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

 FA10_TROCA              Reviewed;         483 AA.
Q4QXT9; A5X459;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
02-DEC-2020, entry version 82.
RecName: Full=Coagulation factor X;
EC=3.4.21.6;
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; Synonyms=TrFX;
Tropidechis carinatus (Australian rough-scaled snake).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
Serpentes; Colubroidea; Elapidae; Notechinae; Tropidechis.
NCBI_TaxID=100989;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=15630489; DOI=10.1160/th04-07-0435;
Reza M.A., Swarup S., Kini R.M.;
"Two parallel prothrombin activator systems in Australian rough-scaled
snake, Tropidechis carinatus. Structural comparison of venom prothrombin
activator with blood coagulation factor X.";
Thromb. Haemost. 93:40-47(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Liver;
PubMed=17239167; DOI=10.1111/j.1538-7836.2006.02266.x;
Reza M.A., Swarup S., Kini R.M.;
"Structure of two genes encoding parallel prothrombin activators in
Tropidechis carinatus snake: gene duplication and recruitment of factor X
gene to the venom gland.";
J. Thromb. Haemost. 5:117-126(2007).
-!- 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. {ECO:0000250}.
-!- 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 {ECO:0000250}.
-!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
-!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
carboxylation. These residues are essential for the binding of calcium.
-!- PTM: The activation peptide is cleaved by factor IXa (in the intrinsic
pathway), or by factor VIIa (in the extrinsic pathway). {ECO:0000250}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor X entry;
URL="https://en.wikipedia.org/wiki/Factor_X";
---------------------------------------------------------------------------
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EMBL; AY651849; AAV65959.1; -; mRNA.
EMBL; DQ533831; ABG02403.1; -; Genomic_DNA.
SMR; Q4QXT9; -.
MEROPS; S01.396; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; IEA:InterPro.
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; 1.
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.
2: Evidence at transcript level;
Calcium; Cleavage on pair of basic residues; Disulfide bond;
EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
Hydrolase; Hydroxylation; Protease; Prothrombin activator; Repeat;
Secreted; Serine protease; Signal; Toxin; Zymogen.
SIGNAL 1..20
/evidence="ECO:0000255"
PROPEP 21..40
/evidence="ECO:0000250"
/id="PRO_0000043201"
CHAIN 41..483
/note="Coagulation factor X"
/id="PRO_0000043202"
CHAIN 41..180
/note="Factor X light chain"
/id="PRO_0000043203"
CHAIN 183..483
/note="Factor X heavy chain"
/id="PRO_0000043204"
PROPEP 183..238
/note="Activation peptide"
/evidence="ECO:0000250"
/id="PRO_0000043205"
CHAIN 239..483
/note="Activated factor Xa heavy chain"
/id="PRO_0000043206"
DOMAIN 41..86
/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 239..470
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
ACT_SITE 280
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 325
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 422
/note="Charge relay system"
/evidence="ECO:0000250"
MOD_RES 46
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 47
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 54
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 56
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 59
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 60
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 65
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 66
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 69
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 72
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 75
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 103
/note="(3R)-3-hydroxyaspartate"
/evidence="ECO:0000250"
CARBOHYD 92
/note="O-linked (Hex...) serine"
/evidence="ECO:0000250"
CARBOHYD 211
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 223
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 241
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 283
/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..345
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463"
DISULFID 245..250
/evidence="ECO:0000250"
DISULFID 265..281
/evidence="ECO:0000250"
DISULFID 393..407
/evidence="ECO:0000250"
DISULFID 418..446
/evidence="ECO:0000250"
SEQUENCE 483 AA; 53901 MW; F040EAC534BC960F CRC64;
MAPQLLLCLI LTFLWSLSEA ESNVFLKSKV ANRFLQRTKR ANSLFEEFKA GNIERECIEE
RCSKEEAREA FEDNEKTETF WNVYVDGDQC SSNPCHYGGT CKDGIGSYTC TCLAGYEGKN
CQYVLYQSCR VDNGNCWHFC KPVQNEIQCS CAESYLLGDD GYSCVAGGDF SCGRNIKARN
KREASLPDFQ TDFSDDYDAI DENNFVETPT NFSGLVPTVQ SQNATLLKKS DNPSPDIRVV
NGTDCKLGEC PWQALLINDQ GDGFCGGTIL SPIYVLTAAH CINQTKYIRV VVGEIDISRK
KTGRLLSVDK IYVHQKFVPS TYDYDIALIQ MKTPIQFSEN VVPACLPTAD FANQVLMKQD
FGIVSGFGRT RERGQTSNTL KVVTLPYVDR HTCMLSSNFP ITQNMFCAGY NTLPQDACQG
DSGGPHITAY RDTHFITGII SWGEGCAQTG KYGAYTKVSR FILWIKRIMR LKLPSTESST
GRL


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WP1654: gamma-Hexachlorocyclohexane degradation
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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)]
[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]
[] 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]
[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]
[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]
[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]
[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]
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[Klkb1 Klk3 Pk] Plasma kallikrein (EC 3.4.21.34) (Fletcher factor) (Kininogenin) (Plasma prekallikrein) [Cleaved into: Plasma kallikrein heavy chain; Plasma kallikrein light 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.