F7 coagulation factor VII [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: F7provided by MGI
Official Full Name: coagulation factor VIIprovided by MGI
Primary source: MGI:MGI:109325
See related: Ensembl:ENSMUSG00000031443 AllianceGenome:MGI:109325
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: Cf7; FVII
Summary: This gene encodes a vitamin K-dependent serine protease that plays a critical role in the extrinsic pathway of blood coagulation. Upon contact with tissue factor III (TF III), the encoded protein forms an activated complex termed TF-FVIIa that initiates the coagulation cascade involving other coagulation factors, ultimately resulting in a fibrin clot. Complete lack of the encoded protein in mice results in in perinatal lethality due to bleeding from normal blood vessels. [provided by RefSeq, Apr 2015]
Expression: Biased expression in liver adult (RPKM 49.6), liver E18 (RPKM 7.5) and 3 other tissues See more
Orthologs: human all
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Genomic context

Location:: 8 A1.1; 8 5.73 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	8	NC_000074.7 (13075499..13085809)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	8	NC_000074.6 (13025506..13035809)

Chromosome 8 - NC_000074.7 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

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?

Trancriptomic analysis shows that expression of the antithrombins serpin C1 and D1 is significantly reduced in Schwann cell-deficient mice. In the absence of peripheral neuromuscular activity, neurodegeneration is completely blocked, and expression of prothrombin in muscle is markedly reduced.
Title: Glial cells maintain synapses by inhibiting an activity-dependent retrograde protease signal.
Leu8 is crucial for FVIIa-EPCR binding; this study characterizes its interaction in vivo in mice
Title: One amino acid in mouse activated factor VII defines its endothelial protein C receptor (EPCR) binding and modulates its EPCR-dependent hemostatic activity in vivo.
FVIIa-antithrombin but not FVIIa is a ligand for LRP1, and LRP1 contributes to the clearance of FVIIa-antithrombin in vivo
Title: LDL receptor-related protein 1 contributes to the clearance of the activated factor VII-antithrombin complex.
FVIIa binding to EPCR leads to a barrier protective effect in vivo
Title: Factor VIIa binding to endothelial cell protein C receptor protects vascular barrier integrity in vivo.
FVIIa binding to EPCR on the endothelium facilitates the transport of FVIIa from circulation to extravascular tissues where TF resides
Title: Endothelial cell protein C receptor-mediated redistribution and tissue-level accumulation of factor VIIa.
Murine FVIIa binds poorly to murine EPCR.
Title: Factor VIIa binding to endothelial cell protein C receptor: differences between mouse and human systems.
GlycoPEGylated rFVIIa (N7-GP) has a prolonged hemostatic effect in hemophilic mice compared with rFVIIa
Title: GlycoPEGylated rFVIIa (N7-GP) has a prolonged hemostatic effect in hemophilic mice compared with rFVIIa.
Conclude that the fVII-targeted verteporfin photodynamic therapy that we report here is a novel and effective therapeutic with improved selectivity for the treatment of breast cancer.
Title: Targeting tissue factor on tumour cells and angiogenic vascular endothelial cells by factor VII-targeted verteporfin photodynamic therapy for breast cancer in vitro and in vivo in mice.
The participation of Egr-1 in FVIIa-mediated regulation of keratinocyte function was confirmed by use of Egr-1-deficient mice, wherein a significant delay in skin wound healing after injury was observed, relative to WT mice.
Title: Factor VII deficiency impairs cutaneous wound healing in mice.
Recombinant FVIIa readily associates with the vascular endothelium and subsequently enters into extravascular spaces where it is likely to bind to tissue factor and is retained for extended time periods.
Title: Bio-distribution of pharmacologically administered recombinant factor VIIa (rFVIIa).

