St14 suppression of tumorigenicity 14 (colon carcinoma) [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: St14provided by MGI
Official Full Name: suppression of tumorigenicity 14 (colon carcinoma)provided by MGI
Primary source: MGI:MGI:1338881
See related: Ensembl:ENSMUSG00000031995 AllianceGenome:MGI:1338881
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: mCAP3; MT-SP1; Prss14; Epithin; Tmprss14; matriptase
Summary: Enables serine-type endopeptidase activity. Involved in proteolysis. Acts upstream of or within epithelial cell morphogenesis involved in placental branching and neural tube closure. Located in external side of plasma membrane and extracellular space. Is expressed in several structures, including alimentary system; brain; early conceptus; genitourinary system; and sensory organ. Used to study Sjogren's syndrome. Human ortholog(s) of this gene implicated in autosomal recessive congenital ichthyosis 11. Orthologous to human ST14 (ST14 transmembrane serine protease matriptase). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in colon adult (RPKM 92.3), small intestine adult (RPKM 64.9) and 12 other tissues See more
Orthologs: human all
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Genomic context

Location:: 9 A4; 9 16.61 cM

Exon count:: 21

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	9	NC_000075.7 (30999886..31043138, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	9	NC_000075.6 (31088590..31131811, complement)

Chromosome 9 - NC_000075.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Kidney-Specific Membrane-Bound Serine Proteases CAP1/Prss8 and CAP3/St14 Affect ENaC Subunit Abundances but Not Its Activity.
Title: Kidney-Specific Membrane-Bound Serine Proteases CAP1/Prss8 and CAP3/St14 Affect ENaC Subunit Abundances but Not Its Activity.
Early-onset tufting enteropathy in HAI-2-deficient mice is independent of matriptase-mediated cleavage of EpCAM.
Title: Early-onset tufting enteropathy in HAI-2-deficient mice is independent of matriptase-mediated cleavage of EpCAM.
Proteolytic cleavage of Podocin by Matriptase exacerbates podocyte injury.
Title: Proteolytic cleavage of Podocin by Matriptase exacerbates podocyte injury.
matriptase is a causative agent in the development of congenital tufting enteropathy (CTE) and may provide a new target for the treatment of CTE in individuals carrying SPINT2 mutation
Title: Matriptase drives early-onset intestinal failure in a mouse model of congenital tufting enteropathy.
The catalytic, stem, and transmembrane portions of matriptase-2 are required for suppressing the expression of the iron-regulatory hormone hepcidin.
Title: The catalytic, stem, and transmembrane portions of matriptase-2 are required for suppressing the expression of the iron-regulatory hormone hepcidin.
These results identify EpCAM as a substrate of matriptase and link HAI-2, matriptase, EpCAM, and claudin-7 in a functionally important pathway that causes disease when it is dysregulated.
Title: Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis.
The proliferation impairment in matriptase-deficient breast cancer cells is caused by their inability to initiate activation of the c-Met signalling pathway in response to fibroblast-secreted pro-HGF.
Title: Targeting matriptase in breast cancer abrogates tumour progression via impairment of stromal-epithelial growth factor signalling.
Matriptase is a critical promoter of late stages of squamous cell carcinoma progression and induces pro-tumorigenic chemokine and cytokine release, and inflammatory cell accumulation in established tumors.
Title: Matriptase promotes inflammatory cell accumulation and progression of established epidermal tumors.
Data show that proteinase-activated receptor (PAR)-2-dependent inflammatory signaling as an essential component of matriptase-mediated and potentiation of ras-mediated oncogenesis.
Title: Non-hematopoietic PAR-2 is essential for matriptase-driven pre-malignant progression and potentiation of ras-mediated squamous cell carcinogenesis.
HAI-1 regulates the activity of activated matriptase, whereas HAI-2 has an essential role in regulating prostasin-dependent matriptase zymogen activation.
Title: The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.

Submit: New GeneRIF Correction See all GeneRIFs (37)

Variation

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Alleles

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

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

General gene information

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Markers

St14 (e-PCR), detects polymorphism
- UniSTS:471848

St14 (e-PCR), detects polymorphism
- UniSTS:471849

G38154 (e-PCR)
- UniSTS:53341

St14 (e-PCR), detects polymorphism
- UniSTS:531095

St14 (e-PCR), detects polymorphism
- UniSTS:525514

St14 (e-PCR), detects polymorphism
- UniSTS:495857

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables serine-type endopeptidase activity	EXP Inferred from Experiment more info	PubMed
enables serine-type peptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables serine-type peptidase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within cell migration	TAS Traceable Author Statement more info	PubMed
acts_upstream_of_or_within epithelial cell morphogenesis involved in placental branching	IGI Inferred from Genetic Interaction more info	PubMed
involved_in keratinocyte differentiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in keratinocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in keratinocyte differentiation	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within neural tube closure	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein catabolic process	IEA Inferred from Electronic Annotation more info
involved_in protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in proteolysis	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in basolateral plasma membrane	IEA Inferred from Electronic Annotation more info
located_in basolateral plasma membrane	ISO Inferred from Sequence Orthology more info
located_in external side of plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	TAS Traceable Author Statement more info	PubMed

General protein information

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Preferred Names: suppressor of tumorigenicity 14 protein homolog

Names: matriptase/MT-SP1; protease, serine, 14 (epithin)

NP_035306.2

EC 3.4.21.109

XP_006510161.1

EC 3.4.21.109

XP_006510162.1

EC 3.4.21.109

XP_036010597.1

EC 3.4.21.109

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_011176.4 → NP_035306.2 suppressor of tumorigenicity 14 protein homolog

See identical proteins and their annotated locations for NP_035306.2

Status: VALIDATED

Source sequence(s)

AC114542, CT025653

Consensus CDS

CCDS22948.1

UniProtKB/Swiss-Prot

P56677

UniProtKB/TrEMBL

Q543E3

Related

ENSMUSP00000034478.3, ENSMUST00000034478.3

Conserved Domains (5) summary

smart00020
Location:614 → 849

Tryp_SPc; Trypsin-like serine protease

cd00041
Location:340 → 444

CUB; CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

cd00112
Location:525 → 559

LDLa; Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about ...

cd00190
Location:615 → 852

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 ...

pfam01390
Location:88 → 179

SEA; SEA domain

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000075.7 Reference GRCm39 C57BL/6J

Range

30999886..31043138 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006510098.5 → XP_006510161.1 suppressor of tumorigenicity 14 protein homolog isoform X2

Conserved Domains (4) summary

cd00041
Location:318 → 422

CUB; CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

cd00112
Location:503 → 537

LDLa; Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about ...

cd00190
Location:593 → 830

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 ...

pfam01390
Location:66 → 156

SEA; SEA domain
XM_006510099.5 → XP_006510162.1 suppressor of tumorigenicity 14 protein homolog isoform X3

Conserved Domains (3) summary

cd00041
Location:168 → 272

CUB; CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

cd00112
Location:353 → 387

LDLa; Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about ...

cd00190
Location:443 → 680

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 ...
XM_036154704.1 → XP_036010597.1 suppressor of tumorigenicity 14 protein homolog isoform X1

Conserved Domains (4) summary

cd00041
Location:360 → 464

CUB; CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

cd00112
Location:545 → 579

LDLa; Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about ...

cd00190
Location:635 → 872

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 ...

pfam01390
Location:108 → 198

SEA; SEA domain