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Entry version 97 (02 Jun 2021)
Sequence version 1 (23 Nov 2004)
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Protein

Gasdermin-A3

Gene

Gsdma3

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

Precursor of a pore-forming protein involved in the transition from catagen to telogen at the end of hair follicle morphogenesis (PubMed:15475261, PubMed:26375003, PubMed:27281216).

This form constitutes the precursor of the pore: upon cleavage, the released N-terminal moiety (Gasdermin-A3, N-terminal) binds to membranes and forms pores, triggering cell death (PubMed:26375003, PubMed:27281216).

3 Publications

Pore-forming protein that causes membrane permeabilization and pyroptosis (PubMed:26375003, PubMed:27281216).

Released upon cleavage in vitro of genetically engineered Gsdma3, and binds to membrane inner leaflet lipids (PubMed:27281216).

Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (PubMed:27281216).

Binds to membrane inner leaflet lipids, including bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-bisphosphate, and more weakly to monophosphorylated phosphatidylinositols (PubMed:27281216).

Also binds to bacterial and mitochondrial lipids, including cardiolipin, and exhibits bactericidal activity (PubMed:27281216, PubMed:29695864).

The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown (Probable). Plays a role in the transition from catagen to telogen at the end of hair follicle morphogenesis, possibly by regulating hair follicle stem cell niche maintenance (PubMed:15475261, PubMed:15737203, PubMed:17572385, PubMed:22155111, PubMed:32302611).

Also required for mammary gland development (PubMed:28168650).

Curated9 Publications

<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

The full-length protein before cleavage is inactive: intramolecular interactions between N- and C-terminal domains mediate autoinhibition in the absence of activation signal (PubMed:25825937, PubMed:26100518, PubMed:26375003). The intrinsic pyroptosis-inducing activity is carried by the released N-terminal moiety (Gasdermin-A3, N-terminal) (PubMed:26100518, PubMed:26375003).3 Publications

<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 functionDevelopmental protein
Biological processNecrosis

<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:
Gasdermin-A3Curated
Alternative name(s):
Gasdermin-31 Publication
Cleaved into the following 2 chains:
Gasdermin-A3, N-terminalCurated
Short name:
GSDMA3-NTCurated
Gasdermin-A3, C-terminalCurated
Short name:
GSDMA3-CTCurated
<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:Gsdma31 PublicationImported
Synonyms:Gsdm31 PublicationImported
<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:3044668, Gsdma3

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei78 – 95Beta strandedCombined sources1 PublicationAdd BLAST18
Transmembranei99 – 120Beta strandedCombined sources1 PublicationAdd BLAST22
Transmembranei164 – 180Beta strandedCombined sources1 PublicationAdd BLAST17
Transmembranei184 – 198Beta strandedCombined sources1 PublicationAdd BLAST15

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Pyroptosis-induced inflammation mediated by Gsdma3 triggers robust anti-tumor immunity and may be used in therapies to suppress tumor growth (PubMed:32188939). Use of a nanoparticle-mediated delivery system that selectively directs release of N-terminal moiety (Gasdermin-A3, N-terminal) into tumor cells, triggers pyroptosis and robust anti-tumor immunity (PubMed:32188939). Pyroptosis of less than 15% of tumor cells is sufficient to clear the entire tumor in a mammary tumor graft (PubMed:32188939).1 Publication

