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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_BOVIN              Reviewed;         492 AA.
P00743;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
23-FEB-2022, entry version 224.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-487.
PubMed=6330671; DOI=10.1093/nar/12.11.4481;
Fung M.R., Campbell R.M., McGillivray R.T.A.;
"Blood coagulation factor X mRNA encodes a single polypeptide chain
containing a prepro leader sequence.";
Nucleic Acids Res. 12:4481-4492(1984).
[2]
PROTEIN SEQUENCE OF 41-180, AND GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47;
GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72; GLU-75 AND
GLU-79.
PubMed=6766735; DOI=10.1021/bi00545a009;
Enfield D.L., Ericsson L.H., Fujikawa K., Walsh K.A., Neurath H.,
Titani K.;
"Amino acid sequence of the light chain of bovine factor X1 (Stuart
factor).";
Biochemistry 19:659-667(1980).
[3]
HYDROXYLATION AT ASP-103.
PubMed=6688526; DOI=10.1016/0006-291x(83)90961-0;
McMullen B.A., Fujikawa K., Kisiel W.;
"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent
blood coagulation zymogens.";
Biochem. Biophys. Res. Commun. 115:8-14(1983).
[4]
PROTEIN SEQUENCE OF 183-492, GLYCOSYLATION AT ASN-218 AND THR-485, AND
DISULFIDE BONDS.
PubMed=1059093; DOI=10.1073/pnas.72.8.3082;
Titani K., Fujikawa K., Enfield D.L., Ericsson L.H., Walsh K.A.,
Neurath H.;
"Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain.";
Proc. Natl. Acad. Sci. U.S.A. 72:3082-3086(1975).
[5]
PROTEIN SEQUENCE OF 183-233, AND GLYCOSYLATION AT THR-208.
PubMed=8243461; DOI=10.1111/j.1432-1033.1993.tb18361.x;
Inoue K., Morita T.;
"Identification of O-linked oligosaccharide chains in the activation
peptides of blood coagulation factor X. The role of the carbohydrate
moieties in the activation of factor X.";
Eur. J. Biochem. 218:153-163(1993).
[6]
ACTIVE SITE.
PubMed=4264286; DOI=10.1021/bi00776a004;
Titani K., Hermodson M.A., Fujikawa K., Ericsson L.H., Walsh K.A.,
Neurath H., Davie E.W.;
"Bovine factor X 1a (activated Stuart factor). Evidence of homology with
mammalian serine proteases.";
Biochemistry 11:4899-4903(1972).
[7]
PROTEOLYTIC PROCESSING.
PubMed=1059122; DOI=10.1073/pnas.72.9.3359;
Fujikawa K., Titani K., Davie E.W.;
"Activation of bovine factor X (Stuart factor): conversion of factor Xa-
alpha to factor Xa-beta.";
Proc. Natl. Acad. Sci. U.S.A. 72:3359-3363(1975).
[8]
CALCIUM-BINDING.
PubMed=6546930;
Sugo T., Bjoerk I., Holmgren A., Stenflo J.;
"Calcium-binding properties of bovine factor X lacking the gamma-
carboxyglutamic acid-containing region.";
J. Biol. Chem. 259:5705-5710(1984).
[9]
SULFATION AT TYR-200.
PubMed=3949800;
Morita T., Jackson C.M.;
"Localization of the structural difference between bovine blood coagulation
factors X1 and X2 to tyrosine 18 in the activation peptide.";
J. Biol. Chem. 261:4008-4014(1986).
[10]
STRUCTURE BY NMR OF 85-126.
PubMed=2261466; DOI=10.1021/bi00487a018;
Selander M., Persson E., Stenflo J., Drakenberg T.;
"1H NMR assignment and secondary structure of the Ca2(+)-free form of the
amino-terminal epidermal growth factor like domain in coagulation factor
X.";
Biochemistry 29:8111-8118(1990).
[11]
STRUCTURE BY NMR OF 85-126.
PubMed=1627540; DOI=10.1021/bi00141a004;
Ullner M., Selander M., Persson E., Stenflo J., Drakenberg T., Teleman O.;
"Three-dimensional structure of the apo form of the N-terminal EGF-like
module of blood coagulation factor X as determined by NMR spectroscopy and
simulated folding.";
Biochemistry 31:5974-5983(1992).
[12]
STRUCTURE BY NMR OF 85-126.
PubMed=1527084; DOI=10.2210/pdb1ccf/pdb;
Selander-Sunnerhagen M., Ullner M., Persson E., Teleman O., Stenflo J.,
Drakenberg T.;
"How an epidermal growth factor (EGF)-like domain binds calcium. High
resolution NMR structure of the calcium form of the NH2-terminal EGF-like
domain in coagulation factor X.";
J. Biol. Chem. 267:19642-19649(1992).
[13]
STRUCTURE BY NMR OF 41-126.
