universal activators of functional NLRP1 alleles.";
Cell Death Dis. 10:587-587(2019).
-!- FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome,
which mediates inflammasome activation in response to various pathogen-
associated signals, leading to subsequent pyroptosis (PubMed:23219391).
Inflammasomes are supramolecular complexes that assemble in the cytosol
in response to pathogens and other damage-associated signals and play
critical roles in innate immunity and inflammation (By similarity).
Acts as a recognition receptor (PRR): recognizes specific pathogens and
other damage-associated signals, and mediates the formation of the
inflammasome polymeric complex (By similarity). In response to
pathogen-associated signals, the N-terminal part of Nlrp1a is degraded
by the proteasome, releasing the cleaved C-terminal part of the protein
(NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which
polymerizes to initiate the formation of the inflammasome complex: the
inflammasome recruits pro-caspase-1 (proCASP1) and promotes caspase-1
(CASP1) activation, which subsequently cleaves and activates
inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading
to pyroptosis (By similarity). Activation of Nlrp1a inflammasome is
also required for HMGB1 secretion; the active cytokines and HMGB1
stimulate inflammatory responses (By similarity). When activated in the
bone marrow, induces the pyroptosis of hematopoietic stem cells and
progenitor cells of both myeloid and lymphoid lineages, hence allowing
the removal of damaged cells, and the release of IL1B, which induces
granulopoiesis (PubMed:23219391). {ECO:0000250|UniProtKB:Q9C000,
ECO:0000269|PubMed:23219391}.
-!- FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a]:
Constitutes the precusor of the Nlrp1a inflammasome, which mediates
autoproteolytic processing within the FIIND domain to generate the N-
terminal and C-terminal parts, which are associated non-covalently in
absence of pathogens and other damage-associated signals.
{ECO:0000250|UniProtKB:Q9C000}.
-!- FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, N-
terminus]: Regulatory part that prevents formation of the Nlrp1a
inflammasome: in absence of pathogens and other damage-associated
signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and
PYD domains-containing protein 1a, C-terminus), preventing activation
of the Nlrp1a inflammasome (By similarity). In response to pathogen-
associated signals, this part is ubiquitinated and degraded by the
proteasome, releasing the cleaved C-terminal part of the protein, which
polymerizes and forms the Nlrp1a inflammasome (By similarity).
{ECO:0000250|UniProtKB:Q9C000}.
-!- FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, C-
terminus]: Constitutes the active part of the Nlrp1a inflammasome (By
similarity). In absence of pathogens and other damage-associated
signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and
PYD domains-containing protein 1a, N-terminus), preventing activation
of the Nlrp1a inflammasome (By similarity). In response to pathogen-
associated signals, the N-terminal part of Nlrp1a is degraded by the
proteasome, releasing this form, which polymerizes to form the Nlrp1a
inflammasome complex: the Nlrp1a inflammasome complex then directly
recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1)
activation, leading to gasdermin-D (GSDMD) cleavage and subsequent
pyroptosis (By similarity). {ECO:0000250|UniProtKB:Q9C000}.
-!- ACTIVITY REGULATION: Nlrp1a inflammasome is activated by pathogens and
other damage-associated signals: activation promotes ubiquitination and
degradation of the N-terminal part, releasing the cleaved C-terminal
part of the protein (NACHT, LRR and PYD domains-containing protein 1a,
C-terminus), which polymerizes and forms the Nlrp1a inflammasome (By
similarity). Nlrp1a inflammasome is inhibited by DPP8 and DPP9 via an
unknown mechanism (By similarity). Nlrp1a inflammasome is activated by
Val-boroPro (Talabostat, PT-100), an inhibitor of dipeptidyl peptidases
DPP8 and DPP9 (PubMed:31383852). Val-boroPro relieves inhibition of
DPP8 and/or DPP9 by inducing the proteasome-mediated destruction of the
N-terminal part of Nlrp1a, releasing its C-terminal part from
autoinhibition (By similarity). {ECO:0000250|UniProtKB:Q2LKW6,
ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:31383852}.
