O88947 · FA10_MOUSE
- ProteinCoagulation factor X
- GeneF10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids481 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Activity regulation
Inhibited by SERPINA5.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 273 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 319 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 416 | Charge relay system | ||||
Sequence: S |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | calcium ion binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | blood coagulation | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCoagulation factor X
- EC number
- Alternative names
- Cleaved into 3 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO88947
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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.
Chemistry
PTM/Processing
Features
Showing features for signal, propeptide, chain, modified residue, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MGSPVQLSLLCVVLASLLLP | ||||||
Propeptide | PRO_0000027792 | 21-40 | ||||
Sequence: GKGVFINRERANNVLARTRR | ||||||
Chain | PRO_0000027794 | 41-180 | Factor X light chain | |||
Sequence: ANSFFEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYKDGDQCESSPCQNQGACRDGIGGYTCTCSEGFEGKNCELFVRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSCISTAPFPCGKITTGRR | ||||||
Chain | PRO_0000027793 | 41-481 | Coagulation factor X | |||
Sequence: ANSFFEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYKDGDQCESSPCQNQGACRDGIGGYTCTCSEGFEGKNCELFVRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSCISTAPFPCGKITTGRRKRSVALNTSDSELDLEDALLDEDFLSPTENPIELLNLNETQPERSSDDLVRIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDWAESTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCKLSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDRSMKARVGPTAETPRTAGPPN | ||||||
Modified residue | 46 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 47 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 54 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 56 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Disulfide bond | 57↔62 | |||||
Sequence: CMEEIC | ||||||
Modified residue | 59 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 60 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 65 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 66 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 69 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 72 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 75 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Modified residue | 79 | 4-carboxyglutamate | ||||
Sequence: E | ||||||
Disulfide bond | 90↔101 | |||||
Sequence: CESSPCQNQGAC | ||||||
Disulfide bond | 95↔110 | |||||
Sequence: CQNQGACRDGIGGYTC | ||||||
Modified residue | 103 | (3R)-3-hydroxyaspartate | ||||
Sequence: D | ||||||
Disulfide bond | 112↔121 | |||||
Sequence: CSEGFEGKNC | ||||||
Disulfide bond | 129↔140 | |||||
Sequence: CRLDNGDCDQFC | ||||||
Disulfide bond | 136↔149 | |||||
Sequence: CDQFCREEQNSVVC | ||||||
Disulfide bond | 151↔164 | |||||
Sequence: CASGYFLGNDGKSC | ||||||
Disulfide bond | 172↔339 | Interchain (between light and heavy chains) | ||||
Sequence: CGKITTGRRKRSVALNTSDSELDLEDALLDEDFLSPTENPIELLNLNETQPERSSDDLVRIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDIAVLRLKTPITFRMNVAPAC | ||||||
Propeptide | PRO_0000027796 | 184-231 | Activation peptide | |||
Sequence: VALNTSDSELDLEDALLDEDFLSPTENPIELLNLNETQPERSSDDLVR | ||||||
Chain | PRO_0000027795 | 184-481 | Factor X heavy chain | |||
Sequence: VALNTSDSELDLEDALLDEDFLSPTENPIELLNLNETQPERSSDDLVRIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDWAESTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCKLSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDRSMKARVGPTAETPRTAGPPN | ||||||
Glycosylation | 187 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 218 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000027797 | 232-481 | Activated factor Xa heavy chain | |||
Sequence: IVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDWAESTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCKLSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDRSMKARVGPTAETPRTAGPPN | ||||||
Disulfide bond | 238↔243 | |||||
Sequence: CKDGEC | ||||||
Disulfide bond | 258↔274 | |||||
Sequence: CGGTILNEFYILTAAHC | ||||||
Disulfide bond | 387↔401 | |||||
Sequence: CKLSTSFSITQNMFC | ||||||
Disulfide bond | 412↔440 | |||||
Sequence: CQGDSGGPHVTRFKNTYYVTGIVSWGEGC |
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).
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-85 | Gla | ||||
Sequence: ANSFFEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYK | ||||||
Domain | 86-122 | EGF-like 1; calcium-binding | ||||
Sequence: DGDQCESSPCQNQGACRDGIGGYTCTCSEGFEGKNCE | ||||||
Domain | 125-165 | EGF-like 2 | ||||
Sequence: VRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSCI | ||||||
Domain | 232-464 | Peptidase S1 | ||||
Sequence: IVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDIAVLRLKTPITFRMNVAPACLPQKDWAESTLMTQKTGIVSGFGRTHEKGRQSNILKMLEVPYVDRNTCKLSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTRFKNTYYVTGIVSWGEGCARKGKYGIYTKVTTFLKWIDRSMK |
Sequence similarities
Belongs to the peptidase S1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length481
- Mass (Da)54,018
- Last updated1998-11-01 v1
- Checksum8AC09DE5EF9D271E
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 250 | in Ref. 4; AAH03877 | ||||
Sequence: I → V | ||||||
Sequence conflict | 294 | in Ref. 2; CAA10933 | ||||
Sequence: E → D | ||||||
Sequence conflict | 298 | in Ref. 2; CAA10933 | ||||
Sequence: M → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |