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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_MOUSE               Reviewed;         446 AA.
P70375; Q61109;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-MAR-2018, entry version 183.
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; Synonyms=Cf7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8701412;
Idusogie E., Rosen E., Geng J.P., Carmeliet P., Collen D.,
Castellino F.J.;
"Characterization of a cDNA encoding murine coagulation factor VII.";
Thromb. Haemost. 75:481-487(1996).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=8972017;
Idusogie E., Rosen E.D., Carmeliet P., Collen D., Castellino F.J.;
"Nucleotide structure and characterization of the murine blood
coagulation factor VII gene.";
Thromb. Haemost. 76:957-964(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INDUCTION.
PubMed=18316400; DOI=10.1128/MCB.01931-07;
Bertolucci C., Cavallari N., Colognesi I., Aguzzi J., Chen Z.,
Caruso P., Foa A., Tosini G., Bernardi F., Pinotti M.;
"Evidence for an overlapping role of CLOCK and NPAS2 transcription
factors in liver circadian oscillators.";
Mol. Cell. Biol. 28:3070-3075(2008).
-!- 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: Selective cleavage of Arg-|-Ile bond in factor
X to form factor Xa.
-!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by
a disulfide bond. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma and liver.
-!- INDUCTION: Expression in the liver and plasma oscillates in a
circadian manner. {ECO:0000269|PubMed:18316400}.
-!- 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: Can be either O-glucosylated or O-xylosylated at Ser-93 by
POGLUT1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; U44795; AAC52570.1; -; mRNA.
EMBL; U66079; AAC33796.1; -; Genomic_DNA.
EMBL; BC061149; AAH61149.1; -; mRNA.
CCDS; CCDS22104.1; -.
RefSeq; NP_034302.2; NM_010172.4.
UniGene; Mm.4827; -.
PDB; 5KXH; X-ray; 1.33 A; B=87-126.
PDB; 5KY2; X-ray; 1.47 A; B=87-126.
PDB; 5KY3; X-ray; 1.53 A; B=87-126.
PDBsum; 5KXH; -.
PDBsum; 5KY2; -.
PDBsum; 5KY3; -.
ProteinModelPortal; P70375; -.
SMR; P70375; -.
STRING; 10090.ENSMUSP00000033820; -.
PhosphoSitePlus; P70375; -.
SwissPalm; P70375; -.
PaxDb; P70375; -.
PeptideAtlas; P70375; -.
PRIDE; P70375; -.
Ensembl; ENSMUST00000033820; ENSMUSP00000033820; ENSMUSG00000031443.
GeneID; 14068; -.
KEGG; mmu:14068; -.
UCSC; uc009kwr.2; mouse.
CTD; 2155; -.
MGI; MGI:109325; F7.
eggNOG; ENOG410IIMB; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; P70375; -.
KO; K01320; -.
OMA; CEQYCSD; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P70375; -.
TreeFam; TF327329; -.
Reactome; R-MMU-1368110; Bmal1:Clock,Npas2 activates circadian gene expression.
Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
PRO; PR:P70375; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031443; -.
CleanEx; MM_F7; -.
ExpressionAtlas; P70375; baseline and differential.
Genevisible; P70375; MM.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:1905286; C:serine-type peptidase complex; ISO:MGI.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; IMP:MGI.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:MGI.
GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0016485; P:protein processing; ISO:MGI.
GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEA:Ensembl.
GO; GO:1905217; P:response to astaxanthin; IEA:Ensembl.
GO; GO:0010037; P:response to carbon dioxide; IEA:Ensembl.
GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0033595; P:response to genistein; IEA:Ensembl.
GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:1904400; P:response to Thyroid stimulating hormone; IEA:Ensembl.
GO; GO:1905225; P:response to thyrotropin-releasing hormone; IEA:Ensembl.
GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
GO; GO:0032571; P:response to vitamin K; IEA:Ensembl.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
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; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR44064:SF1; PTHR44064:SF1; 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; 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.
1: Evidence at protein level;
3D-structure; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 24 {ECO:0000255}.
PROPEP 25 41 {ECO:0000255}.
/FTId=PRO_0000027732.
CHAIN 42 193 Factor VII light chain.
/FTId=PRO_0000027733.
CHAIN 194 446 Factor VII heavy chain.
/FTId=PRO_0000027734.
DOMAIN 42 86 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 87 123 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 128 169 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 194 433 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 234 234 Charge relay system. {ECO:0000250}.
ACT_SITE 283 283 Charge relay system. {ECO:0000250}.
ACT_SITE 385 385 Charge relay system. {ECO:0000250}.
BINDING 379 379 Substrate. {ECO:0000250}.
SITE 193 194 Cleavage; by factor Xa, factor XIIa,
factor IXa, or thrombin. {ECO:0000250}.
MOD_RES 47 47 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 48 48 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 55 55 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 57 57 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 60 60 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 61 61 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 66 66 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 67 67 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 70 70 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 76 76 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 104 104 (3R)-3-hydroxyaspartate. {ECO:0000250}.
CARBOHYD 93 93 O-linked (Glc...) serine; alternate.
{ECO:0000250}.
CARBOHYD 93 93 O-linked (Xyl...) serine; alternate.
{ECO:0000250}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 63 {ECO:0000250}.
DISULFID 91 102 {ECO:0000250}.
DISULFID 96 111 {ECO:0000250}.
DISULFID 113 122 {ECO:0000250}.
DISULFID 132 143 {ECO:0000250}.
DISULFID 139 153 {ECO:0000250}.
DISULFID 155 168 {ECO:0000250}.
DISULFID 176 303 {ECO:0000250}.
DISULFID 200 205 {ECO:0000250}.
DISULFID 219 235 {ECO:0000250}.
DISULFID 351 370 {ECO:0000250}.
DISULFID 381 409 {ECO:0000250}.
CONFLICT 99 99 G -> V (in Ref. 2; AAC52570).
{ECO:0000305}.
HELIX 91 93 {ECO:0000244|PDB:5KXH}.
STRAND 101 105 {ECO:0000244|PDB:5KXH}.
STRAND 108 112 {ECO:0000244|PDB:5KXH}.
STRAND 117 119 {ECO:0000244|PDB:5KXH}.
SEQUENCE 446 AA; 50276 MW; 2512E44A45CBC96E CRC64;
MVPQAHGLLL LCFLLQLQGP LGTAVFITQE EAHGVLHRQR RANSLLEELW PGSLERECNE
EQCSFEEARE IFKSPERTKQ FWIVYSDGDQ CASNPCQNGG TCQDHLKSYV CFCLLDFEGR
NCEKSKNEQL ICANENGDCD QYCRDHVGTK RTCSCHEDYT LQPDEVSCKP KVEYPCGRIP
VVEKRNSSSR QGRIVGGNVC PKGECPWQAV LKINGLLLCG AVLLDARWIV TAAHCFDNIR
YWGNITVVMG EHDFSEKDGD EQVRRVTQVI MPDKYIRGKI NHDIALLRLH RPVTFTDYVV
PLCLPEKSFS ENTLARIRFS RVSGWGQLLD RGATALELMS IEVPRLMTQD CLEHAKHSSN
TPKITENMFC AGYMDGTKDA CKGDSGGPHA THYHGTWYLT GVVSWGEGCA AIGHIGVYTR
VSQYIDWLVR HMDSKLQVGV FRLPLL


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