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Entry version 49 (02 Jun 2021)
Sequence version 1 (05 Oct 2010)
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Protein

NACHT, LRR and PYD domains-containing protein 1 allele 2

Gene

Nlrp1a

Organism
Rattus norvegicus (Rat)
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 Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity).

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, such as B.anthracis lethal toxin (LT) or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex (PubMed:20502689, PubMed:31383852).

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 directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC 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).

By similarity2 Publications

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.

By similarity

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. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome.

By similarity

Constitutes the active part of the Nlrp1a inflammasome. 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. 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

<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

Activated by cleavage by B.anthracis lethal toxin (LT) endopeptidase (PubMed:20502689). Cleavage by LT 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 weakly 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). Weakly activated by Toxoplasma gondii (PubMed:31383852).By similarity2 Publications

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 bindingi181 – 188ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<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 allele 2Curated (EC:3.4.-.-By similarity)
Cleaved into the following 2 chains:
NACHT, LRR and PYD domains-containing protein 1a, C-terminusCurated
Short name:
Nlrp1a-CTBy similarity
NACHT, LRR and PYD domains-containing protein 1a, N-terminusCurated
Short name:
Nlrp1a-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:Nlrp1aBy similarity
Synonyms:Nlrp11 Publication
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus

<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, Nucleus

<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_00004528811 – 1218NACHT, LRR and PYD domains-containing protein 1 allele 2Add BLAST1218
ChainiPRO_00004528821 – 968NACHT, LRR and PYD domains-containing protein 1a, N-terminusBy similarityAdd BLAST968
ChainiPRO_0000452883969 – 1218NACHT, LRR and PYD domains-containing protein 1a, C-terminusBy similarityAdd BLAST250

<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 CASP1 binding. Both N- and C-terminal parts remain associated non-covalently.By similarity
(Microbial infection) Cleavage by B.anthracis lethal toxin (LT) endopeptidase 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.1 Publication
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.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>Sitei968 – 969Cleavage; by autolysisPROSITE-ProRule annotation2

Keywords - PTMi

Ubl conjugation

<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 (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3).

Interacts with NOD2; this interaction is enhanced in the presence of muramyl dipeptide (MDP) and increases IL1B release.

Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation and promotes inflammasome assembly in response to danger-associated signals.

Interacts with MEFV; this interaction targets Nlrp1a to degradation by autophagy, hence preventing excessive IL1B- and IL18-mediated inflammation.

Interacts with DPP8; leading to inhibit activation of the inflammasome via an unknown mechanism.

Interacts with DPP9; leading to inhibit activation of the inflammasome via an unknown mechanism.

By similarity

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.

By similarity

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). The Nlrp1a inflammasome polymeric complex directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC (By similarity).

Interacts (via CARD domain) with CASP1 (via CARD domain); leading to CASP1 activation (By similarity).

By similarity

<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>Domaini175 – 484NACHTPROSITE-ProRule annotationAdd BLAST310
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati343 – 364LRR 1Sequence analysisAdd BLAST22
Repeati673 – 693LRR 2Sequence analysisAdd BLAST21
Repeati730 – 750LRR 3Sequence analysisAdd BLAST21
Domaini835 – 1118FIINDPROSITE-ProRule annotationAdd BLAST284
Domaini1122 – 1211CARDPROSITE-ProRule annotationAdd BLAST90

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>Regioni835 – 968ZU5By similarityAdd BLAST134
Regioni969 – 1118UPABy similarityAdd BLAST150

<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 leucine-rich repeat (LRR) domain may be involved in autoinhibition in the absence of activating signal, possibly through intramolecular interaction with the NACHT domain.By similarity
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.By similarity
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.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

Leucine-rich repeat, Repeat

Family and domain databases

Conserved Domains Database

More...
CDDi
cd08330, CARD_ASC_NALP1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001315, CARD
IPR033516, CARD8/ASC/NALP1_CARD
IPR011029, DEATH-like_dom_sf
IPR025307, FIIND_dom
IPR001611, Leu-rich_rpt
IPR032675, LRR_dom_sf
IPR007111, NACHT_NTPase
IPR041267, NLRP_HD2
IPR041075, NOD2_WH
IPR027417, P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00619, CARD, 1 hit
PF13553, FIIND, 1 hit
PF13516, LRR_6, 2 hits
PF05729, NACHT, 1 hit
PF17776, NLRC4_HD2, 1 hit
PF17779, NOD2_WH, 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>Sequencei

<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.