-!- SUBUNIT: Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop
between motifs BH4 and BH3) (By similarity). Interacts with NOD2; this
interaction is enhanced in the presence of muramyl dipeptide (MDP) and
increases IL1B release (By similarity). Interacts with EIF2AK2/PKR;
this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2
autophosphorylation and promotes inflammasome assembly in response to
danger-associated signals (By similarity). Interacts with MEFV; this
interaction targets Nlrp1a to degradation by autophagy, hence
preventing excessive IL1B- and IL18-mediated inflammation (By
similarity). Interacts with DPP8; leading to inhibit activation of the
inflammasome via an unknown mechanism (By similarity). Interacts with
DPP9; leading to inhibit activation of the inflammasome via an unknown
mechanism (By similarity). {ECO:0000250|UniProtKB:Q9C000}.
-!- SUBUNIT: [NACHT, LRR and PYD domains-containing protein 1a, N-
terminus]: Interacts with the C-terminal part of Nlrp1a (NACHT, LRR and
PYD domains-containing protein 1a, C-terminus) in absence of pathogens
and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.
-!- SUBUNIT: [NACHT, LRR and PYD domains-containing protein 1a, C-
terminus]: Interacts with the N-terminal part of Nlrp1a (NACHT, LRR and
PYD domains-containing protein 1a, N-terminus) in absence of pathogens
and other damage-associated signals (By similarity). Homomultimer;
forms the Nlrp1a inflammasome polymeric complex, a filament composed of
homopolymers of this form in response to pathogens and other damage-
associated signals (By similarity). Interacts (via CARD domain) with
CASP1 (via CARD domain); leading to CASP1 activation (By similarity).
{ECO:0000250|UniProtKB:Q9C000}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q9C000}. Cytoplasm
{ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.
Note=Nucleocytoplasmic distribution in lymphoid organs (probably in T-
cells) and in neurons. In epithelial cells, predominantly cytoplasmic.
{ECO:0000250|UniProtKB:Q9C000}.
-!- SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein
1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q2LKU9-1; Sequence=Displayed;
Name=2;
IsoId=Q2LKU9-2; Sequence=VSP_058002, VSP_058003, VSP_058004;
-!- TISSUE SPECIFICITY: Highly expressed in hematopoietic stem cells and
progenitor cells of both myeloid and lymphoid origin (PubMed:23219391).
The expression is highly strain-dependent. Not expressed in Balb/cJ
animals, but widely expressed in C57BL/6J. Expressed in macrophages
resistant to Bacillus anthracis lethal toxin, but not in toxin-
sensitive macrophages, except in CAST/EiJ strain (PubMed:23506131).
{ECO:0000269|PubMed:23219391, ECO:0000269|PubMed:23506131}.
-!- DOMAIN: The leucine-rich repeat (LRR) domain may be involved in
autoinhibition in the absence of activating signal, possibly through
intramolecular interaction with the NACHT domain.
{ECO:0000250|UniProtKB:Q2LKW6}.
-!- DOMAIN: The FIIND (domain with function to find) region is involved in
homomerization, but not in CASP1-binding. Autocatalytic cleavage in
this region occurs constitutively, prior to activation signals, and is
required for inflammasome activity (IL1B release), possibly by
facilitating CASP1 binding. Both N- and C-terminal fragments remain
associated. {ECO:0000250|UniProtKB:Q2LKW6}.
-!- DOMAIN: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]:
The C-terminal part of Nlrp1a oligomerizes to form the core of the
Nlrp1a inflammasome filament: in the filament, the CARD domains form a
central helical filaments that are promoted by oligomerized, but
flexibly linked, UPA regions surrounding the filaments. The UPA region
reduces the threshold needed for filament formation and signaling.
{ECO:0000250|UniProtKB:Q9C000}.
-!- PTM: [NACHT, LRR and PYD domains-containing protein 1a]:
Autocatalytically cleaved. Autocatalytic cleavage in FIIND region
occurs constitutively, prior to activation signals, and is required for
inflammasome activity (IL1B release), possibly by facilitating CASP1
binding. Both N- and C-terminal parts remain associated non-covalently.
{ECO:0000305|PubMed:31383852}.
-!- PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]:
Ubiquitinated in response to pathogen-associated signals, leading to
its degradation by the proteasome and subsequent release of the cleaved
C-terminal part of the protein (NACHT, LRR and PYD domains-containing
protein 1a, C-terminus), which polymerizes and forms the Nlrp1a
inflammasome. {ECO:0000250|UniProtKB:Q9C000}.