<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

No visible phenotype (PubMed:25825937). A number of gain-of-function mutations, such as alopecia and excoriation (AE), bareskin (Bsk), defolliculated (Dfl), finnegan (Fgn) reduced coat 2 (Rco2), Rex-denuded (Re-den) and recombination induced mutation 3 (Rim3), have been identified: they cause progressive hair loss (alopecia) accompanied with hyperkeratosis and chronic skin inflammation (PubMed:15475261, PubMed:15737203, PubMed:17572385, PubMed:22155111). Gain-of-function mutations cause bulge stem cell depletion, leading to skin inflammation and alopecia (PubMed:22155111).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi9 – 18RALVRELNPR → AALVAELNPAA: Impaired pore-formation. 1 Publication10
Mutagenesisi14E → K: No spontaneous pyroptosis-inducing activity; when associated with D-184. 1 Publication1
Mutagenesisi132R → A: Weak or no effect on ability to induce pyroptosis. Impaired ability to induce pyroptosis; when associated with A-145. 1 Publication1
Mutagenesisi145R → A: Impaired ability to induce pyroptosis; when associated with A-132. 1 Publication1
Mutagenesisi184L → D: Markedly decreased induction of pyroptosis and defects in liposome-binding. No spontaneous pyroptosis-inducing activity; when associated with K-14. 1 Publication1
Mutagenesisi186L → E: Impaired pore-formation. 1 Publication1
Mutagenesisi262 – 464Missing in Dfl mutant; gain-of-function mutation; causes an alopecia phenotype. 1 PublicationAdd BLAST203
Mutagenesisi270L → D: Spontaneous pyroptosis-inducing activity. 1 Publication1
Mutagenesisi278T → P in Fgn mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis. 2 Publications1
Mutagenesisi343L → P in Rco2 mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis. 2 Publications1
Mutagenesisi344Y → C in Bsk mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis. 2 Publications1
Mutagenesisi344Y → D: Spontaneous pyroptosis-inducing activity. 1 Publication1
Mutagenesisi344Y → H in AE mutant; gain-of-function mutation; causes an alopecia phenotype; constitutively active in triggering cell death. Mice also display hypoplastic mammary glands, impairing lactation function. 3 Publications1
Mutagenesisi348A → D: Spontaneous pyroptosis-inducing activity. 1 Publication1
Mutagenesisi348A → T in Rim3 mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis. 2 Publications1
Mutagenesisi359I → T: Gain-of-function mutation; causes an alopecia phenotype. 1 Publication1
Mutagenesisi412A → AEA in Re-den mutant; gain-of-function mutation; causes an alopecia phenotype. Attenuates intramolecular interaction between the N- and C-terminal domains, hence may relieve autoinhibition; constitutively active in triggering pyroptosis. 2 Publications1

<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_00003472721 – 464Gasdermin-A3Add BLAST464
ChainiPRO_00004516701 – ?262Gasdermin-A3, N-terminal1 PublicationAdd BLAST262
ChainiPRO_0000451671?263 – 464Gasdermin-A3, C-terminal1 PublicationAdd BLAST202

<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

Cleavage relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-A3, N-terminal) that initiates pyroptosis.By similarity

Proteomic databases

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

More...
PaxDbi
Q5Y4Y6

PeptideAtlas

More...
PeptideAtlasi
Q5Y4Y6

PRoteomics IDEntifications database

More...
PRIDEi
Q5Y4Y6

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
271445

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q5Y4Y6

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

More...
PhosphoSitePlusi
Q5Y4Y6

<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

Highest levels in skin with weak expression in placenta and testis. Not detected in the gastrointestinal tract. In skin, expressed in postnatal hair follicles and epidermis as well as sebaceous gland basal cells.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

Not detected at postnatal day 1. Expressed on subsequent postnatal days up to day 20 and throughout adulthood.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000064224, Expressed in liver and 32 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q5Y4Y6, baseline and differential

<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

Homooligomer; homooligomeric ring-shaped pore complex containing 27-28 subunits when inserted in the membrane.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000073022

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q5Y4Y6, 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

Secondary structure

1464
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q5Y4Y6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Regioni1 – 261Triggers pyroptosis1 PublicationAdd BLAST261
Regioni9 – 13Lipid-binding1 Publication5

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili255 – 327Sequence analysisAdd BLAST73

<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

Intramolecular interactions between N- and C-terminal domains are important for autoinhibition in the absence of activation signal (PubMed:26375003). The intrinsic pyroptosis-inducing activity is carried by the N-terminal domain (PubMed:26375003).1 Publication

<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 gasdermin family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane beta strand

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502S0IQ, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183140

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5Y4Y6

Database of Orthologous Groups

More...
OrthoDBi
747086at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q5Y4Y6

TreeFam database of animal gene trees

More...
TreeFami
TF331886

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007677, Gasdermin
IPR040460, Gasdermin_pore
IPR041263, Gasdermin_PUB

The PANTHER Classification System

More...
PANTHERi
PTHR16399, PTHR16399, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04598, Gasdermin, 1 hit
PF17708, Gasdermin_C, 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 1 potential isoform that is computationally mapped.Show allAlign All

