F12 coagulation factor XII (Hageman factor) [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: F12provided by MGI
Official Full Name: coagulation factor XII (Hageman factor)provided by MGI
Primary source: MGI:MGI:1891012
See related: Ensembl:ENSMUSG00000021492 AllianceGenome:MGI:1891012
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: HAF; FXII
Summary: This gene encodes a glycoprotein coagulation factor that plays an important role in the intrinsic pathway of blood coagulation and hemostasis. The encoded protein is an inactive zymogen that is autoactivated upon contact with negatively charged surfaces or misfolded protein aggregates. Mice lacking the encoded protein have a severe defect in forming stable fibrin clots. [provided by RefSeq, Apr 2015]
Expression: Biased expression in liver adult (RPKM 284.9), liver E18 (RPKM 133.3) and 2 other tissues See more
Orthologs: human all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 13 B1; 13 30.06 cM

Exon count:: 14

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	13	NC_000079.7 (55565771..55574617, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	13	NC_000079.6 (55417958..55426804, complement)

Chromosome 13 - NC_000079.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: Mouse ENCODE transcriptome data 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

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Factor XII signaling via uPAR-integrin beta1 axis promotes tubular senescence in diabetic kidney disease.
Title: Factor XII signaling via uPAR-integrin β1 axis promotes tubular senescence in diabetic kidney disease.
Factor XII contributes to thrombotic complications and vaso-occlusion in sickle cell disease.
Title: Factor XII contributes to thrombotic complications and vaso-occlusion in sickle cell disease.
FXII regulates the formation of deep vein thrombosis via the PI3K/AKT signaling pathway in mice.
Title: FXII regulates the formation of deep vein thrombosis via the PI3K/AKT signaling pathway in mice.
Factor XII protects neurons from apoptosis by epidermal and hepatocyte growth factor receptor-dependent mechanisms.
Title: Factor XII protects neurons from apoptosis by epidermal and hepatocyte growth factor receptor-dependent mechanisms.
Amelioration of Cognitive and Behavioral Deficits after Traumatic Brain Injury in Coagulation Factor XII Deficient Mice.
Title: Amelioration of Cognitive and Behavioral Deficits after Traumatic Brain Injury in Coagulation Factor XII Deficient Mice.
Coagulation factor XII contributes to hemostasis when activated by soil in wounds.
Title: Coagulation factor XII contributes to hemostasis when activated by soil in wounds.
Use of ""C9/11 Mismatch"" Control siRNA Reveals Sequence-Related Off-Target Effect on Coagulation of an siRNA Targeting Mouse Coagulation Factor XII.
Title: Use of "C9/11 Mismatch" Control siRNA Reveals Sequence-Related Off-Target Effect on Coagulation of an siRNA Targeting Mouse Coagulation Factor XII.
Bacterial-type long-chain polyP promotes platelet activation in a FXII-dependent manner in flowing blood, which may contribute to sepsis-associated thrombotic processes, consumptive coagulopathy, and thrombocytopenia.
Title: Factor XII Activation Promotes Platelet Consumption in the Presence of Bacterial-Type Long-Chain Polyphosphate In Vitro and In Vivo.
FXII and uPAR upregulate neutrophil functions to influence wound healing
Title: Factor XII and uPAR upregulate neutrophil functions to influence wound healing.
Deficiency or pharmacologic blockade of FXII renders mice less susceptible to experimental autoimmune encephalomyelitis (a model of multiple sclerosis) and is accompanied by reduced numbers of interleukin-17A-producing T cells.
Title: Blood coagulation factor XII drives adaptive immunity during neuroinflammation via CD87-mediated modulation of dendritic cells.

Submit: New GeneRIF Correction See all GeneRIFs (22)

Variation

Go to the top of the page Help

Alleles

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

Endonuclease-mediated (3)
Targeted (3) 1 citation

General gene information

Go to the top of the page Help

Markers

F12 (e-PCR), detects polymorphism
- UniSTS:525902

F12 (e-PCR), detects polymorphism
- UniSTS:502724

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables calcium ion binding	IEA Inferred from Electronic Annotation more info
enables peptidase activity	IMP Inferred from Mutant Phenotype 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

Process	Evidence Code	Pubs
involved_in Factor XII activation	IEA Inferred from Electronic Annotation more info
involved_in Factor XII activation	ISO Inferred from Sequence Orthology more info
involved_in blood coagulation	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within blood coagulation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in fibrinolysis	IEA Inferred from Electronic Annotation more info
involved_in plasma kallikrein-kinin cascade	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 fibrinolysis	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of fibrinolysis	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of plasminogen activation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of plasminogen activation	ISO Inferred from Sequence Orthology more info
involved_in protein autoprocessing	IEA Inferred from Electronic Annotation more info
involved_in protein autoprocessing	ISO Inferred from Sequence Orthology more info
involved_in protein processing	ISO Inferred from Sequence Orthology more info
involved_in response to misfolded protein	IEA Inferred from Electronic Annotation more info
involved_in response to misfolded protein	ISO Inferred from Sequence Orthology more info
involved_in zymogen activation	IBA Inferred from Biological aspect of Ancestor more info
involved_in zymogen activation	IEA Inferred from Electronic Annotation more info
involved_in zymogen activation	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	IMP Inferred from Mutant Phenotype more info	PubMed
located_in extracellular space	ISO Inferred from Sequence Orthology more info
is_active_in rough endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info

General protein information

Go to the top of the page Help

Preferred Names: coagulation factor XII

Names: factor XII; hageman factor

NP_067464.2

EC 3.4.21.38

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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_021489.3 → NP_067464.2 coagulation factor XII preproprotein

See identical proteins and their annotated locations for NP_067464.2

Status: REVIEWED

Source sequence(s)

CT009762

Consensus CDS

CCDS36675.1

UniProtKB/Swiss-Prot

O35727, Q6PER0, Q80YC5

Related

ENSMUSP00000021948.9, ENSMUST00000021948.15

Conserved Domains (7) summary

smart00020
Location:354 → 591

Tryp_SPc; Trypsin-like serine protease

cd00054
Location:96 → 131

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 ...

cd00061
Location:133 → 173

FN1; Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces ...

cd00062
Location:41 → 88

FN2; Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and ...

cd00190
Location:355 → 594

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 ...

pfam00008
Location:178 → 206

EGF; EGF-like domain

cl00100
Location:217 → 295

KR; Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and ...