Prtn3 proteinase 3 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Prtn3provided by MGI
Official Full Name: proteinase 3provided by MGI
Primary source: MGI:MGI:893580
See related: Ensembl:ENSMUSG00000057729 AllianceGenome:MGI:893580
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: PR3; PR-3; mPR3
Summary: Predicted to enable enzyme binding activity; serine-type endopeptidase activity; and signaling receptor binding activity. Predicted to be involved in several processes, including mature conventional dendritic cell differentiation; neutrophil extravasation; and positive regulation of GTPase activity. Predicted to be located in azurophil granule lumen; cytosol; and plasma membrane raft. Predicted to be active in extracellular space. Predicted to colocalize with plasma membrane. Is expressed in early conceptus and liver. Orthologous to human PRTN3 (proteinase 3). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in liver E18 (RPKM 90.8), liver E14.5 (RPKM 70.6) and 3 other tissues See more
Orthologs: human all
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Genomic context

Location:: 10 C1; 10 39.72 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	10	NC_000076.7 (79715499..79719008)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	10	NC_000076.6 (79879667..79883174)

Chromosome 10 - NC_000076.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

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?

Proteinase 3 depletion attenuates leukemia by promoting myeloid differentiation.
Title: Proteinase 3 depletion attenuates leukemia by promoting myeloid differentiation.
N-glycan in the variable region of monoclonal ACPA (CCP-Ab1) promotes the exacerbation of experimental arthritis.
Title: N-glycan in the variable region of monoclonal ACPA (CCP-Ab1) promotes the exacerbation of experimental arthritis.
Lack of Proteinase 3 Stabilizes Advanced Atherosclerotic Lesions.
Title: Lack of Proteinase 3 Stabilizes Advanced Atherosclerotic Lesions.
Mice Deficient in the IL-1beta Activation Genes Prtn3, Elane, and Casp1 Are Protected Against the Development of Obesity-Induced NAFLD.
Title: Mice Deficient in the IL-1β Activation Genes Prtn3, Elane, and Casp1 Are Protected Against the Development of Obesity-Induced NAFLD.
Results provide evidence that proteinase 3 as a new factor involved in non-alcoholic fatty liver disease and insulin resistance.
Title: Activation of proteinase 3 contributes to Non-alcoholic Fatty Liver Disease (NAFLD) and insulin resistance.
In different murine models of apoptotic cell injection, the PR3-induced microenvironment instructed pDC-driven Th9/Th2 cell generation.
Title: Proteinase 3 on apoptotic cells disrupts immune silencing in autoimmune vasculitis.
PR3-ANCA is a promising biomarker in primary sclerosing cholangitis.
Title: PR3-ANCA: a promising biomarker in primary sclerosing cholangitis (PSC).
Proteinase 3-mediated caspase-3 activation controls neutrophil spontaneous death
Title: Proteinase 3-dependent caspase-3 cleavage modulates neutrophil death and inflammation.
Increased PRTN3 activity was associated with development of autoimmune diabetes mellitus in NOD mice.
Title: Increased neutrophil elastase and proteinase 3 and augmented NETosis are closely associated with β-cell autoimmunity in patients with type 1 diabetes.
Phagocytosis of apoptotic PR3-expressing cells potentiates proinflammatory cytokines in vivo by resident murine peritoneal macrophages.
Title: Proteinase 3, the autoantigen in granulomatosis with polyangiitis, associates with calreticulin on apoptotic neutrophils, impairs macrophage phagocytosis, and promotes inflammation.

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)

Endonuclease-mediated (4)
Targeted (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Prtn3 (e-PCR), detects polymorphism
- UniSTS:472918

U97073 (e-PCR)
- UniSTS:180072

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables signaling receptor binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in cell-cell junction maintenance	ISO Inferred from Sequence Orthology more info
involved_in collagen catabolic process	IEA Inferred from Electronic Annotation more info
involved_in mature conventional dendritic cell differentiation	ISO Inferred from Sequence Orthology more info
involved_in membrane protein ectodomain proteolysis	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of phagocytosis	ISO Inferred from Sequence Orthology more info
involved_in neutrophil extravasation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of GTPase activity	ISO Inferred from Sequence Orthology more info
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in proteolysis	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in azurophil granule lumen	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
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in intracellular membrane-bounded organelle	ISO Inferred from Sequence Orthology more info
located_in lysosome	IEA Inferred from Electronic Annotation more info
located_in membrane raft	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
colocalizes_with plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane raft	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: myeloblastin

NP_035308.2

EC 3.4.21.76

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_011178.3 → NP_035308.2 myeloblastin precursor

See identical proteins and their annotated locations for NP_035308.2

Status: VALIDATED

Source sequence(s)

AC151846

Consensus CDS

CCDS23993.1

UniProtKB/Swiss-Prot

O08809, Q61096

UniProtKB/TrEMBL

A0A0R4IZY6

Related

ENSMUSP00000006679.8, ENSMUST00000006679.15

Conserved Domains (2) summary

smart00020
Location:29 → 245

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:30 → 248

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 ...