PubMed=8794734; DOI=10.1021/bi960633j;
Sunnerhagen M., Olah G.A., Stenflo J., Forsen S., Drakenberg T.,
Trewhella J.;
"The relative orientation of Gla and EGF domains in coagulation factor X is
altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle
X-ray scattering study.";
Biochemistry 35:11547-11559(1996).
-!- 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.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
residues allows the modified protein to bind calcium.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1059093,
ECO:0000269|PubMed:8243461}.
-!- PTM: Proteolytically cleaved and activated by cathepsin CTSG (By
similarity). The activation peptide is cleaved by factor IXa (in the
intrinsic pathway), or by factor VIIa (in the extrinsic pathway)
(PubMed:1059122). {ECO:0000250|UniProtKB:P00742,
ECO:0000269|PubMed:1059122}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:6688526}.
-!- MISCELLANEOUS: Calcium also binds, with stronger affinity to another
site, beyond the GLA domain.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
---------------------------------------------------------------------------
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EMBL; X00673; CAA25286.1; -; mRNA.
PIR; A22867; EXBO.
RefSeq; NP_001073682.1; NM_001080213.1.
PDB; 1APO; NMR; -; A=85-126.
PDB; 1CCF; NMR; -; A=85-126.
PDB; 1IOD; X-ray; 2.30 A; G=41-84.
PDB; 1KIG; X-ray; 3.00 A; H=234-474, L=129-179.
PDB; 1WHE; NMR; -; A=41-126.
PDB; 1WHF; NMR; -; A=41-126.
PDBsum; 1APO; -.
PDBsum; 1CCF; -.
PDBsum; 1IOD; -.
PDBsum; 1KIG; -.
PDBsum; 1WHE; -.
PDBsum; 1WHF; -.
BMRB; P00743; -.
SMR; P00743; -.
ELM; P00743; -.
IntAct; P00743; 1.
STRING; 9913.ENSBTAP00000021789; -.
BindingDB; P00743; -.
ChEMBL; CHEMBL3656; -.
MEROPS; S01.216; -.
GlyConnect; 101; 2 N-Linked glycans (1 site), 9 O-Linked glycans.
iPTMnet; P00743; -.
PaxDb; P00743; -.
GeneID; 280787; -.
KEGG; bta:280787; -.
CTD; 2159; -.
eggNOG; ENOG502QS4N; Eukaryota.
HOGENOM; CLU_006842_19_5_1; -.
InParanoid; P00743; -.
OMA; HITRYND; -.
OrthoDB; 1314811at2759; -.
TreeFam; TF327329; -.
SABIO-RK; P00743; -.
EvolutionaryTrace; P00743; -.
PRO; PR:P00743; -.
Proteomes; UP000009136; Unplaced.
Bgee; ENSBTAG00000016385; Expressed in liver and 61 other tissues.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
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;
3D-structure; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Direct protein sequencing;
Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal; Sulfation; Zymogen.
SIGNAL 1..23
/evidence="ECO:0000255"
PROPEP 24..40
/evidence="ECO:0000269|PubMed:6766735"
/id="PRO_0000027779"
CHAIN 41..492
/note="Coagulation factor X"
/id="PRO_0000027780"
CHAIN 41..180
/note="Factor X light chain"
/id="PRO_0000027781"
CHAIN 183..492
/note="Factor X heavy chain"
/id="PRO_0000027782"
PROPEP 183..233
/note="Activation peptide"
/id="PRO_0000027783"
CHAIN 234..492
/note="Activated factor Xa heavy chain"
/id="PRO_0000027784"
PROPEP 476..492
/note="May be removed but is not necessary for activation"
/id="PRO_0000027785"
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 234..466
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
REGION 472..492
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 275
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:4264286"
ACT_SITE 321
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:4264286"
ACT_SITE 418
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:4264286"
SITE 233..234
/note="Cleavage; by coagulation factor IXa and coagulation
factor VIIa"
MOD_RES 46
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 47
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 54
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 56
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 59
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 60
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 65
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 66
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 69
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 72
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 75
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 79
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 103
/note="(3R)-3-hydroxyaspartate"
/evidence="ECO:0000269|PubMed:6688526"
MOD_RES 200
/note="Sulfotyrosine"
/evidence="ECO:0000269|PubMed:3949800"
CARBOHYD 208
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:8243461"