-!- MISCELLANEOUS: Three tandem Nrlp1 paralogs, Nrlp1a, Nrlp1b and Nrlp1c,
are present in at least 2 strains, C57BL/6J and 129S1/SvImJ. Nlrp1c is
predicted to be a pseudogene. Nlrp1b is the primary mediator of
macrophage susceptibility to Bacillus anthracis lethal toxin (LT).
Neither Nlrp1a, nor Nrlp1c are expressed in anthrax lethal toxin
susceptible strains, hence neither of them is thought to play an
important role in this phenotype. {ECO:0000269|PubMed:23506131,
ECO:0000305|PubMed:16429160}.
-!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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EMBL; DQ117601; AAZ40527.1; -; mRNA.
EMBL; KC539856; AGH68332.1; -; mRNA.
EMBL; KC539857; AGH68333.1; -; mRNA.
EMBL; KC539858; AGH68334.1; -; mRNA.
EMBL; KC539859; AGH68335.1; -; mRNA.
EMBL; KC539860; AGH68336.1; -; mRNA.
EMBL; KC539861; AGH68337.1; -; mRNA.
EMBL; AY355339; AAR14736.1; -; mRNA.
EMBL; AL596136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK157034; BAE33940.1; -; mRNA.
CCDS; CCDS48838.1; -. [Q2LKU9-1]
RefSeq; NP_001004142.2; NM_001004142.2. [Q2LKU9-1]
RefSeq; XP_017169843.1; XM_017314354.1. [Q2LKU9-1]
RefSeq; XP_017169844.1; XM_017314355.1. [Q2LKU9-1]
ComplexPortal; CPX-4271; NLRP1a inflammasome.
STRING; 10090.ENSMUSP00000104158; -.
MEROPS; S79.A02; -.
iPTMnet; Q2LKU9; -.
PhosphoSitePlus; Q2LKU9; -.
EPD; Q2LKU9; -.
MaxQB; Q2LKU9; -.
PaxDb; Q2LKU9; -.
PRIDE; Q2LKU9; -.
ProteomicsDB; 252904; -. [Q2LKU9-1]
ProteomicsDB; 252905; -. [Q2LKU9-2]
Ensembl; ENSMUST00000048514; ENSMUSP00000038186; ENSMUSG00000069830. [Q2LKU9-2]
Ensembl; ENSMUST00000108518; ENSMUSP00000104158; ENSMUSG00000069830. [Q2LKU9-1]
GeneID; 195046; -.
KEGG; mmu:195046; -.
UCSC; uc007jxq.2; mouse. [Q2LKU9-1]
UCSC; uc011xyf.1; mouse.
CTD; 195046; -.
MGI; MGI:2684861; Nlrp1a.
eggNOG; ENOG502S4A4; Eukaryota.
GeneTree; ENSGT00940000162176; -.
HOGENOM; CLU_002274_2_4_1; -.
OMA; YFTEESQ; -.
OrthoDB; 114368at2759; -.
TreeFam; TF340267; -.
Reactome; R-MMU-844455; The NLRP1 inflammasome.
BioGRID-ORCS; 195046; 0 hits in 52 CRISPR screens.
ChiTaRS; Nlrp1a; mouse.
PRO; PR:Q2LKU9; -.
Proteomes; UP000000589; Chromosome 11.
RNAct; Q2LKU9; protein.
Bgee; ENSMUSG00000069830; Expressed in granulocyte and 47 other tissues.
GO; GO:0061702; C:inflammasome complex; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISS:HGNC-UCL.
GO; GO:0019899; F:enzyme binding; ISS:HGNC-UCL.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:HGNC-UCL.
GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
GO; GO:0006954; P:inflammatory response; IEA:InterPro.
GO; GO:0045087; P:innate immune response; IEA:InterPro.
GO; GO:0051402; P:neuron apoptotic process; ISS:HGNC-UCL.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:BHF-UCL.
GO; GO:0097300; P:programmed necrotic cell death; IDA:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0032495; P:response to muramyl dipeptide; IDA:BHF-UCL.
