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Entry version 15 (02 Jun 2021)
Sequence version 1 (05 Dec 2018)
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Protein

NACHT, LRR and PYD domains-containing protein 1 homolog

Gene

nlrp1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Acts as the sensor component of the nlrp1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed:30150286).

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 (PubMed:30150286).

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 nlrp1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome recruits and activate proinflammatory caspases (caspa and/or caspb), leading to pyroptosis (By similarity).

By similarity1 Publication

Constitutes the precusor of the nlrp1 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.

By similarity

Regulatory part that prevents formation of the nlrp1 inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, C-terminus), preventing activation of the nlrp1 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 nlrp1 inflammasome (By similarity).

By similarity

Constitutes the active part of the nlrp1 inflammasome (By similarity).

In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, N-terminus), preventing activation of the nlrp1 inflammasome (By similarity).

In response to pathogen-associated signals, the N-terminal part of nlrp1 is degraded by the proteasome, releasing this form, which polymerizes to form the nlrp1 inflammasome complex: the nlrp1 inflammasome complex then directly recruits and activates proinflammatory caspases (caspa and/or caspb) activation, leading to subsequent pyroptosis (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

nlrp1 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 1, C-terminus), which polymerizes and forms the nlrp1 inflammasome.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi263 – 270ATPPROSITE-ProRule annotation8

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease
Biological processImmunity, Inflammatory response, Innate immunity, Necrosis
LigandATP-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
NACHT, LRR and PYD domains-containing protein 1 homologCurated (EC:3.4.-.-By similarity)
Cleaved into the following 2 chains:
NACHT, LRR and PYD domains-containing protein 1, C-terminusCurated
Short name:
NLRP1-CTBy similarity
NACHT, LRR and PYD domains-containing protein 1, N-terminusCurated
Short name:
NLRP1-NTBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:nlrp11 Publication
ORF Names:si:ch211-66k16.28
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7955 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesDanionidaeDanioninaeDanio
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000437 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Zebrafish Information Network genome database

More...
ZFINi
ZDB-GENE-120709-59, nlrp1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Inflammasome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Morpholino knockdown in embryos 6 hours post-fertilization (hpf) results in reduced caspa and caspb activation following bacterial infection with E.tarda.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004487891 – 1355NACHT, LRR and PYD domains-containing protein 1 homologAdd BLAST1355
ChainiPRO_00004528611 – 1109NACHT, LRR and PYD domains-containing protein 1, N-terminusBy similarityAdd BLAST1109
ChainiPRO_00004528621110 – 1182NACHT, LRR and PYD domains-containing protein 1, C-terminusBy similarityAdd BLAST73

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating proinflammatory caspases (caspa and/or caspb) binding. Both N- and C-terminal parts remain associated non-covalently.By similarity
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 1, C-terminus), which polymerizes and forms the nlrp1 inflammasome.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1109 – 1110Cleavage; by autolysisPROSITE-ProRule annotationBy similarity2

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
A0A386CAB9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in adult spleen, head kidney, gill and skin and also in the embryo.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In the embryo, highest expression at 2 hours post-fertilization (hpf) with levels decreasing in later stages.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in response to infection with the bacteriim E.tarda.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSDARG00000088423, Expressed in pharyngeal gill and 19 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with the C-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, C-terminus) in absence of pathogens and other damage-associated signals.

By similarity

Interacts with the N-terminal part of nlrp1 (NACHT, LRR and PYD domains-containing protein 1, N-terminus) in absence of pathogens and other damage-associated signals (By similarity). Homomultimer; forms the nlrp1 inflammasome polymeric complex, a filament composed of homopolymers of this form in response to pathogens and other damage-associated signals (By similarity). The nlrp1 inflammasome polymeric complex associates with pycard/asc (PubMed:30150286).

Interacts (via CARD domain) with pycard/asc (via CARD domain); leading to proinflammatory caspases (caspa and/or caspb) recruitment (PubMed:30150286). Pro-caspase-a and pro-caspase-b filament formation increases local enzyme concentration, resulting in trans-autocleavage and activation. Active caspa and caspb then processes il1b and il18 precursors, leading to the release of mature cytokines in the extracellular milieu and inflammatory response (By similarity).

By similarity1 Publication

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-4947, NLRP1 inflammasome, variant 1
CPX-4948, NLRP1 inflammasome, variant 2

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini257 – 458NACHTPROSITE-ProRule annotationAdd BLAST202
Domaini977 – 1252FIINDPROSITE-ProRule annotationAdd BLAST276
Domaini1278 – 1354CARDPROSITE-ProRule annotationAdd BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni977 – 1109ZU5By similarityAdd BLAST133
Regioni1110 – 1252UPABy similarityAdd BLAST143

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The CARD domain is involved in the interaction with pycard.1 Publication
The C-terminal part of nlrp1 oligomerizes to form the core of the nlrp1 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.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NLRP family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QS9E, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_002274_2_4_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
K7DYI4

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.10.10, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00619, CARD, 1 hit
PF13553, FIIND, 1 hit
PF05729, NACHT, 1 hit
PF17776, NLRC4_HD2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47986, SSF47986, 1 hit
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50209, CARD, 1 hit
PS51830, FIIND, 1 hit
PS50837, NACHT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

