Prss27 serine protease 27 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Prss27provided by MGI
Official Full Name: serine protease 27provided by MGI
Primary source: MGI:MGI:2450123
See related: Ensembl:ENSMUSG00000050762 AllianceGenome:MGI:2450123
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Mpn; CAPH2; marapsin
Summary: Predicted to enable serine-type endopeptidase activity. Predicted to be involved in proteolysis. Located in plasma membrane. Is expressed in eye; stomach; and uterus. Orthologous to human PRSS27 (serine protease 27). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in large intestine adult (RPKM 8.9), stomach adult (RPKM 8.5) and 10 other tissues See more
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Genomic context

Location:: 17 A3.3; 17 12.21 cM

Exon count:: 6

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	17	NC_000083.7 (24257217..24264923)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	17	NC_000083.6 (24038243..24045949)

Chromosome 17 - NC_000083.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors.
Title: Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors.
Marapsin's restricted expression, localization, and cytokine-inducible expression suggest a role in the terminal differentiation of keratinocytes in hyperproliferating squamous epithelia.
Title: The serine protease marapsin is expressed in stratified squamous epithelia and is up-regulated in the hyperproliferative epidermis of psoriasis and regenerating wounds.

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Variation

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Alleles

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

Endonuclease-mediated (2)
Gene trapped (1)
Targeted (3)

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:491851

Mpn (e-PCR), detects polymorphism
- UniSTS:265727

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: serine protease 27

Names: channel-activating protease 2-like protein; pancreasin; protease, serine 27

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_175440.4 → NP_780649.1 serine protease 27 precursor

See identical proteins and their annotated locations for NP_780649.1

Status: PROVISIONAL

Source sequence(s)

CT010502

Consensus CDS

CCDS28472.1

UniProtKB/Swiss-Prot

Q14A25, Q8BJR6

Related

ENSMUSP00000056483.6, ENSMUST00000059482.6

Conserved Domains (2) summary

smart00020
Location:37 → 275

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:39 → 278

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 ...