F10
entrez
2159
canonical
uniprot
P00742
canonical
ensembl
ENSG00000126218
resolver
ensp
ENSP00000364701
resolver
ensp
ENSP00000364709
resolver
ensp
ENSP00000528640
resolver
enst
ENST00000375551
resolver
enst
ENST00000375559
resolver
genesymbol
F10
resolver
hgnc
HGNC:3528
resolver
uniprot
Q14340
resolver
uniprot
Q5JVE7
resolver
uniprot
Q5JVE8
resolver
uniprot_entry
FA10_HUMAN
resolver
uniprot_entry
Q5JVE7_HUMAN
resolver
uniprot_entry
Q5JVE8_HUMAN
resolver
uniprot_sec
Q14340
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by SERPINA5 and SERPINA10. {ECO:0000269|PubMed:20427285, ECO:0000269|PubMed:6323392}.
uniprot
proteins
amino_acid_sequence
MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK
uniprot
proteins
disease_involvement
DISEASE: Factor X deficiency (FA10D) [MIM:227600]: A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis. {ECO:0000269|PubMed:10468877, ECO:0000269|PubMed:10739379, ECO:0000269|PubMed:10746568, ECO:0000269|PubMed:11248282, ECO:0000269|PubMed:11728527, ECO:0000269|PubMed:12574802, ECO:0000269|PubMed:12945883, ECO:0000269|PubMed:15075089, ECO:0000269|PubMed:15650540, ECO:0000269|PubMed:17393015, ECO:0000269|PubMed:19135706, ECO:0000269|PubMed:1973167, ECO:0000269|PubMed:1985698, ECO:0000269|PubMed:25313940, ECO:0000269|PubMed:26222694, ECO:0000269|PubMed:2790181, ECO:0000269|PubMed:7669671, ECO:0000269|PubMed:7860069, ECO:0000269|PubMed:8529633, ECO:0000269|PubMed:8845463, ECO:0000269|PubMed:8910490}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.6
uniprot
proteins
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 (PubMed:22409427, PubMed:39880037). Factor Xa activates pro-inflammatory signaling pathways in a protease-activated receptor (PAR)-dependent manner (PubMed:24041930, PubMed:30568593, PubMed:34831181, PubMed:18202198). Up-regulates expression of protease-activated receptors (PARs) F2R, F2RL1 and F2RL2 in dermal microvascular endothelial cells (PubMed:35738824). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, in cardiac fibroblasts and umbilical vein endothelial cells in PAR-1/F2R-dependent manner (PubMed:30568593, PubMed:34831181). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2, IL6, TNF/TNF, IL-1beta/IL1B, IL8/CXCL8 and IL18, in endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824, PubMed:9780208). Induces expression of adhesion molecules, such as ICAM1, VCAM1 and SELE, in endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824, PubMed:9780208). Increases expression of phosphorylated ERK1/2 in dermal microvascular endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824). Triggers activation of the transcription factor NF-kappa-B in dermal microvascular endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824). Activates pro-inflammatory and pro-fibrotic responses in dermal fibroblasts and enhances wound healing probably via PAR-2/F2RL1-dependent mechanism (PubMed:18202198). Activates barrier protective signaling responses in endothelial cells in PAR-2/F2RL1-dependent manner; the activity depends on the cleavage of PAR-2/F2RL1 by factor Xa (PubMed:22409427). Up-regulates expression of plasminogen activator inhibitor 1 (SERPINE1) in atrial tissues (PubMed:24041930). {ECO:0000269|PubMed:18202198, ECO:0000269|PubMed:22409427, ECO:0000269|PubMed:24041930, ECO:0000269|PubMed:30568593, ECO:0000269|PubMed:34831181, ECO:0000269|PubMed:35738824, ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:9780208}.
