GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]

 FA10_MOUSE              Reviewed;         481 AA.
O88947; O54740; Q99L32;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
29-SEP-2021, entry version 185.
RecName: Full=Coagulation factor X;
EC=3.4.21.6;
AltName: Full=Stuart factor;
Contains:
RecName: Full=Factor X light chain;
Contains:
RecName: Full=Factor X heavy chain;
Contains:
RecName: Full=Activated factor Xa heavy chain;
Flags: Precursor;
Name=F10;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=9684791;
Liang Z., Cooper A., DeFord M.E., Carmeliet P., Collen D., Castellino F.J.,
Rosen E.D.;
"Cloning and characterization of a cDNA encoding murine coagulation factor
X.";
Thromb. Haemost. 80:87-91(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9783672; DOI=10.1016/s0049-3848(98)00110-8;
Heidtmann H.H., Kontermann R.E.;
"Cloning and recombinant expression of mouse coagulation factor X.";
Thromb. Res. 92:33-41(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=10823271;
Cooper A., Liang Z., Castellino F.J., Rosen E.D.;
"Cloning and characterization of the murine coagulation factor X gene.";
Thromb. Haemost. 83:732-735(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
-!- 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.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
prothrombin to form thrombin.; EC=3.4.21.6;
-!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
-!- SUBUNIT: The two chains are formed from a single-chain precursor by the
excision of two Arg residues and are held together by 1 or more
disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
residues allows the modified protein to bind calcium.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- PTM: The activation peptide is cleaved by factor IXa (in the intrinsic
pathway), or by factor VIIa (in the extrinsic pathway). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AF087644; AAC36345.1; -; mRNA.
EMBL; AJ222677; CAA10933.1; -; mRNA.
EMBL; AF211347; AAF22980.1; -; Genomic_DNA.
EMBL; BC003877; AAH03877.1; -; mRNA.
CCDS; CCDS40226.1; -.
RefSeq; NP_031998.3; NM_007972.4.
SMR; O88947; -.
BioGRID; 199566; 10.
IntAct; O88947; 2.
STRING; 10090.ENSMUSP00000068389; -.
MEROPS; S01.216; -.
GlyGen; O88947; 2 sites.
iPTMnet; O88947; -.
PhosphoSitePlus; O88947; -.
CPTAC; non-CPTAC-3413; -.
jPOST; O88947; -.
PaxDb; O88947; -.
PeptideAtlas; O88947; -.
PRIDE; O88947; -.
ProteomicsDB; 275832; -.
Antibodypedia; 11687; 683 antibodies.
DNASU; 14058; -.
Ensembl; ENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444.
GeneID; 14058; -.
KEGG; mmu:14058; -.
UCSC; uc009kws.2; mouse.
CTD; 2159; -.
MGI; MGI:103107; F10.
VEuPathDB; HostDB:ENSMUSG00000031444; -.
eggNOG; ENOG502QS4N; Eukaryota.
GeneTree; ENSGT00940000157694; -.
HOGENOM; CLU_006842_19_5_1; -.
InParanoid; O88947; -.
TreeFam; TF327329; -.
Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
BioGRID-ORCS; 14058; 2 hits in 62 CRISPR screens.
ChiTaRS; F10; mouse.
PRO; PR:O88947; -.
Proteomes; UP000000589; Chromosome 8.
RNAct; O88947; protein.
Bgee; ENSMUSG00000031444; Expressed in liver and 124 other tissues.
ExpressionAtlas; O88947; baseline and differential.
Genevisible; O88947; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005543; F:phospholipid binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
GO; GO:0007596; P:blood coagulation; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation; Calcium; Cleavage on pair of basic residues;
Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1..20
/evidence="ECO:0000255"
PROPEP 21..40
/evidence="ECO:0000250"
/id="PRO_0000027792"
CHAIN 41..481
/note="Coagulation factor X"
/id="PRO_0000027793"
CHAIN 41..180
/note="Factor X light chain"
/evidence="ECO:0000250"
/id="PRO_0000027794"
CHAIN 184..481
/note="Factor X heavy chain"
/evidence="ECO:0000250"
/id="PRO_0000027795"
PROPEP 184..231
/note="Activation peptide"
/evidence="ECO:0000250"
/id="PRO_0000027796"
CHAIN 232..481
/note="Activated factor Xa heavy chain"
/evidence="ECO:0000250"
/id="PRO_0000027797"
DOMAIN 41..85
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 86..122
/note="EGF-like 1; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 125..165
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 232..464
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
ACT_SITE 273
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 319
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 416
/note="Charge relay system"
/evidence="ECO:0000250"
MOD_RES 46
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 47
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 54
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 56
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 59
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 60
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 65
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 66
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 69
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 72
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 75
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 79
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 103
/note="(3R)-3-hydroxyaspartate"
/evidence="ECO:0000250"
CARBOHYD 187
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16944957"
CARBOHYD 218
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 57..62
/evidence="ECO:0000250"
DISULFID 90..101
/evidence="ECO:0000250"
DISULFID 95..110
/evidence="ECO:0000250"
DISULFID 112..121
/evidence="ECO:0000250"
DISULFID 129..140
/evidence="ECO:0000250"
DISULFID 136..149
/evidence="ECO:0000250"
DISULFID 151..164
/evidence="ECO:0000250"
DISULFID 172..339
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463"
DISULFID 238..243
/evidence="ECO:0000250"
DISULFID 258..274
/evidence="ECO:0000250"
DISULFID 387..401
/evidence="ECO:0000250"
DISULFID 412..440
/evidence="ECO:0000250"
CONFLICT 250
/note="I -> V (in Ref. 4; AAH03877)"
/evidence="ECO:0000305"
CONFLICT 294
/note="E -> D (in Ref. 2; CAA10933)"
/evidence="ECO:0000305"
CONFLICT 298
/note="M -> L (in Ref. 2; CAA10933)"
/evidence="ECO:0000305"
SEQUENCE 481 AA; 54018 MW; 8AC09DE5EF9D271E CRC64;
MGSPVQLSLL CVVLASLLLP GKGVFINRER ANNVLARTRR ANSFFEEFKK GNLERECMEE
ICSYEEVREI FEDDEKTKEY WTKYKDGDQC ESSPCQNQGA CRDGIGGYTC TCSEGFEGKN
CELFVRKLCR LDNGDCDQFC REEQNSVVCS CASGYFLGND GKSCISTAPF PCGKITTGRR
KRSVALNTSD SELDLEDALL DEDFLSPTEN PIELLNLNET QPERSSDDLV RIVGGRECKD
GECPWQALLI NEDNEGFCGG TILNEFYILT AAHCLHQARR FKVRVGDRNT EKEEGNEMVH
EVDVVIKHNK FQRDTYDYDI AVLRLKTPIT FRMNVAPACL PQKDWAESTL MTQKTGIVSG
FGRTHEKGRQ SNILKMLEVP YVDRNTCKLS TSFSITQNMF CAGYEAKLED ACQGDSGGPH
VTRFKNTYYV TGIVSWGEGC ARKGKYGIYT KVTTFLKWID RSMKARVGPT AETPRTAGPP
N


