Ctsg cathepsin G [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ctsgprovided by MGI
Official Full Name: cathepsin Gprovided by MGI
Primary source: MGI:MGI:88563
See related: Ensembl:ENSMUSG00000040314 AllianceGenome:MGI:88563
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: VSP; CatG
Summary: This gene encodes a member of the peptidase S1 (chymotrypsin) family of serine endopeptidases. The encoded preproprotein is proteolytically processed to generate a mature protein product. This product appears to play a role in host defense, including inflammation and antigen processing. Homozygous knockout mice for this gene exhibit enhanced susceptibility to bacterial and fungal infection. [provided by RefSeq, Aug 2015]
Expression: Biased expression in liver E18 (RPKM 25.7), liver E14 (RPKM 22.2) and 1 other tissue See more
Orthologs: human all
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Genomic context

Location:: 14 C3; 14 28.19 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	14	NC_000080.7 (56337342..56340031, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	14	NC_000080.6 (56099885..56102574, complement)

Chromosome 14 - NC_000080.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Absence of the neutrophil serine protease cathepsin G decreases neutrophil granulocyte infiltration but does not change the severity of acute pancreatitis.
Title: Absence of the neutrophil serine protease cathepsin G decreases neutrophil granulocyte infiltration but does not change the severity of acute pancreatitis.
these findings present evidence of an arterial-specific recruitment pattern centered on CatG-instructed adhesion strengthening. The inhibition of this process could provide a novel strategy for treatment of arterial inflammation with limited side effects.
Title: Cathepsin G Controls Arterial But Not Venular Myeloid Cell Recruitment.
Cathepsin G activity may impair efferocytosis, which could lead to an accumulation of lesion-associated apoptotic cells and the accelerated progression of early atherosclerotic lesions to more complex lesions in Apoe(-/-) mice.
Title: Cathepsin G deficiency decreases complexity of atherosclerotic lesions in apolipoprotein E-deficient mice.
SerpinB1 is critical for maintaining polymorphonuclear neutrophils survival by antagonizing intracellular cathepsin G activity.
Title: SerpinB1 is critical for neutrophil survival through cell-autonomous inhibition of cathepsin G.
Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions.
Title: Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions.
NADPH oxidase in antimicrobial host defense against A. fumigatus and B. cepacia, whereas the proteases neutrophil elastase, cathepsin G, and lysosomal cysteine protease cathepsin C/ dipeptidyl peptidase I are dispensable
Title: Role of NADPH oxidase versus neutrophil proteases in antimicrobial host defense.
Cathepsin G and neutrophil elastase contribute to lung-protective immunity against mycobacterial infections in mice.
Title: Cathepsin G and neutrophil elastase contribute to lung-protective immunity against mycobacterial infections in mice.
This is the first study showing a contribution of neutrophil-derived neutral serine proteases CG and NE to lung-protective immunity against focal pneumonia-inducing serotype 19 S. pneumoniae in mice.
Title: Cathepsin G and neutrophil elastase play critical and nonredundant roles in lung-protective immunity against Streptococcus pneumoniae in mice.
In the absence of a pathogen challenge, neutrophil-derived proteases and nucleosomes contribute to large vessels thrombosis, the main trigger of myocardial infarction and stroke.
Title: Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases.
Inhibition of TGF-beta significantly reduces microvessel density in mammary tumor-induced bone lesions, mediated by decreased expression of both vascular endothelial growth factor (VEGF) and monocyte chemotactic protein (MCP)-1.
Title: Cathepsin G-mediated enhanced TGF-beta signaling promotes angiogenesis via upregulation of VEGF and MCP-1.

Submit: New GeneRIF Correction See all GeneRIFs (15)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (5) 1 citation
Endonuclease-mediated (2)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:489045

NoName (e-PCR)
- UniSTS:495465

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables caspase binding	ISO Inferred from Sequence Orthology more info
enables heparin binding	ISO Inferred from Sequence Orthology more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables peptidase activity	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables receptor ligand activity	ISO Inferred from Sequence Orthology more info
enables serine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables serine-type peptidase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in antibacterial humoral response	ISO Inferred from Sequence Orthology more info
involved_in biofilm matrix disassembly	ISO Inferred from Sequence Orthology more info
involved_in cellular response to lipopolysaccharide	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within chemotaxis	IEA Inferred from Electronic Annotation more info
involved_in defense response to Gram-negative bacterium	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within defense response to Gram-positive bacterium	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in defense response to Gram-positive bacterium	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within defense response to bacterium	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within defense response to fungus	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within defense response to fungus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in monocyte chemotaxis	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of T cell activation	ISO Inferred from Sequence Orthology more info
involved_in neutrophil activation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within neutrophil-mediated killing of gram-positive bacterium	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in platelet activation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of immune response	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within positive regulation of immune response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of platelet aggregation	ISO Inferred from Sequence Orthology more info
involved_in protein phosphorylation	ISO Inferred from Sequence Orthology more info
involved_in protein processing	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within proteolysis	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within response to lipopolysaccharide	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within response to lipopolysaccharide	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasmic stress granule	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
is_active_in intracellular membrane-bounded organelle	IBA Inferred from Biological aspect of Ancestor more info
located_in lysosome	ISO Inferred from Sequence Orthology more info
located_in membrane	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in secretory granule	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: cathepsin G

Names: vimentin-specific protease

NP_031826.1

EC 3.4.21.20

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_007800.2 → NP_031826.1 cathepsin G preproprotein

See identical proteins and their annotated locations for NP_031826.1

Status: REVIEWED

Source sequence(s)

AC091783, BU755975, CJ056088

Consensus CDS

CCDS27142.1

UniProtKB/Swiss-Prot

P28293

UniProtKB/TrEMBL

Q059V7

Related

ENSMUSP00000015583.2, ENSMUST00000015583.2

Conserved Domains (2) summary

smart00020
Location:20 → 238

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:21 → 241

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...