Thrombin

F2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1A2C, 1A3B, 1A3E, 1ABI, 1ABJ, 1AD8, 1AE8, 1AI8, 1AIX, 1AWF, 1AWH, 1AY6, 1B5G, 1B7X, 1BA8, 1BB0, 1BCU, 1BHX, 1BMM, 1BMN, 1BTH, 1C1U, 1C1V, 1C1W, 1C4U, 1C4V, 1C4Y, 1C5L, 1C5N, 1C5O, 1CA8, 1D3D, 1D3P, 1D3Q, 1D3T, 1D4P, 1D6W, 1D9I, 1DE7, 1DIT, 1DM4, 1DOJ, 1DWB, 1DWC, 1DWD, 1DX5, 1E0F, 1EB1, 1EOJ, 1EOL, 1FPC, 1G30, 1G32, 1G37, 1GHV, 1GHW, 1GHX, 1GHY, 1GJ4, 1GJ5, 1H8D, 1H8I, 1HAI, 1HAO, 1HAP, 1HBT, 1HLT, 1HUT, 1HXE, 1HXF, 1IHS, 1JMO, 1JOU, 1JWT, 1K21, 1K22, 1KTS, 1KTT, 1LHC, 1LHD, 1LHE, 1LHF, 1LHG, 1MH0, 1MU6, 1MU8, 1MUE, 1NM6, 1NRN, 1NRO, 1NRP, 1NRQ, 1NRR, 1NRS, 1NT1, 1NU7, 1NU9, 1NY2, 1NZQ, 1O0D, 1O2G, 1O5G, 1OOK, 1OYT, 1P8V, 1PPB, 1QBV, 1QHR, 1QJ1, 1QJ6, 1QJ7, 1QUR, 1RD3, 1RIW, 1SB1, 1SFQ, 1SG8, 1SGI, 1SHH, 1SL3, 1SR5, 1T4U, 1T4V, 1TA2, 1TA6, 1TB6, 1THP, 1THR, 1THS, 1TMB, 1TMU, 1TOM, 1TQ0, 1TQ7, 1TWX, 1UVS, 1VR1, 1VZQ, 1W7G, 1WAY, 1WBG, 1XM1, 1XMN, 1YPE, 1YPG, 1YPJ, 1YPK, 1YPL, 1YPM, 1Z71, 1Z8I, 1Z8J, 1ZGI, 1ZGV, 1ZRB, 2A0Q, 2A2X, 2A45, 2AFQ, 2ANK, 2ANM, 2B5T, 2BDY, 2BVR, 2BVS, 2BVX, 2BXT, 2BXU, 2C8Y, 2FEQ, 2FES, 2GDE, 2GP9, 2H9T, 2HGT, 2HNT, 2HPP, 2HPQ, 2HWL, 2JH0, 2JH6, 2OD3, 2PGB, 2PGQ, 2PW8, 2R2M, 2THF, 2ZFQ, 2ZFR, 2ZG0, 2ZHE, 2ZHF, 2ZHW, 2ZI2, 2ZIQ, 2ZNK, 2ZO3, 3B23, 3B9F, 3BEF, 3BEI, 3BF6, 3BIU, 3BIV, 3BV9, 3C1K, 3C27, 3D49, 3DA9, 3DD2, 3DT0, 3DUX, 3E6P, 3EE0, 3EQ0, 3F68, 3GIC, 3GIS, 3HAT, 3HKJ, 3HTC, 3JZ2, 3LDX, 3LU9, 3NXP, 3P17, 3P6Z, 3P70, 3PO1, 3QGN, 3QLP, 3QTO, 3QTV, 3QWC, 3QX5, 3R3G, 3RLW, 3RLY, 3RM0, 3RM2, 3RML, 3RMM, 3RMN, 3RMO, 3S7H, 3S7K, 3SHA, 3SHC, 3SI3, 3SI4, 3SQE, 3SQH, 3SV2, 3T5F, 3TU7, 3U69, 3U8O, 3U8R, 3U8T, 3U98, 3U9A, 3UTU, 3UWJ, 3VXE, 3VXF, 4BAH, 4BAK, 4BAM, 4BAN, 4BAO, 4BAQ, 4BOH, 4DIH, 4DII, 4DT7, 4DY7, 4E05, 4E06, 4E7R, 4H6S, 4H6T, 4HFP, 4HTC, 4THN, 5GDS, 7KME, 8KME, 1A46, 1A4W, 1A5G, 1A61, 1AFE, 1AHT, 1DWE, 1FPH, 1HAG, 1HAH, 1HDT, 1HGT, 1IHT, 1NO9, 1TBZ, 1TMT, 1UMA, 2C8W, 2C8X, 2C8Z, 2C90, 2C93, 2CF8, 2CF9, 2CN0, 2JH5, 2PKS, 2UUF, 2UUJ, 2UUK, 2V3H, 2V3O, 2ZC9, 2ZDA, 2ZDV, 2ZF0, 2ZFF, 2ZFP, 2ZGB, 2ZGX, 2ZHQ, 3DHK, 3EGK, 3JZ1, 3K65, 3PMH, 3QDZ, 4AX9, 4AYV, 4AYY, 4AZ2, 4CH2, 4CH8, 4HZH, 4I7Y, 4LOY, 4LXB, 4LZ1, 4LZ4, 4MLF, 4N3L, 4NZE, 4NZQ, 4O03, 4RKJ, 4RKO, 4RN6, 4YES, 4UD9, 4UDW, 4UE7, 4UEH, 5AF9, 5AFY, 5AFZ, 5AHG, 5CMX, 4UFD, 5EDM, 5E8E, 5EDK, 4UFE, 4UFG, 4UFF, 5A2M, 5JDU
Identifiers
Aliases	F2, PT, RPRGL2, THPH1, coagulation factor II, thrombin
External IDs	OMIM: 176930; MGI: 88380; HomoloGene: 426; GeneCards: F2; OMA:F2 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	46,739,506 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	91,466,759 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; testicle; ; oocyte; ; secondary oocyte; ; cerebellar hemisphere; ; right hemisphere of cerebellum; ; popliteal artery; ; tibial arteries; ; fundus; ; embryo;
	Top expressed in
	left lobe of liver; ; fetal liver hematopoietic progenitor cell; ; gallbladder; ; yolk sac; ; human fetus; ; sexually immature organism; ; morula; ; primary oocyte; ; secondary oocyte; ; zygote;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	calcium ion binding; signaling receptor binding; peptidase activity; hydrolase activity; growth factor activity; serine-type peptidase activity; thrombospondin receptor activity; protein binding; serine-type endopeptidase activity; lipopolysaccharide binding; heparin binding; enzyme activator activity;
Cellular component	extracellular exosome; blood microparticle; endoplasmic reticulum lumen; Golgi lumen; plasma membrane; extracellular region; extracellular space; external side of plasma membrane; collagen-containing extracellular matrix;
Biological process	blood coagulation, intrinsic pathway; regulation of blood coagulation; positive regulation of phosphatidylinositol 3-kinase signaling; positive regulation of collagen biosynthetic process; multicellular organism development; peptidyl-glutamic acid carboxylation; acute-phase response; positive regulation of reactive oxygen species metabolic process; endoplasmic reticulum to Golgi vesicle-mediated transport; positive regulation of cell growth; cell surface receptor signaling pathway; regulation of gene expression; positive regulation of release of sequestered calcium ion into cytosol; positive regulation of cell population proliferation; leukocyte migration; negative regulation of fibrinolysis; positive regulation of blood coagulation; regulation of cytosolic calcium ion concentration; response to wounding; signal peptide processing; positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; regulation of cell shape; hemostasis; negative regulation of proteolysis; negative regulation of platelet activation; negative regulation of astrocyte differentiation; positive regulation of protein phosphorylation; fibrinolysis; blood coagulation; proteolysis; platelet activation; positive regulation of protein localization to nucleus; positive regulation of lipid kinase activity; regulation of complement activation; antimicrobial humoral immune response mediated by antimicrobial peptide; negative regulation of cytokine production involved in inflammatory response; regulation of signaling receptor activity; G protein-coupled receptor signaling pathway; positive regulation of receptor signaling pathway via JAK-STAT; blood coagulation, fibrin clot formation;
	Sources:Amigo / QuickGO
Orthologs
	2147
	14061
	ENSG00000180210
	ENSMUSG00000027249
	P00734
	P19221
	NM_000506; NM_001311257
	NM_010168
	NP_000497
	NP_034298
	Wikidata
View/Edit Human	View/Edit Mouse