Related products :

Catalog number Product name Quantity
20-272-192177 Factor V Heavy Chain - Mouse monoclonal to Factor V Heavy Chain; Activated protein C cofactor Monoclonal 0.125 mg
20-272-192174 Factor XII heavy chain - Mouse monoclonal [B7C9] to Factor XII heavy chain; EC 3.4.21.38; Hageman factor; HAF Monoclonal 0.125 mg
E0676b ELISA Bos taurus,Bovine,Coagulation factor XIII A chain,Coagulation factor XIIIa,F13A,F13A1,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
E0676r ELISA kit Coagulation factor XIII A chain,Coagulation factor XIIIa,F13a,F13a1,Protein-glutamine gamma-glutamyltransferase A chain,Rat,Rattus norvegicus,Transglutaminase A chain 96T
E0676m ELISA kit Coagulation factor XIII A chain,Coagulation factor XIIIa,F13a,F13a1,Mouse,Mus musculus,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
E0676b ELISA kit Bos taurus,Bovine,Coagulation factor XIII A chain,Coagulation factor XIIIa,F13A,F13A1,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
E0676m ELISA Coagulation factor XIII A chain,Coagulation factor XIIIa,F13a,F13a1,Mouse,Mus musculus,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
U0676b CLIA Bos taurus,Bovine,Coagulation factor XIII A chain,Coagulation factor XIIIa,F13A,F13A1,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
E0676r ELISA Coagulation factor XIII A chain,Coagulation factor XIIIa,F13a,F13a1,Protein-glutamine gamma-glutamyltransferase A chain,Rat,Rattus norvegicus,Transglutaminase A chain 96T
U0676m CLIA Coagulation factor XIII A chain,Coagulation factor XIIIa,F13a,F13a1,Mouse,Mus musculus,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
U0676r CLIA Coagulation factor XIII A chain,Coagulation factor XIIIa,F13a,F13a1,Protein-glutamine gamma-glutamyltransferase A chain,Rat,Rattus norvegicus,Transglutaminase A chain 96T
E0676h ELISA kit Coagulation factor XIII A chain,Coagulation factor XIIIa,F13A,F13A1,Homo sapiens,Human,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
U0676h CLIA Coagulation factor XIII A chain,Coagulation factor XIIIa,F13A,F13A1,Homo sapiens,Human,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
E0676h ELISA Coagulation factor XIII A chain,Coagulation factor XIIIa,F13A,F13A1,Homo sapiens,Human,Protein-glutamine gamma-glutamyltransferase A chain,Transglutaminase A chain 96T
EIAAB13708 Coagulation factor XIII B chain,F13B,Fibrin-stabilizing factor B subunit,Homo sapiens,Human,Protein-glutamine gamma-glutamyltransferase B chain,Transglutaminase B chain
GTX21007 Coagulation factor XII (F12) (Heavy Chain) 125 µg
GTX21015 Coagulation factor V (F5) (Heavy Chain) 125 µg
GTX21007 Coagulation factor XII (F12) (Heavy Chain) 125 µg
BM2329 Coagulation factor XII (F12) (Heavy Chain) 0.25 mg
BM2329 Coagulation factor XII (F12) (Heavy Chain) 0.25 mg
BM2328 Coagulation factor V (F5) (Heavy Chain) 0.25 mg
BM2328 Coagulation factor V (F5) (Heavy Chain) 0.25 mg
GTX21015 Coagulation factor V (F5) (Heavy Chain) 125 µg
GTX40797 Coagulation factor XII (F12) (Heavy Chain) 100 µg
19801 Coagulation factor XII (F12) (Heavy Chain) 0.25 mg
Pathways :
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP2148: Brain derived neurotrophic factor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1983: Splicing factor NOVA regulated synpatic proteins
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP272: Blood Clotting Cascade
WP1002: Electron Transport Chain
WP1665: Limonene and pinene degradation
WP111: Electron Transport Chain
WP772: Electron Transport Chain
WP1339: Electron Transport Chain
WP884: Electron Transport Chain
WP1626: Benzoate degradation via CoA ligation
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP542: Electron Transport Chain

