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Activation peptide fragment 1 (EC 3 4 21 5) (Activation peptide fragment 2) (Coagulation factor II) (Prothrombin) (Thrombin heavy chain) (Thrombin light chain)

 A0A4W2EET2_BOBOX        Unreviewed;       631 AA.
A0A4W2EET2;
18-SEP-2019, integrated into UniProtKB/TrEMBL.
18-SEP-2019, sequence version 1.
29-SEP-2021, entry version 13.
RecName: Full=Activation peptide fragment 1 {ECO:0000256|ARBA:ARBA00013849};
EC=3.4.21.5 {ECO:0000256|ARBA:ARBA00012174};
AltName: Full=Activation peptide fragment 2 {ECO:0000256|ARBA:ARBA00013851};
AltName: Full=Coagulation factor II {ECO:0000256|ARBA:ARBA00019447};
AltName: Full=Prothrombin {ECO:0000256|ARBA:ARBA00014840};
AltName: Full=Thrombin heavy chain {ECO:0000256|ARBA:ARBA00022013};
AltName: Full=Thrombin light chain {ECO:0000256|ARBA:ARBA00014325};
Name=F2 {ECO:0000313|Ensembl:ENSBIXP00000035482};
Bos indicus x Bos taurus (Hybrid cattle).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Bovinae; Bos.
NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000035482, ECO:0000313|Proteomes:UP000314981};
[1] {ECO:0000313|Ensembl:ENSBIXP00000035482, ECO:0000313|Proteomes:UP000314981}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
"Haplotype-resolved cattle genomes.";
Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSBIXP00000035482}
IDENTIFICATION.
Ensembl;
Submitted (JUL-2019) to UniProtKB.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form
fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
Evidence={ECO:0000256|ARBA:ARBA00001621};
-!- CAUTION: Lacks conserved residue(s) required for the propagation of
feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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SMR; A0A4W2EET2; -.
Ensembl; ENSBIXT00000046277; ENSBIXP00000035482; ENSBIXG00000007295.
Proteomes; UP000314981; Chromosome 15.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0070053; F:thrombospondin receptor activity; IEA:Ensembl.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
GO; GO:0051838; P:cytolysis by host of symbiont cells; IEA:Ensembl.
GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; IEA:Ensembl.
GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:0090218; P:positive regulation of lipid kinase activity; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
CDD; cd00108; KR; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 3.
Gene3D; 2.40.20.10; -; 2.
Gene3D; 4.10.140.10; -; 1.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR003966; Prothrombin/thrombin.
InterPro; IPR018992; Thrombin_light_chain.
InterPro; IPR037111; Thrombin_light_chain_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24254:SF10; PTHR24254:SF10; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00051; Kringle; 2.
Pfam; PF09396; Thrombin_light; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001149; Thrombin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
PRINTS; PR01505; PROTHROMBIN.
SMART; SM00069; GLA; 1.
SMART; SM00130; KR; 2.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 2.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS00021; KRINGLE_1; 2.
PROSITE; PS50070; KRINGLE_2; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
4: Predicted;
Acute phase {ECO:0000256|ARBA:ARBA00022486};
Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
ECO:0000256|PIRSR:PIRSR001149-4};
Hemostasis {ECO:0000256|ARBA:ARBA00023084};
Hydrolase {ECO:0000256|RuleBase:RU363034};
Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
ProRule:PRU00121}; Protease {ECO:0000256|RuleBase:RU363034};
Reference proteome {ECO:0000313|Proteomes:UP000314981};
Serine protease {ECO:0000256|RuleBase:RU363034};
Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
SIGNAL 1..24
/evidence="ECO:0000256|SAM:SignalP"
CHAIN 25..631
/note="Activation peptide fragment 1"
/evidence="ECO:0000256|SAM:SignalP"
/id="PRO_5021327691"
DOMAIN 44..90
/note="Gla"
/evidence="ECO:0000259|PROSITE:PS50998"
DOMAIN 108..187
/note="Kringle"
/evidence="ECO:0000259|PROSITE:PS50070"
DOMAIN 213..292
/note="Kringle"
/evidence="ECO:0000259|PROSITE:PS50070"
DOMAIN 367..627
/note="Peptidase S1"
/evidence="ECO:0000259|PROSITE:PS50240"
ACT_SITE 409
/note="Charge relay system"
/evidence="ECO:0000256|PIRSR:PIRSR001149-1"
ACT_SITE 471
/note="Charge relay system"
/evidence="ECO:0000256|PIRSR:PIRSR001149-1"
ACT_SITE 577
/note="Charge relay system"
/evidence="ECO:0000256|PIRSR:PIRSR001149-1"
SITE 199..200
/note="Cleavage; by thrombin"
/evidence="ECO:0000256|PIRSR:PIRSR001149-2"
SITE 330..331
/note="Cleavage; by factor Xa"
/evidence="ECO:0000256|PIRSR:PIRSR001149-2"
SITE 366..367
/note="Cleavage; by factor Xa"
/evidence="ECO:0000256|PIRSR:PIRSR001149-2"
DISULFID 61..66
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 91..104
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 109..187
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 130..170
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 158..182
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 214..292
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 235..275
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 263..287
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 339..491
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 394..410
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 545..559
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
DISULFID 573..603
/evidence="ECO:0000256|PIRSR:PIRSR001149-4"
SEQUENCE 631 AA; 71047 MW; E5E827FD4EC938FF CRC64;
MARVRGPRLP GCLALAALFS LVHSQHVFLA HQQASSLLQR ARRANKGFLE EVRKGNLERE
CLEEPCSREE AFEALESLSA TDAFWAKYTA CESARNPREK LNECLEGNCA EGVGMNYRGN
VSVTRSGIEC QLWRSRYPHK PEINSTTHPG ADLRENFCRN PDGSITGPWC YTTSPTLRRE
ECSVPVCGQD RVTVEVIPRS GGSTTSQSPL LETCVPDRGR EYRGRLAVTT SGSRCLAWSS
EQAKALSKDQ DFNPAVPLAE NFCRNPDGDE EGAWCYVADQ PGDFEYCDLN YCEEPVDGDL
GDRLGEDPDP DAAIEGRTSE DHFQPFFNEK TFGAGEADCG LRPLFEKKQV QDQTEKELFE
SYIEGRIVEG QDAEVGLSPW QVMLFRKSPQ ELLCGASLIS DRWVLTAAHC LLYPPWDKNF
TVDDLLVRIG KHSRTRCGGA PRYERKVEKI SMLDKIYIHP RYNWKENLDR DIALLKLKRP
IELSDYIHPV CLPDKQTAAK LLHAGFKGRV TGWGNRRETW TTSVAEVQPS VLQVVNLPLV
ERPVCKASTR IRITDNMFCA GYKPGEGKRG DACEGDSGGP FVMKSPYNNR WYQMGIVSWG
EGCDRDGKYG FYTHVFRLKK WIQKVIDRLG S


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Related Genes :
[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]
[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]
[] 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] 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] 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]
[PLG] Plasminogen (EC 3.4.21.7) [Cleaved into: Plasmin heavy chain A; Activation peptide; Angiostatin; Plasmin heavy chain A, short form; Plasmin light chain B]
[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]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII 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]
[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)]
[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]
[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]
[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]
[F2 ORTSPA_R05543] Activation peptide fragment 1 (EC 3.4.21.5) (Activation peptide fragment 2) (Coagulation factor II) (Prothrombin) (Thrombin heavy chain) (Thrombin light chain) (Fragment)
[F2 EULNIG_R03319] Activation peptide fragment 1 (EC 3.4.21.5) (Activation peptide fragment 2) (Coagulation factor II) (Prothrombin) (Thrombin heavy chain) (Thrombin light chain) (Fragment)
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B heavy chain]
[F2RL1 GPR11 PAR2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1) [Cleaved into: Proteinase-activated receptor 2, alternate cleaved 1; Proteinase-activated receptor 2, alternate cleaved 2]
[F13A1 F13A] Coagulation factor XIII A chain (Coagulation factor XIIIa) (EC 2.3.2.13) (Protein-glutamine gamma-glutamyltransferase A chain) (Transglutaminase A 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]
[F2RL3 PAR4] Proteinase-activated receptor 4 (PAR-4) (Coagulation factor II receptor-like 3) (Thrombin receptor-like 3)
[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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F2rl1 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (Thrombin receptor-like 1)
[F2rl1 Gpcr11 Gpr11 Par2] Proteinase-activated receptor 2 (PAR-2) (Coagulation factor II receptor-like 1) (G-protein coupled receptor 11) (Thrombin receptor-like 1)

Bibliography :
[10373475] Role of regulatory exosite I in binding of thrombin to human factor V, factor Va, factor Va subunits, and activation fragments.
[2268268] Activation of factor V during intrinsic and extrinsic coagulation. Inhibition by heparin, hirudin and D-Phe-Pro-Arg-Ch2Cl.