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Entry version 144 (10 Feb 2021)
Sequence version 1 (05 Jul 2004)
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Protein

NAD(+) hydrolase SARM1

Gene

Sarm1

Organism
Mus musculus (Mouse)
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

NAD+ hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD+ metabolism (PubMed:25818290, PubMed:26686637, PubMed:27735788, PubMed:32312889). Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site (PubMed:21555464, PubMed:22678360, PubMed:25818290, PubMed:26686637, PubMed:26423149). Wallerian degeneration is triggered by NAD+ depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD+ into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD+ cleavage promoting cytoskeletal degradation and axon destruction (PubMed:28334607). Also able to hydrolyze NADP+, but not other NAD+-related molecules (By similarity). Can activate neuronal cell death in response to stress (PubMed:19587044). Regulates dendritic arborization through the MAPK4-JNK pathway (PubMed:17724133, PubMed:21555464). Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38 (PubMed:21555464).By similarity10 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Autoinhibited: in the inactive state, the enzymatic TIR domain is held apart by the autoinhibiting ARM repeats. NAD+-binding to ARM repeats maintains an inactive state by promoting interaction between ARM repeats and the TIR domain, thereby facilitating inhibition of the enzymatic TIR domain. Following activation, possibly by nicotinamide mononucleotide (NMN), auto-inhibitory interactions are released, allowing self-association of the TIR domains and subsequent activation of the NAD+ hydrolase (NADase) activity. Self-association of TIR domains is facilitated by the octamer of SAM domains.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei103NAD 1; inhibitorBy similarity1
Binding sitei110NAD 1; inhibitorBy similarity1
Binding sitei599NAD 2; substrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei642PROSITE-ProRule annotation1

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 bindingi149 – 157NAD 1; inhibitorBy similarity9
Nucleotide bindingi190 – 193NAD 1; inhibitorBy similarity4
Nucleotide bindingi569 – 570NAD 2; substrateBy similarity2

<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 - Molecular functioni

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
Biological processDifferentiation, Immunity, Innate immunity, Neurogenesis
LigandNAD

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-166166, MyD88-independent TLR4 cascade
R-MMU-936964, Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-MMU-937041, IKK complex recruitment mediated by RIP1
R-MMU-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex

<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:
NAD(+) hydrolase SARM1Curated (EC:3.2.2.61 Publication)
Short name:
NADase SARM1Curated
Alternative name(s):
NADP(+) hydrolase SARM1Curated (EC:3.2.2.-By similarity)
Sterile alpha and TIR motif-containing protein 11 Publication
<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:Sarm11 PublicationImported
Synonyms:Kiaa05241 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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:2136419, Sarm1

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Mitochondrion, Synapse

<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

Absence of Sarm1 provides a level of protection against axon degeneration (PubMed:22678360, PubMed:26912636, PubMed:28978465). Genetic deletion blocks Wallerian degeneration of sciatic nerve and cultured superior cervical ganglia and peripheral polyneuropathy induced by vincristine (PubMed:22678360, PubMed:27797810). Severed Sarm1 null axons are able to persist up to 72 hours after axotomy, whereas wild-type axons degenerate within 8 hours (PubMed:22678360). Similarly, axons appear to be protected from degeneration in a sciatic nerve lesion model, lasting up to 14 days compared with 3 days for wild type (PubMed:22678360). Mice display improved traumatic brain injury-associated phenotypes after injury: mice develop fewer beta-amyloid precursor protein aggregates in axons of the corpus callosum after traumatic brain injury and show improved axonal integrity (PubMed:26912636). Mice show some protection against early but not late axonal degeneration in experimental allergic encephalomyelitis mouse model (PubMed:32584865). Mice exhibit normal glucose metabolism and pain sensitivity but show attenuated diabetic peripheral neuropathy (PubMed:31439642). Mice lacking both Sarm1 and Nmnat2 are viable and survive: Sarm1 deficiency corrects axon outgrowth in mice lacking Nmnat2, independently of NMNAT metabolites, preventing perinatal lethality (PubMed:25818290). Mice lacking both Rho and Sarm1 show a level of protection against retinal degeneration induced by the absence of Rho: the absence of Sarm1 promoting rod and cone photoreceptor cell survival (PubMed:32312889).8 Publications

