O88947 · FA10_MOUSE

  • Protein
    Coagulation factor X
  • Gene
    F10
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. Factor Xa activates pro-inflammatory signaling pathways in a protease-activated receptor (PAR)-dependent manner (By similarity).

Catalytic activity

  • Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
    EC:3.4.21.6 (UniProtKB | ENZYME | Rhea)

Activity regulation

Inhibited by SERPINA5.

Features

Showing features for active site.

148150100150200250300350400450
TypeIDPosition(s)Description
Active site273Charge relay system
Active site319Charge relay system
Active site416Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Molecular Functionserine-type endopeptidase activity
Biological Processblood coagulation
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      F10

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6 X CBA
    • 129/SvJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O88947
  • Secondary accessions
    • O54740
    • Q99L32

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 29 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for signal, propeptide, chain, modified residue, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-20
PropeptidePRO_000002779221-40
ChainPRO_000002779441-180Factor X light chain
ChainPRO_000002779341-481Coagulation factor X
Modified residue464-carboxyglutamate
Modified residue474-carboxyglutamate
Modified residue544-carboxyglutamate
Modified residue564-carboxyglutamate
Disulfide bond57↔62
Modified residue594-carboxyglutamate
Modified residue604-carboxyglutamate
Modified residue654-carboxyglutamate
Modified residue664-carboxyglutamate
Modified residue694-carboxyglutamate
Modified residue724-carboxyglutamate
Modified residue754-carboxyglutamate
Modified residue794-carboxyglutamate
Disulfide bond90↔101
Disulfide bond95↔110
Modified residue103(3R)-3-hydroxyaspartate
Disulfide bond112↔121
Disulfide bond129↔140
Disulfide bond136↔149
Disulfide bond151↔164
Disulfide bond172↔339Interchain (between light and heavy chains)
PropeptidePRO_0000027796184-231Activation peptide
ChainPRO_0000027795184-481Factor X heavy chain
Glycosylation187N-linked (GlcNAc...) asparagine
Glycosylation218N-linked (GlcNAc...) asparagine
ChainPRO_0000027797232-481Activated factor Xa heavy chain
Disulfide bond238↔243
Disulfide bond258↔274
Disulfide bond387↔401
Disulfide bond412↔440

Post-translational modification

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated.
Proteolytically cleaved and activated by cathepsin CTSG (By similarity).
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Plasma; synthesized in the liver.

Gene expression databases

Interaction

Subunit

The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain41-85Gla
Domain86-122EGF-like 1; calcium-binding
Domain125-165EGF-like 2
Domain232-464Peptidase S1

Sequence similarities

Belongs to the peptidase S1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    481
  • Mass (Da)
    54,018
  • Last updated
    1998-11-01 v1
  • Checksum
    8AC09DE5EF9D271E
MGSPVQLSLLCVVLASLLLPGKGVFINRERANNVLARTRRANSFFEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYKDGDQCESSPCQNQGACRDGIGGYTCTCSEGFEGKNCELFVRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSCISTAPFPCGKITTGRRKRSVALNTSDSELDLEDALLDEDFLSPTENPIELLNLNETQPERSSDDLVRIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDWAESTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCKLSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDRSMKARVGPTAETPRTAGPPN

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q3U3V1Q3U3V1_MOUSEF10493
D3Z7R3D3Z7R3_MOUSEF10119
D3Z215D3Z215_MOUSEF10321
D3Z521D3Z521_MOUSEF10319

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict250in Ref. 4; AAH03877
Sequence conflict294in Ref. 2; CAA10933
Sequence conflict298in Ref. 2; CAA10933

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF087644
EMBL· GenBank· DDBJ
AAC36345.1
EMBL· GenBank· DDBJ
mRNA
AJ222677
EMBL· GenBank· DDBJ
CAA10933.1
EMBL· GenBank· DDBJ
mRNA
AF211347
EMBL· GenBank· DDBJ
AAF22980.1
EMBL· GenBank· DDBJ
Genomic DNA
BC003877
EMBL· GenBank· DDBJ
AAH03877.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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