Prothrombin (Coagulation factor II) is encoded in the human by the F2 gene. It is proteolytically cleaved during the clotting process by the prothrombinase enzyme complex to form thrombin.

Thrombin (Factor IIa) (EC 3.4.21.5, fibrinogenase, thrombase, thrombofort, topical, thrombin-C, tropostasin, activated blood-coagulation factor II, E thrombin, beta-thrombin, gamma-thrombin) is a serine protease, that converts fibrinogen into strands of insoluble fibrin, as well as catalyzing many other coagulation-related reactions.^[5]^[6]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000180210 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027249 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL (May 1987). "Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively". Somatic Cell and Molecular Genetics. 13 (3): 285–92. doi:10.1007/BF01535211. PMID 3474786. S2CID 45686258.
^ Degen SJ, Davie EW (September 1987). "Nucleotide sequence of the gene for human prothrombin". Biochemistry. 26 (19): 6165–77. doi:10.1021/bi00393a033. PMID 2825773.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000180210 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000027249 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid3474786-5] Royle NJ, Irwin DM, Koschinsky ML, MacGillivray RT, Hamerton JL (May 1987). "Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively". Somatic Cell and Molecular Genetics. 13 (3): 285–92. doi:10.1007/BF01535211. PMID 3474786. S2CID 45686258.

[pmid2825773-6] Degen SJ, Davie EW (September 1987). "Nucleotide sequence of the gene for human prothrombin". Biochemistry. 26 (19): 6165–77. doi:10.1021/bi00393a033. PMID 2825773.

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