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 27MitochondrionBy similarityAdd BLAST27
<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_000009759028 – 724NAD(+) hydrolase SARM1Add BLAST697

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei548PhosphoserineCombined sources1
Modified residuei558PhosphoserineCombined sources1

<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

Phosphorylation at Ser-548 by JNK kinases (MAPK8, MAPK9 and /or MAPK10) enhance the NAD+ hydrolase (NADase) activity. Phosphorylation at Ser-548 and subsequent activation takes place in response to oxidative stress conditions and inhibits mitochondrial respiration.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PeptideAtlas

More...
PeptideAtlasi
Q6PDS3

PRoteomics IDEntifications database

More...
PRIDEi
Q6PDS3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6PDS3

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q6PDS3

<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

Widely expressed in the brain and neurons (at protein level) (PubMed:21555464). Expressed in photoreceptor cells of the neural retina (PubMed:32312889).2 Publications

<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

Down-regulated in sciatic nerve of mice with diabetic peripheral neuropathy (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000050132, Expressed in blastocyst and 115 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q6PDS3, MM

<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

Homooctamer; forms an octomeric ring via SAM domains (By similarity).

Interacts with TICAM1/TRIF and thereby interferes with TICAM1/TRIF function (By similarity).

Interacts with SDC2 (via cytoplasmic domain) and MAPK10/JNK3 (PubMed:17724133, PubMed:21555464).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
231917, 3 interactors

Protein interaction database and analysis system

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IntActi
Q6PDS3, 11 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000103922

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q6PDS3, protein

<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

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q6PDS3

Database of comparative protein structure models

More...
ModBasei
Search...

<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 '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>Repeati60 – 100ARM 1Sequence analysisAdd BLAST41
Repeati114 – 153ARM 2Sequence analysisAdd BLAST40
Repeati155 – 193ARM 3Sequence analysisAdd BLAST39
Repeati196 – 235ARM 4Sequence analysisAdd BLAST40
Repeati237 – 280ARM 5Sequence analysisAdd BLAST44
Repeati281 – 314ARM 6Sequence analysisAdd BLAST34
Repeati315 – 354ARM 7Sequence analysisAdd BLAST40
Repeati359 – 402ARM 8Sequence analysisAdd BLAST44
<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>Domaini412 – 476SAM 1PROSITE-ProRule annotationAdd BLAST65
Domaini486 – 548SAM 2PROSITE-ProRule annotationAdd BLAST63
Domaini560 – 703TIRPROSITE-ProRule annotationAdd BLAST144

<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 TIR domain mediates NAD+ hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.By similarity
The ARM repeats inhibit the NAD+ hydrolase (NADase) activity by binding to NAD+: NAD+-binding to ARM repeats facilitates inhibition of the TIR domain NADase through their domain interface. In contrast to classical ARM repeats, the last helix of ARM 6 does not fold back to interact with the first two helices, but instead turns towards the N-terminus of SARM1. As a result, the two following motifs ARM 7 and ARM 8 reverse their directions and lie perpendicularly. Moreover, ARM repeats interact with different domains not only within each protomer but also of the adjacent ones.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 SARM1 family.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3678, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000004155

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_003286_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q6PDS3

Identification of Orthologs from Complete Genome Data

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OMAi
CEVQTWL

Database of Orthologous Groups

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OrthoDBi
206466at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q6PDS3

