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Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]

 FA7_PANTR               Reviewed;         466 AA.
Q2F9P2;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 1.
02-DEC-2020, entry version 88.
RecName: Full=Coagulation factor VII;
EC=3.4.21.21;
AltName: Full=Serum prothrombin conversion accelerator;
Contains:
RecName: Full=Factor VII light chain;
Contains:
RecName: Full=Factor VII heavy chain;
Flags: Precursor;
Name=F7;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16292673; DOI=10.1007/s00439-005-0045-5;
Sabater-Lleal M., Soria J.M., Bertranpetit J., Almasy L., Blangero J.,
Fontcuberta J., Calafell F.;
"Human F7 sequence is split into three deep clades that are related to FVII
plasma levels.";
Hum. Genet. 118:741-751(2006).
-!- FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine
protease that circulates in the blood in a zymogen form. Factor VII is
converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or
thrombin by minor proteolysis. In the presence of tissue factor and
calcium ions, factor VIIa then converts factor X to factor Xa by
limited proteolysis. Factor VIIa will also convert factor IX to factor
IXa in the presence of tissue factor and calcium (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
factor Xa.; EC=3.4.21.21;
-!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by a
disulfide bond. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
residues allows the modified protein to bind calcium. {ECO:0000250}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
-!- PTM: O-glycosylated. O-fucosylated by POFUT1 on a conserved serine or
threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of
EGF domains, where C2 and C3 are the second and third conserved
cysteines. {ECO:0000250}.
-!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-112 by
POGLUT1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
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EMBL; DQ142914; ABD17894.1; -; Genomic_DNA.
EMBL; DQ142915; ABD17895.1; -; Genomic_DNA.
STRING; 9598.ENSPTRP00000010284; -.
MEROPS; S01.215; -.
PaxDb; Q2F9P2; -.
eggNOG; ENOG502QRGI; Eukaryota.
InParanoid; Q2F9P2; -.
Proteomes; UP000002277; Unplaced.
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.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; 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; IPR033190; F7.
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.
PANTHER; PTHR24278:SF26; PTHR24278:SF26; 1.
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.
3: Inferred from homology;
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..60
/evidence="ECO:0000250"
/id="PRO_0000235182"
CHAIN 61..212
/note="Factor VII light chain"
/id="PRO_0000235183"
CHAIN 213..466
/note="Factor VII heavy chain"
/id="PRO_0000235184"
DOMAIN 61..105
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 106..142
/note="EGF-like 1; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 147..188
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 213..452
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
ACT_SITE 253
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 302
/note="Charge relay system"
/evidence="ECO:0000250"
ACT_SITE 404
/note="Charge relay system"
/evidence="ECO:0000250"
BINDING 398
/note="Substrate"
/evidence="ECO:0000250"
SITE 113
/note="Important for S-112 for O-xylosylation"
SITE 212..213
/note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
thrombin"
/evidence="ECO:0000250"
MOD_RES 66
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 67
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 74
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 76
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 79
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 80
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 85
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 86
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 89
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 95
/note="4-carboxyglutamate"
/evidence="ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463"
MOD_RES 123
/note="(3R)-3-hydroxyaspartate"
/evidence="ECO:0000250"
CARBOHYD 112
/note="O-linked (Glc...) serine; alternate"
/evidence="ECO:0000250|UniProtKB:P08709"
CARBOHYD 112
/note="O-linked (Xyl...) serine; alternate"
/evidence="ECO:0000250|UniProtKB:P08709"
CARBOHYD 120
/note="O-linked (Fuc) serine"
/evidence="ECO:0000250"
CARBOHYD 205
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 382
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 77..82
/evidence="ECO:0000250"
DISULFID 110..121
/evidence="ECO:0000250"
DISULFID 115..130
/evidence="ECO:0000250"
DISULFID 132..141
/evidence="ECO:0000250"
DISULFID 151..162
/evidence="ECO:0000250"
DISULFID 158..172
/evidence="ECO:0000250"
DISULFID 174..187
/evidence="ECO:0000250"
DISULFID 195..322
/evidence="ECO:0000250"
DISULFID 219..224
/evidence="ECO:0000250"
DISULFID 238..254
/evidence="ECO:0000250"
DISULFID 370..389
/evidence="ECO:0000250"
DISULFID 400..428
/evidence="ECO:0000250"
SEQUENCE 466 AA; 51641 MW; 8F5D5B3B22B58C36 CRC64;
MVSQALRLLC LLLGLQGCLA AGGVAEASGG ETRDXXWKPG PHRVFITQEE AHGVLHRRRR
ANAFLEELRP GSLERECKEE QCSFEEAREI FKDLERTKLF WISYSDGDQC ASSPCQNGGS
CKDQLQSYIC FCLPAFEGRN CETYKDDQLI CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL
LADGVSCTPT VEYPCGKIPI LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG
TLINTIWVVS AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYIPGTTN
HDIALLRLHQ PVVLTDHVVP LCLPERAFSE RTLAFVRFSL VSGWGQLLDR GATALELMVL
NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC KGDSGGPHAT HYRGTWYLTG
IVSWGQGCAS VGHFGVYTRV SQYIEWLQKL MRSEPRPGVL LRAPFP


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Related Genes :
[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]
[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]
[F7] 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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [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]
[] 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]
[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)]
[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]
[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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator)
[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]
[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]
[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]
[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]
[] Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B 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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[] 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]

Bibliography :
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