ID FA7_PANTR Reviewed; 466 AA.
AC Q2F9P2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=Coagulation factor VII;
DE EC=3.4.21.21;
DE AltName: Full=Serum prothrombin conversion accelerator;
DE Contains:
DE RecName: Full=Factor VII light chain;
DE Contains:
DE RecName: Full=Factor VII heavy chain;
DE Flags: Precursor;
GN Name=F7;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16292673; DOI=10.1007/s00439-005-0045-5;
RA Sabater-Lleal M., Soria J.M., Bertranpetit J., Almasy L., Blangero J.,
RA Fontcuberta J., Calafell F.;
RT "Human F7 sequence is split into three deep clades that are related to FVII
RT plasma levels.";
RL Hum. Genet. 118:741-751(2006).
CC -!- FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine
CC protease that circulates in the blood in a zymogen form. Factor VII is
CC converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or
CC thrombin by minor proteolysis. In the presence of tissue factor and
CC calcium ions, factor VIIa then converts factor X to factor Xa by
CC limited proteolysis. Factor VIIa will also convert factor IX to factor
CC IXa in the presence of tissue factor and calcium (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC factor Xa.; EC=3.4.21.21;
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by a
CC disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC residues allows the modified protein to bind calcium. {ECO:0000250}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- PTM: O-glycosylated. O-fucosylated by POFUT1 on a conserved serine or
CC threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of
CC EGF domains, where C2 and C3 are the second and third conserved
CC cysteines. {ECO:0000250}.
CC -!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-112 by
CC POGLUT1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; DQ142914; ABD17894.1; -; Genomic_DNA.
DR EMBL; DQ142915; ABD17895.1; -; Genomic_DNA.
DR STRING; 9598.ENSPTRP00000072813; -.
DR MEROPS; S01.215; -.
DR GlyCosmos; Q2F9P2; 4 sites, No reported glycans.
DR PaxDb; 9598-ENSPTRP00000010284; -.
DR eggNOG; ENOG502QRGI; Eukaryota.
DR InParanoid; Q2F9P2; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProt.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF26; COAGULATION FACTOR VII; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..60
FT /evidence="ECO:0000250"
FT /id="PRO_0000235182"
FT CHAIN 61..212
FT /note="Factor VII light chain"
FT /id="PRO_0000235183"
FT CHAIN 213..466
FT /note="Factor VII heavy chain"
FT /id="PRO_0000235184"
FT DOMAIN 61..105
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 106..142
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 147..188
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 213..452
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 253
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 113
FT /note="Important for S-112 for O-xylosylation"
FT SITE 212..213
FT /note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
FT thrombin"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 74
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 76
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 79
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 80
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 85
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 86
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 89
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 95
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 123
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="O-linked (Glc...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08709"
FT CARBOHYD 112
FT /note="O-linked (Xyl...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08709"
FT CARBOHYD 120
FT /note="O-linked (Fuc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..82
FT /evidence="ECO:0000250"
FT DISULFID 110..121
FT /evidence="ECO:0000250"
FT DISULFID 115..130
FT /evidence="ECO:0000250"
FT DISULFID 132..141
FT /evidence="ECO:0000250"
FT DISULFID 151..162
FT /evidence="ECO:0000250"
FT DISULFID 158..172
FT /evidence="ECO:0000250"
FT DISULFID 174..187
FT /evidence="ECO:0000250"
FT DISULFID 195..322
FT /evidence="ECO:0000250"
FT DISULFID 219..224
FT /evidence="ECO:0000250"
FT DISULFID 238..254
FT /evidence="ECO:0000250"
FT DISULFID 370..389
FT /evidence="ECO:0000250"
FT DISULFID 400..428
FT /evidence="ECO:0000250"
SQ 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
//