TreeFam database of animal gene trees

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TreeFami
TF315263

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.150.50, 2 hits
1.25.10.10, 1 hit
3.40.50.10140, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011989, ARM-like
IPR016024, ARM-type_fold
IPR001660, SAM
IPR013761, SAM/pointed_sf
IPR039184, SARM1
IPR000157, TIR_dom
IPR035897, Toll_tir_struct_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR22998, PTHR22998, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF07647, SAM_2, 2 hits
PF13676, TIR_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00454, SAM, 2 hits
SM00255, TIR, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47769, SSF47769, 2 hits
SSF48371, SSF48371, 1 hit
SSF52200, SSF52200, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50105, SAM_DOMAIN, 2 hits
PS50104, TIR, 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>Sequences (4)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 describes 4 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q6PDS3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVLTLLFSAY KLCRFFTMSG PRPGADRLTV PGPDRSGGAS PWWAAGGRGS
60 70 80 90 100
REVSPGVGTE VQGALERSLP ELQQALSELK QASAARAVGA GLAEVFQLVE
110 120 130 140 150
EAWLLPAVGR EVAQGLCDAI RLDGGLDLLL RLLQAPELET RVQAARLLEQ
160 170 180 190 200
ILVAENRDRV ARIGLGVILN LAKEREPVEL ARSVAGILEH MFKHSEETCQ
210 220 230 240 250
RLVAAGGLDA VLYWCRRTDP ALLRHCALAL ANCALHGGQT VQRCMVEKRA
260 270 280 290 300
AEWLFPLAFS KEDELLRLHA CLAVAVLATN KEVEREVEHS GTLALVEPLV
310 320 330 340 350
ASLDPGRFAR CLVDASDTSQ GRGPDDLQSL VLLLDSSRLE AQCIGAFYLC
360 370 380 390 400
AEAAIKSLQG KTKVFSDIGA IQSLKRLVSY STNGTTSALA KRALRLLGEE
410 420 430 440 450
VPRRILPCVA SWKEAEVQTW LQQIGFSQYC ENFREQQVDG DLLLRLTDEE
460 470 480 490 500
LQTDLGMKSS ITRKRFFREL TELKTFASYA TCDRSNLADW LGSLDPRFRQ
510 520 530 540 550
YTYGLVSCGL DRSLLHRVSE QQLLEDCGIR LGVHRTRILS AAREMLHSPL
560 570 580 590 600
PCTGGKLSGD TPDVFISYRR NSGSQLASLL KVHLQLHGFS VFIDVEKLEA
610 620 630 640 650
GKFEDKLIQS VIAARNFVLV LSAGALDKCM QDHDCKDWVH KEIVTALSCG
660 670 680 690 700
KNIVPIIDGF EWPEPQALPE DMQAVLTFNG IKWSHEYQEA TIEKIIRFLQ
710 720
GRPSQDSSAG SDTSLEGATP MGLP
Length:724
Mass (Da):79,606
Last modified:July 5, 2004 - 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:i9A5BF03ED22E6102
GO
Isoform 2 (identifier: Q6PDS3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     435-439: Missing.

Show »
Length:719
Mass (Da):79,007
Checksum:i08843BA13C0DD69F
GO
Isoform 3 (identifier: Q6PDS3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     543-543: R → RGHFAQTGLRSLRRPSLHDDGPRDKQWGRATLTSMSLSLAP

Show »
Length:764
Mass (Da):84,006
Checksum:iD76542F538604CF8
GO
Isoform 4 (identifier: Q6PDS3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-536: Missing.
     537-543: RILSAAR → MSLSLAP

Show »
Length:188
Mass (Da):20,594
Checksum:i35C1A626B521791D
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAD32242 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAI25546 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti61V → A in AAR17521 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0136061 – 536Missing in isoform 4. CuratedAdd BLAST536
Alternative sequenceiVSP_013604435 – 439Missing in isoform 2. 1 Publication5
Alternative sequenceiVSP_013607537 – 543RILSAAR → MSLSLAP in isoform 4. Curated7
Alternative sequenceiVSP_013605543R → RGHFAQTGLRSLRRPSLHDD GPRDKQWGRATLTSMSLSLA P in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY444167 mRNA Translation: AAR17521.1
AK172964 Transcribed RNA Translation: BAD32242.1 Different initiation.
AK044113 mRNA Translation: BAC31784.1
AL591177 Genomic DNA Translation: CAI25544.1
AL591177 Genomic DNA Translation: CAI25545.1
AL591177 Genomic DNA Translation: CAI25546.1 Sequence problems.
BC058534 mRNA Translation: AAH58534.1
BC080850 mRNA Translation: AAH80850.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS25105.1 [Q6PDS3-1]
CCDS48857.1 [Q6PDS3-3]

NCBI Reference Sequences

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RefSeqi
NP_001161993.1, NM_001168521.1 [Q6PDS3-3]
NP_766383.2, NM_172795.3 [Q6PDS3-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000061174; ENSMUSP00000051059; ENSMUSG00000050132 [Q6PDS3-1]
ENSMUST00000108287; ENSMUSP00000103922; ENSMUSG00000050132 [Q6PDS3-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
237868