CDD; cd08330; CARD_ASC_NALP1; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001315; CARD.
InterPro; IPR033516; CARD8/ASC/NALP1_CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR025307; FIIND_dom.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR041267; NLRP_HD2.
InterPro; IPR041075; NOD2_WH.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00619; CARD; 1.
Pfam; PF13553; FIIND; 1.
Pfam; PF13516; LRR_6; 1.
Pfam; PF05729; NACHT; 1.
Pfam; PF17776; NLRC4_HD2; 1.
Pfam; PF17779; NOD2_WH; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS51830; FIIND; 1.
PROSITE; PS51450; LRR; 3.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cytoplasm; Hydrolase; Immunity;
Inflammasome; Inflammatory response; Innate immunity; Leucine-rich repeat;
Necrosis; Nucleotide-binding; Nucleus; Protease; Reference proteome;
Repeat; Ubl conjugation.
CHAIN 1..1182
/note="NACHT, LRR and PYD domains-containing protein 1a"
/id="PRO_0000435102"
CHAIN 1..932
/note="NACHT, LRR and PYD domains-containing protein 1a, N-
terminus"
/evidence="ECO:0000250|UniProtKB:Q9C000"
/id="PRO_0000452853"
CHAIN 933..1182
/note="NACHT, LRR and PYD domains-containing protein 1a, C-
terminus"
/evidence="ECO:0000250|UniProtKB:Q9C000"
/id="PRO_0000452854"
DOMAIN 133..442
/note="NACHT"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
REPEAT 634..655
/note="LRR 1"
REPEAT 691..711
/note="LRR 2"
REPEAT 720..743
/note="LRR 3"
DOMAIN 799..1082
/note="FIIND"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01174"
DOMAIN 1092..1175
/note="CARD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
NP_BIND 139..146
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
REGION 1..23
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 780..806
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 799..932
/note="ZU5"
/evidence="ECO:0000250|UniProtKB:Q9C000"
REGION 933..1082
/note="UPA"
/evidence="ECO:0000250|UniProtKB:Q9C000"
SITE 932..933
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:Q9C000,
ECO:0000255|PROSITE-ProRule:PRU01174"
VAR_SEQ 668
/note="W -> CTLPEDMNKAEVKNTEAKGSLGEKAPGPRNDIFPFPPAHCPYNQTST
SEHLPCR (in isoform 2)"
/id="VSP_058002"
VAR_SEQ 785
/note="S -> SGMVGWLLKEDNVKKIKQNATNTYAHTHTHTHAELVPLKTFHPCSPV
SP (in isoform 2)"
/id="VSP_058003"
VAR_SEQ 1072..1085
/note="DLRPALPKIATAPK -> KISLRPETLRVEERDTKGAFLCSFPVSSLSL
(in isoform 2)"
/id="VSP_058004"
VARIANT 3
/note="E -> K (in strain: CAST/EiJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 88
/note="F -> Y (in strain: PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 112
/note="E -> G (in strain: CAST/EiJ, DBA/2J and PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 227
/note="Q -> R (in strain: PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 256
/note="G -> E (in strain: CAST/EiJ, DBA/2J and PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 291
/note="R -> Q (in strain: DBA/2J)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 337
/note="K -> N (in strain: PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 484
/note="S -> G (in strain: DBA/2J and CAST/EiJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 541
/note="V -> M (in strain: PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 660
/note="R -> H (in strain: AKR/J)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 664
/note="L -> I (in strain: PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 705
/note="G -> D (in strain: DBA/2J)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 857
/note="D -> N (in strain: PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 975
/note="N -> S (in strain: PWK/PhJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 1030
/note="R -> Q (in strain: DBA/2J)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 1043
/note="I -> F (in strain: CAST/EiJ)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 1110
/note="P -> S (in strain: DBA/2J)"
/evidence="ECO:0000269|PubMed:23506131"
VARIANT 1181
/note="K -> R (in strain: CAST/EiJ and DBA/2J)"
/evidence="ECO:0000269|PubMed:23506131"
MUTAGEN 593
/note="Q->P: Constitutively active in IL1B release. In
conventional housing conditions, mice bearing this mutation
develop a systemic inflammatory phenotype associated with
elevated IL1B and IL18 levels at 3-5 months of age. In a
germ-free environment, they exhibit neutrophilia and
myocarditis."