A0A386CAB9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSDYTDRNN LASAIKTLGD MLEKDEAFQR LMYNASTKGE INRGRVNKVF
60 70 80 90 100
LKALLSAGDK VGEFLNELID HLNLFKVLGD FSWNPPVLKE AELNERTSQL
110 120 130 140 150
RTQQHKYVER VSGFSHYGFG ETGTPARGDI TSPRGPQVAS IEEDLATSKL
160 170 180 190 200
AELLLAVGDH LEKIEKKGQF LPENVERFSL DCFITSESVK LSSEAVELAP
210 220 230 240 250
CYTEPVIIQR SKEQTEKYCQ EYVRSPHTSS HLLSNDKTQS IRIGQLFSPD
260 270 280 290 300
SDGNTPKTVI LCGDSGRGKS FVLEKIILDW VHLEHHFENF DAVFLLKYEE
310 320 330 340 350
LKCLSEEMSL TELLSRSCSL TSDQISQILQ LTPEKVLFLI DGIDDFSFNA
360 370 380 390 400
HIQISSPTDP SQKAPVISII HCLMRDLLLV ESSVIVTTRY TAAAELSSLC
410 420 430 440 450
KRPQRFTEIE GFSERRVQEY FQKFFQDEQL FKKAYESMKT NETLLTFCSV
460 470 480 490 500
PLLCWMVCFC LKKDADQVMT ELKTTTSIYV HFVSTLLEDH HQSQSFLRSL
510 520 530 540 550
GQLAEEGMKN RQNLFDEKSV TRTGLDPATR VFMNKIYLKR KKKHELLFKF
560 570 580 590 600
KHLSFQEFFA ALYYIMLDEE ESWCKVSELF NMMESEALIH RSPPIFRGRL
610 620 630 640 650
SNPIPSVMMF LCGLFNKKVS SSLFEKMKST FSHNVKLKKK ELKKKLMKMI
660 670 680 690 700
PAMIRQYGFE LFALHCLYEL QDERFVTKVL ETHKFIDLSN VSLRSTDCLV
710 720 730 740 750
LCYCLRLCPN IRELNFMNCD LTAAKLKILQ PALGLCETLR FSVEHLSEIG
760 770 780 790 800
DLIQILSESK ILRELKVRED EYGVESPRWS FNLSVTRGDV LLTLSSSEKN
810 820 830 840 850
PSFSSVLNIR LTCAQSQISR TDWTLFLQRL RKTGTLTEDS SADDDHVSLQ
860 870 880 890 900
LSSLHSVGLK SLDLTLVSLN ESWASGIISL IQNCTSLQQL KVSVTGLLLE
910 920 930 940 950
EGLKLLKKSL TDPHCTVIIE GRRNCSEPSE EHLRQSYEKV EIHFKPKLLE
960 970 980 990 1000
ELAELSICNP GSSALNIHCQ SCVDVADSDQ WVQVEPSVCR GEGGTEFRIT
1010 1020 1030 1040 1050
TPAGRFQCSR TRMRWVCDGD VTLHYRAVDG HFLNAELERL QCERVAPVLD
1060 1070 1080 1090 1100
VNVISGKLEE AHLPHYMCLA ESDPALTNAV KLLSVEDEGI SLESVELTRF
1110 1120 1130 1140 1150
HAKILQPMFS PKTVLVKLGI PVKVHCDLLI FMTHTCPIIL NVYFFPSDSL
1160 1170 1180 1190 1200
VEENIKTEEK SSHQIKCSRP EAPLQMKKQH SLEVPDAVVQ PEAIKLRGNM
1210 1220 1230 1240 1250
KPNFFQVKQP VVNDITMILS RVDDQKSVWT GTIWKKLIDI KLNKTESDLF
1260 1270 1280 1290 1300
QSGQKHKTSQ PAHSFDKAQF FDTHWCNLIK SVENVDTVAD KLLQKQIIHE
1310 1320 1330 1340 1350
QFYSEIIHHK STSEESMRKI CVIVRKGSAA VKEIFISILL QENPNLLNHL

PSSDS
Length:1,355
Mass (Da):154,257
Last modified:December 5, 2018 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9C98D90D3F622A93
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A5S7K9I4A0A5S7K9I4_DANRE
Si:ch211-66k16.28
nlrp1
1,192Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2R8PYP6A0A2R8PYP6_DANRE
Si:ch211-66k16.28
nlrp1
76Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
MH118554 mRNA Translation: AYC80945.1
BX005331 Genomic DNA No translation available.
CR450720 Genomic DNA No translation available.

NCBI Reference Sequences

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RefSeqi
XP_009297081.1, XM_009298806.2

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
MH118554 mRNA Translation: AYC80945.1
BX005331 Genomic DNA No translation available.
CR450720 Genomic DNA No translation available.
RefSeqiXP_009297081.1, XM_009298806.2

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
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Protein-protein interaction databases

ComplexPortaliCPX-4947, NLRP1 inflammasome, variant 1
CPX-4948, NLRP1 inflammasome, variant 2

Proteomic databases

PaxDbiA0A386CAB9

Organism-specific databases

ZFINiZDB-GENE-120709-59, nlrp1

Phylogenomic databases

eggNOGiENOG502QS9E, Eukaryota
HOGENOMiCLU_002274_2_4_1
InParanoidiK7DYI4

Miscellaneous databases

Protein Ontology

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PROi
PR:A0A386CAB9

Gene expression databases

BgeeiENSDARG00000088423, Expressed in pharyngeal gill and 19 other tissues

Family and domain databases

Gene3Di3.80.10.10, 1 hit
PfamiView protein in Pfam
PF00619, CARD, 1 hit
PF13553, FIIND, 1 hit
PF05729, NACHT, 1 hit
PF17776, NLRC4_HD2, 1 hit
SUPFAMiSSF47986, SSF47986, 1 hit
SSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50209, CARD, 1 hit
PS51830, FIIND, 1 hit
PS50837, NACHT, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNLRP1_DANRE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0A386CAB9
Secondary accession number(s): K7DYI4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 11, 2019
Last sequence update: December 5, 2018
Last modified: June 2, 2021
This is version 15 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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