FA7_BOVIN
ID FA7_BOVIN Reviewed; 447 AA.
AC P22457; A6H6Y5; Q58DL3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 191.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 41-447, AND GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47;
RP GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-74 AND GLU-75.
RX PubMed=3049594; DOI=10.1016/s0021-9258(18)68119-0;
RA Takeya H., Kawabata S., Nakagawa K., Yamamichi Y., Miyata T., Iwanaga S.;
RT "Bovine factor VII. Its purification and complete amino acid sequence.";
RL J. Biol. Chem. 263:14868-14877(1988).
RN [4]
RP GLYCOSYLATION AT SER-92, AND STRUCTURE OF CARBOHYDRATE ON SER-92.
RX PubMed=3149637; DOI=10.1093/oxfordjournals.jbchem.a122571;
RA Hase S., Kawabata S., Nishimura H., Takeya H., Sueyoshi T., Miyata T.,
RA Iwanaga S., Takao T., Shimonishi Y., Ikenaka T.;
RT "A new trisaccharide sugar chain linked to a serine residue in bovine blood
RT coagulation factors VII and IX.";
RL J. Biochem. 104:867-868(1988).
RN [5]
RP GLYCOSYLATION AT SER-92, AND STRUCTURE OF CARBOHYDRATE ON SER-92.
RX PubMed=2129367; DOI=10.1007/978-1-4615-3806-6_12;
RA Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
RT "A new trisaccharide sugar chain linked to a serine residue in the first
RT EGF-like domain of clotting factors VII and IX and protein Z.";
RL Adv. Exp. Med. Biol. 281:121-131(1990).
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.
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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC residues allows the modified protein to bind calcium.
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-92 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; BT021584; AAX46431.1; -; mRNA.
DR EMBL; BC146045; AAI46046.1; -; mRNA.
DR PIR; A31979; KFBO7.
DR RefSeq; NP_001029978.1; NM_001034806.1.
DR AlphaFoldDB; P22457; -.
DR SMR; P22457; -.
DR ELM; P22457; -.
DR STRING; 9913.ENSBTAP00000009746; -.
DR MEROPS; S01.215; -.
DR iPTMnet; P22457; -.
DR PaxDb; P22457; -.
DR PRIDE; P22457; -.
DR Ensembl; ENSBTAT00000009746; ENSBTAP00000009746; ENSBTAG00000007411.
DR GeneID; 617960; -.
DR KEGG; bta:617960; -.
DR CTD; 2155; -.
DR VEuPathDB; HostDB:ENSBTAG00000007411; -.
DR VGNC; VGNC:28689; F7.
DR eggNOG; ENOG502QRGI; Eukaryota.
DR GeneTree; ENSGT00940000154474; -.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; P22457; -.
DR OMA; DDQFQDY; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF327329; -.
DR Reactome; R-BTA-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-BTA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000007411; Expressed in cortex of kidney and 35 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1905286; C:serine-type peptidase complex; IEA:Ensembl.
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:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 4.10.740.10; -; 1.
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; IPR033190; F7.
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:SF26; PTHR24278:SF26; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
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 1: Evidence at protein level;
KW Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..40
FT /evidence="ECO:0000269|PubMed:3049594"
FT /id="PRO_0000240126"
FT CHAIN 41..192
FT /note="Factor VII light chain"
FT /evidence="ECO:0000269|PubMed:3049594"
FT /id="PRO_0000027727"
FT CHAIN 193..447
FT /note="Factor VII heavy chain"
FT /evidence="ECO:0000269|PubMed:3049594"
FT /id="PRO_0000027728"
FT DOMAIN 41..85
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 86..122
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 127..168
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 193..432
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 384
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 93
FT /note="Important for S-92 for O-xylosylation"
FT /evidence="ECO:0000250"
FT SITE 192..193
FT /note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
FT thrombin"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 74
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3049594"
FT CARBOHYD 92
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:2129367,
FT ECO:0000269|PubMed:3149637"
FT CARBOHYD 92
FT /note="O-linked (Glc...) serine; alternate"
FT /evidence="ECO:0000250, ECO:0000269|PubMed:2129367,
FT ECO:0000269|PubMed:3149637"
FT CARBOHYD 92
FT /note="O-linked (Xyl...) serine; alternate"
FT /evidence="ECO:0000250, ECO:0000269|PubMed:2129367,
FT ECO:0000269|PubMed:3149637"
FT CARBOHYD 100
FT /note="O-linked (Fuc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3049594"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3049594"
FT DISULFID 57..62
FT /evidence="ECO:0000250"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
FT DISULFID 95..110
FT /evidence="ECO:0000250"
FT DISULFID 112..121
FT /evidence="ECO:0000250"
FT DISULFID 131..142
FT /evidence="ECO:0000250"
FT DISULFID 138..152
FT /evidence="ECO:0000250"
FT DISULFID 154..167
FT /evidence="ECO:0000250"
FT DISULFID 175..302
FT /evidence="ECO:0000250"
FT DISULFID 199..204
FT /evidence="ECO:0000250"
FT DISULFID 218..234
FT /evidence="ECO:0000250"
FT DISULFID 350..369
FT /evidence="ECO:0000250"
FT DISULFID 380..408
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 48961 MW; 6FE6CA805E84B871 CRC64;
MLSQAWALAL LCFLLSLWGS LPAVFLPQEQ ALSILHRPRR ANGFLEELLP GSLERECREE
LCSFEEAHEI FRNEERTRQF WVSYNDGDQC ASSPCQNGGS CEDQLRSYIC FCPDGFEGRN
CETDKQSQLI CANDNGGCEQ YCGADPGAGR FCWCHEGYAL QADGVSCAPT VEYPCGKIPV
LEKRNGSKPQ GRIVGGHVCP KGECPWQAML KLNGALLCGG TLVGPAWVVS AAHCFERLRS
RGNLTAVLGE HDLSRVEGPE QERRVAQIIV PKQYVPGQTD HDVALLQLAQ PVALGDHVAP
LCLPDPDFAD QTLAFVRFSA VSGWGQLLER GVTARKLMVV LVPRLLTQDC LQQSRQRPGG
PVVTDNMFCA GYSDGSKDAC KGDSGGPHAT RFRGTWFLTG VVSWGEGCAA AGHFGIYTRV
SRYTAWLRQL MGHPPSRQGF FQVPLLP