Q5Y4Y6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPVFEDVTRA LVRELNPRGD LTPLDSLIDF KHFRPFCLVL RKRKSTLFWG
60 70 80 90 100
ARYVRTDYTL LDLLEPGSSP SDLTDSGNFS FKNMLDVQVQ GLVEVPKTVK
110 120 130 140 150
VKGTAGLSQS STLEVQTLSV APSALENLKK ERKLSADHSF LNEMRYHEKN
160 170 180 190 200
LYVVMEAVEA KQEVTVEQTG NANAIFSLPS LALLGLQGSL NNNKAVTIPK
210 220 230 240 250
GCVLAYRVRL LRVFLFNLWD IPYICNDSMQ TFPKIRRVPC SAFISPTQMI
260 270 280 290 300
SEEPEEEKLI GEMHEDFKTL KEEVQRETQE VEKLSPVGRS SLLTSLSHLL
310 320 330 340 350
GKKKELQDLE QKLEGALDKG QKVTLEALPK DVLLSKDAMD AILYFLGALT
360 370 380 390 400
ELTEEQLKIL VKSLEKKILP VQLKLVESTL EQNFLQDKEG VFPLQPDLLS
410 420 430 440 450
SLGEEELTLT EALVGLSGLE VQRSGPQYAW DPDTRHNLCA LYAGLSLLHL
460
LSRKSNALTY CALS
Length:464
Mass (Da):52,020
Last modified:November 23, 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:i112C6F81F26AD1E0
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Z4YKL5Z4YKL5_MOUSE
Gasdermin-A3
Gsdma3
455Annotation 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>

<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 CAM24379 differs from that shown. Reason: Erroneous gene model prediction.Curated

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
AY679090 mRNA Translation: AAU95732.1
AL591125 Genomic DNA Translation: CAM24379.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS25356.1

NCBI Reference Sequences

More...
RefSeqi
NP_001007462.1, NM_001007461.1
XP_006533737.1, XM_006533674.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000073295; ENSMUSP00000073022; ENSMUSG00000064224

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
450219

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:450219

UCSC genome browser

More...
UCSCi
uc007lgs.1, mouse

<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
AY679090 mRNA Translation: AAU95732.1
AL591125 Genomic DNA Translation: CAM24379.1 Sequence problems.
CCDSiCCDS25356.1
RefSeqiNP_001007462.1, NM_001007461.1
XP_006533737.1, XM_006533674.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5B5RX-ray1.90A1-464[»]
6CB8electron microscopy3.80A1-262[»]
SMRiQ5Y4Y6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000073022

PTM databases

iPTMnetiQ5Y4Y6
PhosphoSitePlusiQ5Y4Y6

Proteomic databases

PaxDbiQ5Y4Y6
PeptideAtlasiQ5Y4Y6
PRIDEiQ5Y4Y6
ProteomicsDBi271445

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
450219

Genome annotation databases

EnsembliENSMUST00000073295; ENSMUSP00000073022; ENSMUSG00000064224
GeneIDi450219
KEGGimmu:450219
UCSCiuc007lgs.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
450219
MGIiMGI:3044668, Gsdma3

Phylogenomic databases

eggNOGiENOG502S0IQ, Eukaryota
GeneTreeiENSGT00950000183140
InParanoidiQ5Y4Y6
OrthoDBi747086at2759
PhylomeDBiQ5Y4Y6
TreeFamiTF331886

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
450219, 0 hits in 53 CRISPR screens

Protein Ontology

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PROi
PR:Q5Y4Y6
RNActiQ5Y4Y6, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000064224, Expressed in liver and 32 other tissues
ExpressionAtlasiQ5Y4Y6, baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR007677, Gasdermin
IPR040460, Gasdermin_pore
IPR041263, Gasdermin_PUB
PANTHERiPTHR16399, PTHR16399, 1 hit
PfamiView protein in Pfam
PF04598, Gasdermin, 1 hit
PF17708, Gasdermin_C, 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 nameiGSDA3_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: Q5Y4Y6
Secondary accession number(s): A2A4X5
<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: September 2, 2008
Last sequence update: November 23, 2004
Last modified: June 2, 2021
This is version 97 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

3D-structure, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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