D9I2G3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEESQSKQES NTRVAQHGSQ QDVDPTFQTK RALEKERSKP RPRPLPRVQL
60 70 80 90 100
QSLPGWSSTS KDVPLSQLIR EMDHESRRCI HRSKKKLDRS EHISQGTIPE
110 120 130 140 150
IYEKRKETIS HTQSMEQKYL FQNFTKLLLL QKCCPGGSEK LVRESWHPCV
160 170 180 190 200
PEEGGHMIEI QDLFDPNLDT EKKPQLVIIE GAAGIGKSTL ARQVKRAWDE
210 220 230 240 250
GQLYRDRFQH VFFFSCRELA QCKQLSLAEL IAQGQEVPTA PTRQILSRPE
260 270 280 290 300
KLLFILDGID EPAWVLEDQN PELCVHWSQA QPVHTLLGSL LGKSILPEAS
310 320 330 340 350
LMLTARTTAL QKLVPSLGQP HRVEVLGFSE FERKDYFYKY FAKERNTIID
360 370 380 390 400
FNLIGSIPVL LTLCEVPWVC WLLCTCLEKQ MQQGEVLSLT SQTTTALCLK
410 420 430 440 450
YLSLTIPGQH LSTQLRTLCS LAAEGICQRR TLFSKSDLCK QGLAEDAIAT
460 470 480 490 500
FLKIGVLQRQ PSSLSYSFAH LCLQEFFAAM SYILEDSEEA HGDMGNDRTV
510 520 530 540 550
ETLVERYGRQ NLFEAPTVRF LLGLLNTREM REMENIFACK FPWETKLKLL
560 570 580 590 600
QSIIGEPFCQ PCHLGLFHCL YENQEEELLT ETMLCFPLTA SGPNHMEATV
610 620 630 640 650
FQTNVKRLVI QTDMELMVVT FCITFSHVRS LRLKGKGQQE YKLTAPAMVL
660 670 680 690 700
YRWTPISEAS WKVLFSNLKC TRNLEELDLS GNPLSYSAVR SLCTALRQPG
710 720 730 740 750
CRLKTLWLVD CGLTSRCCSF LASMLSAHSR LAELDLRLND LGDNGVRQLC
760 770 780 790 800
EGLRNPACNL SILRLDQASL SEQVITELRA LETKNPKLFI SSTWMSHMTM
810 820 830 840 850
PTENTDGEES LTSSKQQQQQ SGDKHMEPLG TDDDFWGPSG PVSTEVVDRE
860 870 880 890 900
RNLYRVRLPM AGSYHCPSTG LHFVVTRAVT IEIGFCAWSQ FLHETPLQHS
910 920 930 940 950
HMVAGPLFDI KAEHGAVTAV CLPHFVSLQE GKVDSSLFHV AHFQDHGMVL
960 970 980 990 1000
ETPARVEPHF AVLENPSFSP MGVLLRMIPA VGHFIPITSI TLIYYRLYLE
1010 1020 1030 1040 1050
DITFHLYLVP NDCTIRKAID EEELKFQFVR INKPPPVDAL YVGSRYIVSS
1060 1070 1080 1090 1100
SKEVEILPKE LELCYRSPRE SQLFSEIYVG NIGSGINLQL TDKKYMNLIW
1110 1120 1130 1140 1150
EALLKPGDLR PALPRMASAP KDAPALLHFV DQHREQLVAR VTSVDPLLDK
1160 1170 1180 1190 1200
LHGLVLSEED YETVRAEATN QDKMRKLFRG SRSWSWDCKD HFYQALKETH
1210
PHLIMDLLEK SGGVSVRL
Length:1,218
Mass (Da):138,406
Last modified:October 5, 2010 - 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:i25E107F8B61D71DB
GO

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Nlrp1a gene is extremely polymorphic. 5 alleles have been described: 1 (AC D9I2F9), 2 (this entry), 3 (AC D9I2H0), 4 (AC D9I2G1) and 5 (AC D9I2G4).1 Publication

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
HM060632 mRNA Translation: ADI96229.1

<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
HM060632 mRNA Translation: ADI96229.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Family and domain databases

CDDicd08330, CARD_ASC_NALP1, 1 hit
Gene3Di3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR001315, CARD
IPR033516, CARD8/ASC/NALP1_CARD
IPR011029, DEATH-like_dom_sf
IPR025307, FIIND_dom
IPR001611, Leu-rich_rpt
IPR032675, LRR_dom_sf
IPR007111, NACHT_NTPase
IPR041267, NLRP_HD2
IPR041075, NOD2_WH
IPR027417, P-loop_NTPase
PfamiView protein in Pfam
PF00619, CARD, 1 hit
PF13553, FIIND, 1 hit
PF13516, LRR_6, 2 hits
PF05729, NACHT, 1 hit
PF17776, NLRC4_HD2, 1 hit
PF17779, NOD2_WH, 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
Search...

<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 nameiNL1A2_RAT
<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: D9I2G3
<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: June 2, 2021
Last sequence update: October 5, 2010
Last modified: June 2, 2021
This is version 49 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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