CARBOHYD 218
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:1059093"
/id="CAR_000011"
CARBOHYD 485
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 57..62
/evidence="ECO:0000250"
DISULFID 90..101
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 95..110
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 112..121
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 129..140
/evidence="ECO:0000250"
DISULFID 136..149
/evidence="ECO:0000250"
DISULFID 151..164
/evidence="ECO:0000250"
DISULFID 172..341
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|PubMed:1059093"
DISULFID 240..245
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 260..276
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 389..403
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 414..442
/evidence="ECO:0000269|PubMed:1059093"
CONFLICT 103
/note="D -> N (in Ref. 2; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 293
/note="Missing (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 296..298
/note="EGN -> GDE (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 335
/note="Missing (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 349..350
/note="EA -> AE (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 355
/note="Missing (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 442..445
/note="CARK -> GKFG (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
HELIX 46..48
/evidence="ECO:0007829|PDB:1IOD"
HELIX 53..57
/evidence="ECO:0007829|PDB:1IOD"
STRAND 58..61
/evidence="ECO:0007829|PDB:1WHE"
HELIX 64..71
/evidence="ECO:0007829|PDB:1IOD"
HELIX 74..82
/evidence="ECO:0007829|PDB:1IOD"
TURN 86..90
/evidence="ECO:0007829|PDB:1WHE"
STRAND 100..102
/evidence="ECO:0007829|PDB:1CCF"
STRAND 105..107
/evidence="ECO:0007829|PDB:1APO"
STRAND 109..111
/evidence="ECO:0007829|PDB:1CCF"
STRAND 116..118
/evidence="ECO:0007829|PDB:1APO"
STRAND 121..123
/evidence="ECO:0007829|PDB:1WHF"
TURN 131..134
/evidence="ECO:0007829|PDB:1KIG"
STRAND 135..138
/evidence="ECO:0007829|PDB:1KIG"
STRAND 155..157
/evidence="ECO:0007829|PDB:1KIG"
STRAND 164..166
/evidence="ECO:0007829|PDB:1KIG"
STRAND 168..170
/evidence="ECO:0007829|PDB:1KIG"
STRAND 235..237
/evidence="ECO:0007829|PDB:1KIG"
TURN 242..244
/evidence="ECO:0007829|PDB:1KIG"
STRAND 248..252
/evidence="ECO:0007829|PDB:1KIG"
STRAND 254..256
/evidence="ECO:0007829|PDB:1KIG"
STRAND 258..264
/evidence="ECO:0007829|PDB:1KIG"
STRAND 266..272
/evidence="ECO:0007829|PDB:1KIG"
STRAND 304..309
/evidence="ECO:0007829|PDB:1KIG"
TURN 315..317
/evidence="ECO:0007829|PDB:1KIG"
STRAND 323..329
/evidence="ECO:0007829|PDB:1KIG"
HELIX 345..350
/evidence="ECO:0007829|PDB:1KIG"
TURN 351..354
/evidence="ECO:0007829|PDB:1KIG"
STRAND 355..363
/evidence="ECO:0007829|PDB:1KIG"
STRAND 365..367
/evidence="ECO:0007829|PDB:1KIG"
STRAND 370..372
/evidence="ECO:0007829|PDB:1KIG"
STRAND 377..383
/evidence="ECO:0007829|PDB:1KIG"
HELIX 386..392
/evidence="ECO:0007829|PDB:1KIG"
STRAND 401..407
/evidence="ECO:0007829|PDB:1KIG"
STRAND 421..426
/evidence="ECO:0007829|PDB:1KIG"
STRAND 429..443
/evidence="ECO:0007829|PDB:1KIG"
STRAND 447..454
/evidence="ECO:0007829|PDB:1KIG"
HELIX 455..457
/evidence="ECO:0007829|PDB:1KIG"
HELIX 458..464
/evidence="ECO:0007829|PDB:1KIG"
SEQUENCE 492 AA; 54510 MW; D5BD911FB72F1D30 CRC64;
MAGLLHLVLL STALGGLLRP AGSVFLPRDQ AHRVLQRARR ANSFLEEVKQ GNLERECLEE
ACSLEEAREV FEDAEQTDEF WSKYKDGDQC EGHPCLNQGH CKDGIGDYTC TCAEGFEGKN
CEFSTREICS LDNGGCDQFC REERSEVRCS CAHGYVLGDD SKSCVSTERF PCGKFTQGRS
RRWAIHTSED ALDASELEHY DPADLSPTES SLDLLGLNRT EPSAGEDGSQ VVRIVGGRDC
AEGECPWQAL LVNEENEGFC GGTILNEFYV LTAAHCLHQA KRFTVRVGDR NTEQEEGNEM
AHEVEMTVKH SRFVKETYDF DIAVLRLKTP IRFRRNVAPA CLPEKDWAEA TLMTQKTGIV
SGFGRTHEKG RLSSTLKMLE VPYVDRSTCK LSSSFTITPN MFCAGYDTQP EDACQGDSGG
PHVTRFKDTY FVTGIVSWGE GCARKGKFGV YTKVSNFLKW IDKIMKARAG AAGSRGHSEA
PATWTVPPPL PL


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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)
WP1983: Splicing factor NOVA regulated synpatic proteins
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
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
WP1708: Terpenoid backbone biosynthesis

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] 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]
[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]
[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]
[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]
[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.