Submit: New GeneRIF Correction See all GeneRIFs (16)

Variation

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Alleles

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

Endonuclease-mediated (4)
Spontaneous (1)
Targeted (5) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

F7 (e-PCR), detects polymorphism
- UniSTS:525909

F7 (e-PCR), detects polymorphism
- UniSTS:143056

AI132620 (e-PCR)
- UniSTS:159737

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables calcium ion binding	IEA Inferred from Electronic Annotation more info
enables endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables peptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
contributes_to serine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables serine-type peptidase activity	IEA Inferred from Electronic Annotation more info
enables signaling receptor binding	IEA Inferred from Electronic Annotation more info
enables signaling receptor binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in animal organ regeneration	IEA Inferred from Electronic Annotation more info
involved_in blood coagulation	IBA Inferred from Biological aspect of Ancestor more info
involved_in blood coagulation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within blood coagulation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in blood coagulation	ISO Inferred from Sequence Orthology more info
involved_in circadian rhythm	IEA Inferred from Electronic Annotation more info
involved_in hemostasis	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of TOR signaling	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of TOR signaling	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of blood coagulation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of blood coagulation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of leukocyte chemotaxis	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of leukocyte chemotaxis	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of platelet-derived growth factor receptor signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of platelet-derived growth factor receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of positive chemotaxis	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of positive chemotaxis	ISO Inferred from Sequence Orthology more info
involved_in protein processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein processing	IEA Inferred from Electronic Annotation more info
involved_in protein processing	ISO Inferred from Sequence Orthology more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in regulation of body fluid levels	IEA Inferred from Electronic Annotation more info
involved_in response to 2,3,7,8-tetrachlorodibenzodioxine	IEA Inferred from Electronic Annotation more info
involved_in response to Thyroid stimulating hormone	IEA Inferred from Electronic Annotation more info
involved_in response to astaxanthin	IEA Inferred from Electronic Annotation more info
involved_in response to astaxanthin	ISO Inferred from Sequence Orthology more info
involved_in response to carbon dioxide	IEA Inferred from Electronic Annotation more info
involved_in response to cholesterol	IEA Inferred from Electronic Annotation more info
involved_in response to cholesterol	ISO Inferred from Sequence Orthology more info
involved_in response to estradiol	IEA Inferred from Electronic Annotation more info
involved_in response to estrogen	IEA Inferred from Electronic Annotation more info
involved_in response to genistein	IEA Inferred from Electronic Annotation more info
involved_in response to growth hormone	IEA Inferred from Electronic Annotation more info
involved_in response to hormone	IEA Inferred from Electronic Annotation more info
involved_in response to hypoxia	IEA Inferred from Electronic Annotation more info
involved_in response to nutrient levels	IEA Inferred from Electronic Annotation more info
involved_in response to nutrient levels	ISO Inferred from Sequence Orthology more info
involved_in response to stress	IEA Inferred from Electronic Annotation more info
involved_in response to thyroid hormone	IEA Inferred from Electronic Annotation more info
involved_in response to thyrotropin-releasing hormone	IEA Inferred from Electronic Annotation more info
involved_in response to thyroxine	IEA Inferred from Electronic Annotation more info
involved_in response to vitamin K	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in extracellular region	TAS Traceable Author Statement more info
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	IEA Inferred from Electronic Annotation more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
part_of serine-type peptidase complex	IEA Inferred from Electronic Annotation more info
part_of serine-type peptidase complex	ISO Inferred from Sequence Orthology more info
located_in vesicle	IEA Inferred from Electronic Annotation more info
located_in vesicle	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: coagulation factor VII

Names: serum prothrombin conversion accelerator

NP_034302.2

EC 3.4.21.21

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_010172.5 → NP_034302.2 coagulation factor VII preproprotein

See identical proteins and their annotated locations for NP_034302.2

Status: VALIDATED

Source sequence(s)

AC127308

Consensus CDS

CCDS22104.1

UniProtKB/Swiss-Prot

P70375, Q61109

UniProtKB/TrEMBL

Q542C2

Related

ENSMUSP00000033820.4, ENSMUST00000033820.4

Conserved Domains (5) summary

smart00020
Location:193 → 427

Tryp_SPc; Trypsin-like serine protease

smart00069
Location:24 → 85

GLA; Domain containing Gla (gamma-carboxyglutamate) residues

cd00054
Location:87 → 123

EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...

cd00190
Location:194 → 431

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 ...

pfam14670
Location:132 → 168

FXa_inhibition; Coagulation Factor Xa inhibitory site