F2
entrez
2147
canonical
uniprot
P00734
canonical
ensembl
ENSG00000180210
resolver
ensp
ENSP00000308541
resolver
enst
ENST00000311907
resolver
genesymbol
F2
resolver
hgnc
HGNC:3535
resolver
uniprot
B2R7F7
resolver
uniprot
B4E1A7
resolver
uniprot
Q4QZ40
resolver
uniprot
Q53H04
resolver
uniprot
Q53H06
resolver
uniprot
Q69EZ7
resolver
uniprot
Q7Z7P3
resolver
uniprot
Q9UCA1
resolver
uniprot_entry
THRB_HUMAN
resolver
uniprot_sec
B2R7F7
resolver
uniprot_sec
B4E1A7
resolver
uniprot_sec
Q4QZ40
resolver
uniprot_sec
Q53H04
resolver
uniprot_sec
Q53H06
resolver
uniprot_sec
Q69EZ7
resolver
uniprot_sec
Q7Z7P3
resolver
uniprot_sec
Q9UCA1
resolver
activity_regulation
ACTIVITY REGULATION: Activity is promoted in the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate (PubMed:2019570, PubMed:21976677). Inhibited by SERPINA5 (PubMed:6323392). {ECO:0000269|PubMed:2019570, ECO:0000269|PubMed:21976677, ECO:0000269|PubMed:6323392}.
uniprot
proteins
amino_acid_sequence
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE
uniprot
proteins
disease_involvement
DISEASE: Factor II deficiency (FA2D) [MIM:613679]: A very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. {ECO:0000269|PubMed:1349838, ECO:0000269|PubMed:1354985, ECO:0000269|PubMed:1421398, ECO:0000269|PubMed:14962227, ECO:0000269|PubMed:2719946, ECO:0000269|PubMed:3242619, ECO:0000269|PubMed:3567158, ECO:0000269|PubMed:3771562, ECO:0000269|PubMed:3801671, ECO:0000269|PubMed:6405779, ECO:0000269|PubMed:7792730, ECO:0000269|PubMed:7865694}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Thrombophilia due to thrombin defect (THPH1) [MIM:188050]: A multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation. {ECO:0000269|PubMed:2825773}. Note=The disease is caused by variants affecting the gene represented in this entry. A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis.; DISEASE: Pregnancy loss, recurrent, 2 (RPRGL2) [MIM:614390]: A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions. {ECO:0000269|PubMed:11506076}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.5
uniprot
proteins
function
FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces (PubMed:2019570, PubMed:21976677). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (PubMed:30568593, PubMed:9780208). {ECO:0000269|PubMed:2019570, ECO:0000269|PubMed:21976677, ECO:0000269|PubMed:2856554, ECO:0000269|PubMed:30568593, ECO:0000269|PubMed:9780208}.
uniprot
proteins
mass_dalton
70037
uniprot
proteins
mutagenesis
MUTAGEN 314; /note="R->Q: Loss of cleavage by factor Xa."; /evidence="ECO:0000269|PubMed:34265300"; MUTAGEN 363; /note="R->Q: Loss of cleavage by factor Xa."; /evidence="ECO:0000269|PubMed:34265300"; MUTAGEN 568; /note="S->A: Loss of catalytic activity; no effect on cleavage at R-198 by factor Xa."; /evidence="ECO:0000269|PubMed:34265300
uniprot
proteins
post_translational_modification
PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin. {ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407}.; PTM: N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:873923}.; PTM: In the penultimate step of the coagulation cascade, prothrombin is converted to thrombin by the prothrombinase complex composed of factor Xa (F10), cofactor Va (F5), and phospholipids. This activation requires factor Xa-catalyzed sequential cleavage at 2 sites, Arg-314 and Arg-363, along 2 possible pathways. In the first pathway, the first cleavage occurs at Arg-314, leading to the formation of the inactive intermediate prethrombin-2. This pathway preferentially occurs on platelets and in the absence of cofactor Va. In the second pathway, the first cleavage occurs at Arg-363, which separates protease domain into 2 chains that remain connected through a disulfide bond and generates the active intermediate meizothrombin. The presence of cofactor Va directs activation along the meizothrombin pathway and greatly accelerates the rate of cleavage at Arg-363, but has a smaller effect on the cleavage of meizothrombin at Arg-314. Meizothrombin accumulates as an intermediate when prothrombinase is assembled on the membrane of red blood cells. {ECO:0000305|PubMed:34265300}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10051558
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
11493008
uniprot
proteins
pubmed
11506076
uniprot
proteins
pubmed
1349838
uniprot
proteins
pubmed
1354985
uniprot
proteins
pubmed
1421398
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14760718
uniprot
proteins
pubmed
14962227
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15534175
uniprot
proteins
pubmed
15885491
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16763681
uniprot
proteins
pubmed
17244316
uniprot
proteins
pubmed
17685615
uniprot
proteins
pubmed
18291642
uniprot
proteins
pubmed
18362344
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19838169
uniprot
proteins
pubmed
2019570
uniprot
proteins
pubmed
21976677
uniprot
proteins
pubmed
22028381
uniprot
proteins
pubmed
22053189
uniprot
proteins
pubmed
22171320
uniprot
proteins
pubmed
23223529
uniprot
proteins
pubmed
2369893
uniprot
proteins
pubmed
2374926
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2583108
uniprot
proteins
pubmed
266717
uniprot
proteins
pubmed
2719946
uniprot
proteins
pubmed
2825773
uniprot
proteins
pubmed
2856554
uniprot
proteins
pubmed
28592490
uniprot
proteins
pubmed
30568593
uniprot
proteins
pubmed
3242619
uniprot
proteins
pubmed
33732248
uniprot
proteins
pubmed
34265300
uniprot
proteins
pubmed
34502392
uniprot
proteins
pubmed
34688666
uniprot
proteins
pubmed
3567158
uniprot
proteins
pubmed
3759958
uniprot
proteins
pubmed
3771562
uniprot
proteins
pubmed
3801671
uniprot
proteins
pubmed
6305407
uniprot
proteins
pubmed
6323392
uniprot
proteins
pubmed
6405779
uniprot
proteins
pubmed
7792730
uniprot
proteins
pubmed
7865694
uniprot
proteins
pubmed
8071320
uniprot
proteins
pubmed
8073540
uniprot
proteins
pubmed
8251938
uniprot
proteins
pubmed
873923
uniprot
proteins
pubmed
9183005
uniprot
proteins
pubmed
9214615
uniprot
proteins
pubmed
9780208
uniprot
proteins
sequence_length
622
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space.
uniprot
proteins