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:237868

UCSC genome browser

More...
UCSCi
uc007kjh.2, mouse [Q6PDS3-4]
uc007kji.2, mouse [Q6PDS3-1]
uc007kjj.2, mouse [Q6PDS3-3]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AY444167 mRNA Translation: AAR17521.1
AK172964 Transcribed RNA Translation: BAD32242.1 Different initiation.
AK044113 mRNA Translation: BAC31784.1
AL591177 Genomic DNA Translation: CAI25544.1
AL591177 Genomic DNA Translation: CAI25545.1
AL591177 Genomic DNA Translation: CAI25546.1 Sequence problems.
BC058534 mRNA Translation: AAH58534.1
BC080850 mRNA Translation: AAH80850.1
CCDSiCCDS25105.1 [Q6PDS3-1]
CCDS48857.1 [Q6PDS3-3]
RefSeqiNP_001161993.1, NM_001168521.1 [Q6PDS3-3]
NP_766383.2, NM_172795.3 [Q6PDS3-1]

3D structure databases

SMRiQ6PDS3
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi231917, 3 interactors
IntActiQ6PDS3, 11 interactors
STRINGi10090.ENSMUSP00000103922

PTM databases

iPTMnetiQ6PDS3
PhosphoSitePlusiQ6PDS3

Proteomic databases

PeptideAtlasiQ6PDS3
PRIDEiQ6PDS3

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
14061, 197 antibodies

Genome annotation databases

EnsembliENSMUST00000061174; ENSMUSP00000051059; ENSMUSG00000050132 [Q6PDS3-1]
ENSMUST00000108287; ENSMUSP00000103922; ENSMUSG00000050132 [Q6PDS3-3]
GeneIDi237868
KEGGimmu:237868
UCSCiuc007kjh.2, mouse [Q6PDS3-4]
uc007kji.2, mouse [Q6PDS3-1]
uc007kjj.2, mouse [Q6PDS3-3]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23098
MGIiMGI:2136419, Sarm1

Rodent Unidentified Gene-Encoded large proteins database

More...
Rougei
Search...

Phylogenomic databases

eggNOGiKOG3678, Eukaryota
GeneTreeiENSGT00390000004155
HOGENOMiCLU_003286_2_0_1
InParanoidiQ6PDS3
OMAiCEVQTWL
OrthoDBi206466at2759
PhylomeDBiQ6PDS3
TreeFamiTF315263

Enzyme and pathway databases

ReactomeiR-MMU-166166, MyD88-independent TLR4 cascade
R-MMU-936964, Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-MMU-937041, IKK complex recruitment mediated by RIP1
R-MMU-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
237868, 0 hits in 17 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Sarm1, mouse

Protein Ontology

More...
PROi
PR:Q6PDS3
RNActiQ6PDS3, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000050132, Expressed in blastocyst and 115 other tissues
GenevisibleiQ6PDS3, MM

Family and domain databases

Gene3Di1.10.150.50, 2 hits
1.25.10.10, 1 hit
3.40.50.10140, 1 hit
InterProiView protein in InterPro
IPR011989, ARM-like
IPR016024, ARM-type_fold
IPR001660, SAM
IPR013761, SAM/pointed_sf
IPR039184, SARM1
IPR000157, TIR_dom
IPR035897, Toll_tir_struct_dom_sf
PANTHERiPTHR22998, PTHR22998, 1 hit
PfamiView protein in Pfam
PF07647, SAM_2, 2 hits
PF13676, TIR_2, 1 hit
SMARTiView protein in SMART
SM00454, SAM, 2 hits
SM00255, TIR, 1 hit
SUPFAMiSSF47769, SSF47769, 2 hits
SSF48371, SSF48371, 1 hit
SSF52200, SSF52200, 1 hit
PROSITEiView protein in PROSITE
PS50105, SAM_DOMAIN, 2 hits
PS50104, TIR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiSARM1_MOUSE
<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: Q6PDS3
Secondary accession number(s): Q5SYG5
, Q5SYG6, Q6A054, Q6SZW0, Q8BRI9
<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: May 10, 2005
Last sequence update: July 5, 2004
Last modified: February 10, 2021
This is version 144 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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