uniprot
proteins
mass_dalton
54732
uniprot
proteins
mutagenesis
MUTAGEN 255; /note="E->Q: Reduces activity for cleavage of PAR-2/F2RL1. No significant effects on factor Va (F5) binding and activity toward prothrombin in the prothrombinase complex (F10-F5)."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 256; /note="E->Q: Reduces activity for cleavage of PAR-2/F2RL1. No significant effects on factor Va (F5) binding and activity toward prothrombin in the prothrombinase complex (F10-F5)."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 258; /note="E->Q: Reduces activity for cleavage of PAR-2/F2RL1. No significant effects on factor Va (F5) binding and activity toward prothrombin in the prothrombinase complex (F10-F5)."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 282; /note="K->E: Reduces activity for cleavage of PAR-2/F2RL1. No significant effects on factor Va (F5) binding and activity toward prothrombin in the prothrombinase complex (F10-F5)."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 283; /note="R->E: Reduces activity for cleavage of PAR-2/F2RL1. No significant effects on factor Va (F5) binding and activity toward prothrombin in the prothrombinase complex (F10-F5)."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 306; /note="E->A: No significant effects on activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 310; /note="K->A: No significant effects on activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 345; /note="E->A: No significant effects on activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 350; /note="E->A: No significant effects on activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 366; /note="R->A: Reduces activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 372; /note="R->A: Reduces activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 376; /note="R->A: Reduces activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 387; /note="R->A: Reduces activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427"; MUTAGEN 391; /note="K->A: Reduces activity for cleavage of PAR-2/F2RL1."; /evidence="ECO:0000269|PubMed:22409427
uniprot
proteins
post_translational_modification
PTM: Carboxylated by vitamin K-dependent GGCX to form gamma-carboxyglutamate; these residues are essential for the binding of calcium. {ECO:0000269|PubMed:39880037}.; PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8243461}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (PubMed:8920993). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity). {ECO:0000250|UniProtKB:P00743, ECO:0000269|PubMed:8920993}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6871167}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10468877
uniprot
proteins
pubmed
10739379
uniprot
proteins
pubmed
10746568
uniprot
proteins
pubmed
11248282
uniprot
proteins
pubmed
11728527
uniprot
proteins
pubmed
11986214
uniprot
proteins
pubmed
12574802
uniprot
proteins
pubmed
12945883
uniprot
proteins
pubmed
15075089
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15650540
uniprot
proteins
pubmed
16807644
uniprot
proteins
pubmed
17227710
uniprot
proteins
pubmed
17393015
uniprot
proteins
pubmed
18042685
uniprot
proteins
pubmed
18202198
uniprot
proteins
pubmed
1902434
uniprot
proteins
pubmed
19135706
uniprot
proteins
pubmed
1973167
uniprot
proteins
pubmed
1985698
uniprot
proteins
pubmed
20427285
uniprot
proteins
pubmed
21673107
uniprot
proteins
pubmed
22171320
uniprot
proteins
pubmed
22383955
uniprot
proteins
pubmed
22409427
uniprot
proteins
pubmed
24041930
uniprot
proteins
pubmed
25313940
uniprot
proteins
pubmed
2582420
uniprot
proteins
pubmed
2612918
uniprot
proteins
pubmed
26222694
uniprot
proteins
pubmed
2790181
uniprot
proteins
pubmed
3011603
uniprot
proteins
pubmed
30568593
uniprot
proteins
pubmed
31133602
uniprot
proteins
pubmed
34502392
uniprot
proteins
pubmed
34831181
uniprot
proteins
pubmed
35738824
uniprot
proteins
pubmed
37469515
uniprot
proteins
pubmed
3768336
uniprot
proteins
pubmed
39528527
uniprot
proteins
pubmed
39880037
uniprot
proteins
pubmed
6323392
uniprot
proteins
pubmed
6587384
uniprot
proteins
pubmed
6871167
uniprot
proteins
pubmed
7669671
uniprot
proteins
pubmed
7860069
uniprot
proteins
pubmed
8243461
uniprot
proteins
pubmed
8355279
uniprot
proteins
pubmed
8529633
uniprot
proteins
pubmed
8845463
uniprot
proteins
pubmed
8910490
uniprot
proteins
pubmed
8920993
uniprot
proteins
pubmed
9618463
uniprot
proteins
pubmed
9780208
uniprot
proteins
sequence_length
488
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted.
uniprot
proteins