/evidence="ECO:0000269|PubMed:23219391"
CONFLICT 228
/note="N -> D (in Ref. 5; BAE33940)"
/evidence="ECO:0000305"
SEQUENCE 1182 AA; 134308 MW; D6D3F9FD5629D44A CRC64;
MEESQSKQES STKVAQHEGQ EDVDPTFKTK KLMEVELMKH RVQLERNLKL RTFPGARTKQ
VKEALYPLLT WSSKSKNLFQ NFTKLLLFKK LCQRGSENLV RESWYPCVPE EEAHMIDIQD
LFGPNLGTQK KPQLVIIEGA AGIGKSTLAR LVKRAWKEGK LYRNDFHHVF FFSCRELAQY
EQLSLAELIV QGQEVPTAPI RQILSHPEKL LFILDGIDEP AWVLADQNPE LCLHWSQTQP
VHTLLGSLLG KSILPGASFL LTTRTTALQK FIPSLEQPCQ VEVLGFTLFE RKNYFYKYFG
KKKGGVTTFT LVKSNSALLT LCEVPWVCWL VCTCLKKQME QGGELSLTSQ TTTALCLKYL
SLTIPGQHMR TQLRDLCSLA AEGVCQRRTL FSESDLCKQG LDEHAIASFL KIGVLQKQAS
SLSYSFAHLC LQEFFAAMSY ILDDSEERHA DMKNDRIVET LVERYGRQNL FEAPTVRFLF
GLLSKEELKK IEKLFSCSLH GKTKLKLLWH ILGKSQPHQP PCLGLLHCLY ENQDMELLTH
VMHDLQGTIV PGPDDLAHTV LQTNVKHLVI QTDMDLMVVT FCIKFCCHVR SLQLNRKVQQ
GHKFTAPGMV LYRWTPITDA SWKIFFSNLK LARNLEELDL SGNPLSYYAV HSLCTTLRKR
GCQLKTLWLV ECGLTSTYCS LLASVLSARS SLTELDLQLN DLGDGGVKML CEGLRNPACN
LSILWLDQAS LSDQVIAELR TLEAKNPKLL ISSTWKPHVM VPTMNMDKEE VGDSQALLKQ
QRQQSGDKHM EPLGTEDEFW GPTGPVTTEV VDRERNLYRV QLPMAGSYHC PSTGLHFVVT
RAVTIEIEFC AWSQYLDKTP LQQSHMVVGP LFDIKAEQGA VTAVYLPHFV ALQEGIVDSS
LFHVAHFQEH GMVLETPARV EQHYAVLENP SFSPMGILLR MIPAVGHFIP ITSTTLIYYH
LYLEDVTFHL YLVPNDCSIR KAIDDEEMKF QFVRINKPPP VDALYLGSRY IVSSSKLVEI
IPKELELCYR SPGESQLFSE IDIGHMDSEI KLQIKDKRHM NLKWEALLKP GDLRPALPKI
ATAPKDAPSL LHFMDQHREQ LVARVTSVDP LLDKLHGLVL SEDSYEVVRS ETTNQDKMRK
LFSLSRSWSW DCKDQFYQAL KETHPHLVMD ILEKLGGVSV KS


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WP813: G Protein Signaling Pathways
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WP2218: sGC
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Related Genes :
[Nlrp1a Card7 Nalp1 Nalp1a Nlrp1] NACHT, LRR and PYD domains-containing protein 1a (EC 3.4.-.-) (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
[Nlrp1a Nlrp1] NACHT, LRR and PYD domains-containing protein 1a allele 1 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
[NLRP1 CARD7 DEFCAP KIAA0926 NAC NALP1] NACHT, LRR and PYD domains-containing protein 1 (EC 3.4.-.-) (EC 3.6.4.-) (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1, C-terminus (NLRP1-CT); NACHT, LRR and PYD domains-containing protein 1, N-terminus (NLRP1-NT)]
[Nlrp1a Nlrp1] NACHT, LRR and PYD domains-containing protein 1 allele 2 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
[Nlrp1a Nlrp1] NACHT, LRR and PYD domains-containing protein 1a allele 4 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
[Nlrp1a Nlrp1] NACHT, LRR and PYD domains-containing protein 1a allele 3 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
[Nlrp1a Nlrp1] NACHT, LRR and PYD domains-containing protein 1a allele 5 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)]
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 1 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1b, C-terminus (Nlrp1b1-CT); NACHT, LRR and PYD domains-containing protein 1b, N-terminus (Nlrp1b1-NT)]
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 5 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1b, C-terminus (Nlrp1b1-CT); NACHT, LRR and PYD domains-containing protein 1b, N-terminus (Nlrp1b1-NT)]