Related Genes :
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10 FX] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Virus-activating protease) (VAP) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F9] Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain]
[] Venom prothrombin activator pseutarin-C catalytic subunit (PCCS) (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F10 TrFX] Coagulation factor X (EC 3.4.21.6) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
[F12] Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)]
[] Coagulation factor X-activating enzyme heavy chain (EC 3.4.24.58) (Coagulation factor X-activating enzyme chain alpha) (Snake venom metalloproteinase) (SVMP) (VL factor X activator) (VLFXA heavy chain) [Cleaved into: Coagulation factor X-activating enzyme heavy chain alternate form]
[F2] Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]
[F11] Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain]
[F7 Cf7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F8 F8C] Coagulation factor VIII (Antihemophilic factor) (AHF) (Procoagulant component) [Cleaved into: Factor VIIIa heavy chain, 200 kDa isoform; Factor VIIIa heavy chain, 92 kDa isoform; Factor VIII B chain; Factor VIIIa light chain]
[PROC] Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B heavy chain]
[HABP2 HGFAL PHBP] Hyaluronan-binding protein 2 (EC 3.4.21.-) (Factor VII-activating protease) (Factor seven-activating protease) (FSAP) (Hepatocyte growth factor activator-like protein) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form]
[F10] Coagulation factor X isoform 1 (PFX1) (EC 3.4.21.6) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F10] Coagulation factor X isoform 2 (PFX2) (EC 3.4.21.6) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[KLKB1 KLK3] Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) (PKK) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light chain]
[CFI IF] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[MASP1 CRARF CRARF1 PRSS5] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[Cfi If] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[PPAF1 PPAF-I] Phenoloxidase-activating factor 1 (EC 3.4.21.-) (Prophenoloxidase-activating factor I) (Serine protease PPAF-1) [Cleaved into: Phenoloxidase-activating factor 1 light chain; Phenoloxidase-activating factor 1 heavy chain]

Bibliography :
[30578302] Occlusion of anion-binding exosite 2 in meizothrombin explains its impaired ability to activate factor V.
[19389514] Secondary structure and 3D homology modeling of swine leukocyte antigen class 2 (SLA-2) molecules.
[15725905] Coagulation factor V: a plethora of anticoagulant molecules.
[11513607] Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity.
[10627463] Reduction of the antigenicity of factor VIII toward complex inhibitory antibody plasmas using multiply-substituted hybrid human/porcine factor VIII molecules.
[9718313] Proteolysis of factor V by cathepsin G and elastase indicates that cleavage at Arg1545 optimizes cofactor function by facilitating factor Xa binding.
[9242537] Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V.
[9065469] Inhibitory mechanism of the protein C pathway on tissue factor-induced thrombin generation. Synergistic effect in combination with tissue factor pathway inhibitor.
[8841400] Kinetics of factor VIII light-chain cleavage by thrombin and factor Xa. A regulatory role of the factor VIII heavy-chain region Lys713-Arg740.
[7492334] Characterization of des-(741-1668)-factor VIII, a single-chain factor VIII variant with a fusion site susceptible to proteolysis by thrombin and factor Xa.