F2
entrez
14061
canonical
uniprot
P19221
canonical
ensembl
ENSMUSG00000027249
resolver
ensp
ENSMUSP00000028681
resolver
enst
ENSMUST00000028681
resolver
genesymbol
F2
resolver
genesymbol_syn
Cf2
resolver
uniprot
Q3TJ94
resolver
uniprot_entry
Q3TJ94_MOUSE
resolver
uniprot_entry
THRB_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Activity is promoted in the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate (By similarity). Inhibited by SERPINA5 (By similarity). {ECO:0000250|UniProtKB:P00734}.
uniprot
proteins
amino_acid_sequence
MSHVRGLGLPGCLALAALVSLVHSQHVFLAPQQALSLLQRVRRANSGFLEELRKGNLERECVEEQCSYEEAFEALESPQDTDVFWAKYTVCDSVRKPRETFMDCLEGRCAMDLGVNYLGTVNVTHTGIQCQLWRSRYPHKPEINSTTHPGADLKENFCRNPDSSTTGPWCYTTDPTVRREECSVPVCGQEGRTTVVMTPRSGGSKDNLSPPLGQCLTERGRLYQGNLAVTTLGSPCLPWNSLPAKTLSKYQDFDPEVKLVENFCRNPDWDEEGAWCYVAGQPGDFEYCNLNYCEEAVGEENYDVDESIAGRTTDAEFHTFFNEKTFGLGEADCGLRPLFEKKSLKDTTEKELLDSYIDGRIVEGWDAEKGIAPWQVMLFRKSPQELLCGASLISDRWVLTAAHCILYPPWDKNFTENDLLVRIGKHSRTRYERNVEKISMLEKIYVHPRYNWRENLDRDIALLKLKKPVPFSDYIHPVCLPDKQTVTSLLRAGYKGRVTGWGNLRETWTTNINEIQPSVLQVVNLPIVERPVCKASTRIRITDNMFCAGFKVNDTKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRKGKYGFYTHVFRLKRWIQKVIDQFG
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 (By similarity). Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces (By similarity). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P00734}.
uniprot
proteins
mass_dalton
70269
uniprot
proteins
mutagenesis
MUTAGEN 565; /note="S->A: Loss of protease activity."; /evidence="ECO:0000269|PubMed:17606903
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:2222810}.; 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-311 and Arg-360, along 2 possible pathways. In the first pathway, the first cleavage occurs at Arg-311, 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-360, 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-360, but has a smaller effect on the cleavage of meizothrombin at Arg-311. Meizothrombin accumulates as an intermediate when prothrombinase is assembled on the membrane of red blood cells. {ECO:0000250|UniProtKB:P00734}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1557383
uniprot
proteins
pubmed
17330941
uniprot
proteins
pubmed
17428793
uniprot
proteins
pubmed
17606903
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2222810
uniprot
proteins
sequence_length
618
uniprot
proteins