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 2 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1b, C-terminus (Nlrp1b1-CT); NACHT, LRR and PYD domains-containing protein 1b, N-terminus (Nlrp1b1-NT)]
[nlrp1 si:ch211-66k16.28] NACHT, LRR and PYD domains-containing protein 1 homolog (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1, C-terminus (NLRP1-CT); NACHT, LRR and PYD domains-containing protein 1, N-terminus (NLRP1-NT)]
[NLRP3 C1orf7 CIAS1 NALP3 PYPAF1] NACHT, LRR and PYD domains-containing protein 3 (Angiotensin/vasopressin receptor AII/AVP-like) (Caterpiller protein 1.1) (CLR1.1) (Cold-induced autoinflammatory syndrome 1 protein) (Cryopyrin) (PYRIN-containing APAF1-like protein 1)
[Nlrp3 Cias1 Mmig1 Nalp3 Pypaf1] NACHT, LRR and PYD domains-containing protein 3 (Cold autoinflammatory syndrome 1 protein homolog) (Cryopyrin) (Mast cell maturation-associated-inducible protein 1) (PYRIN-containing APAF1-like protein 1)
[NLRP10 NALP10 NOD8 PYNOD] NACHT, LRR and PYD domains-containing protein 10 (Nucleotide-binding oligomerization domain protein 8)
[Nlrp10 Nalp10 Pynod] NACHT, LRR and PYD domains-containing protein 10
[Nlrp6 Nalp6 Navr Pypaf5] NACHT, LRR and PYD domains-containing protein 6 (Angiotensin II/vasopressin receptor) (Non-angiotensin-vasopressin receptor) (Non-AVR) (PYRIN-containing APAF1-like protein 5-like)
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 3
[Nlrp3 Nalp3 Pypaf1] NACHT, LRR and PYD domains-containing protein 3 (Cold autoinflammatory syndrome 1 protein homolog) (Cryopyrin) (Mast cell maturation-associated-inducible protein 1) (PYRIN-containing APAF1-like protein 1)
[CARD8 DACAR KIAA0955 NDPP1] Caspase recruitment domain-containing protein 8 (EC 3.4.-.-) (CARD-inhibitor of NF-kappa-B-activating ligand) (CARDINAL) (Tumor up-regulated CARD-containing antagonist of CASP9) (TUCAN) [Cleaved into: Caspase recruitment domain-containing protein 8, C-terminus (CARD8-CT); Caspase recruitment domain-containing protein 8, N-terminus (CARD8-NT)]
[NLRC4 CARD12 CLAN CLAN1 IPAF UNQ6189/PRO20215] NLR family CARD domain-containing protein 4 (CARD, LRR, and NACHT-containing protein) (CED-4-like protein Clan) (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[Nlrp1b Nalp1b] NACHT, LRR and PYD domains-containing protein 1b allele 4
[NLRP3] NACHT, LRR and PYD domains-containing protein 3
[Nlrp5 Mater Nalp5] NACHT, LRR and PYD domains-containing protein 5 (Maternal antigen that embryos require) (Mater protein) (Ooplasm-specific protein 1) (OP1)
[NLRP5 MATER NALP5] NACHT, LRR and PYD domains-containing protein 5 (Mater protein homolog) (Maternal Antigen that Embryos Require)
[PYCARD ASC CARD5 TMS1] Apoptosis-associated speck-like protein containing a CARD (hASC) (Caspase recruitment domain-containing protein 5) (PYD and CARD domain-containing protein) (Target of methylation-induced silencing 1)
[NLRP3] NACHT, LRR and PYD domains-containing protein 3
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

Bibliography :
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