ID   FA7_MOUSE               Reviewed;         446 AA.
AC   P70375; Q61109;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 217.
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; Synonyms=Cf7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8701412;
RA   Idusogie E., Rosen E., Geng J.P., Carmeliet P., Collen D., Castellino F.J.;
RT   "Characterization of a cDNA encoding murine coagulation factor VII.";
RL   Thromb. Haemost. 75:481-487(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8972017;
RA   Idusogie E., Rosen E.D., Carmeliet P., Collen D., Castellino F.J.;
RT   "Nucleotide structure and characterization of the murine blood coagulation
RT   factor VII gene.";
RL   Thromb. Haemost. 76:957-964(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INDUCTION.
RX   PubMed=18316400; DOI=10.1128/mcb.01931-07;
RA   Bertolucci C., Cavallari N., Colognesi I., Aguzzi J., Chen Z., Caruso P.,
RA   Foa A., Tosini G., Bernardi F., Pinotti M.;
RT   "Evidence for an overlapping role of CLOCK and NPAS2 transcription factors
RT   in liver circadian oscillators.";
RL   Mol. Cell. Biol. 28:3070-3075(2008).
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.
CC   -!- TISSUE SPECIFICITY: Plasma and liver.
CC   -!- INDUCTION: Expression in the liver and plasma oscillates in a circadian
CC       manner. {ECO:0000269|PubMed:18316400}.
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: Can be either O-glucosylated or O-xylosylated at Ser-93 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; U44795; AAC52570.1; -; mRNA.
DR   EMBL; U66079; AAC33796.1; -; Genomic_DNA.
DR   EMBL; BC061149; AAH61149.1; -; mRNA.
DR   CCDS; CCDS22104.1; -.
DR   RefSeq; NP_034302.2; NM_010172.4.
DR   PDB; 5KXH; X-ray; 1.33 A; B=87-126.
DR   PDB; 5KY2; X-ray; 1.47 A; B=87-126.
DR   PDB; 5KY3; X-ray; 1.53 A; B=87-126.
DR   PDBsum; 5KXH; -.
DR   PDBsum; 5KY2; -.
DR   PDBsum; 5KY3; -.
DR   AlphaFoldDB; P70375; -.
DR   SMR; P70375; -.
DR   BioGRID; 199575; 8.
DR   ComplexPortal; CPX-279; Coagulation factor VIIa - tissue factor complex.
DR   STRING; 10090.ENSMUSP00000033820; -.
DR   GlyCosmos; P70375; 3 sites, No reported glycans.
DR   GlyGen; P70375; 3 sites.
DR   PhosphoSitePlus; P70375; -.
DR   SwissPalm; P70375; -.
DR   CPTAC; non-CPTAC-3914; -.
DR   PaxDb; 10090-ENSMUSP00000033820; -.
DR   PeptideAtlas; P70375; -.
DR   ProteomicsDB; 271849; -.
DR   Antibodypedia; 11679; 736 antibodies from 37 providers.
DR   DNASU; 14068; -.
DR   Ensembl; ENSMUST00000033820.4; ENSMUSP00000033820.4; ENSMUSG00000031443.8.
DR   GeneID; 14068; -.
DR   KEGG; mmu:14068; -.
DR   UCSC; uc009kwr.2; mouse.
DR   AGR; MGI:109325; -.
DR   CTD; 2155; -.
DR   MGI; MGI:109325; F7.
DR   VEuPathDB; HostDB:ENSMUSG00000031443; -.
DR   eggNOG; ENOG502QRGI; Eukaryota.
DR   GeneTree; ENSGT00940000154474; -.
DR   HOGENOM; CLU_006842_19_5_1; -.
DR   InParanoid; P70375; -.
DR   OMA; QGRNCET; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; P70375; -.
DR   TreeFam; TF327329; -.
DR   Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   BioGRID-ORCS; 14068; 0 hits in 79 CRISPR screens.
DR   PRO; PR:P70375; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P70375; Protein.
DR   Bgee; ENSMUSG00000031443; Expressed in left lobe of liver and 35 other cell types or tissues.
DR   ExpressionAtlas; P70375; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:1905286; C:serine-type peptidase complex; ISO:MGI.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:MGI.
DR   GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
DR   GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR   GO; GO:0016485; P:protein processing; ISO:MGI.
DR   GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEA:Ensembl.
DR   GO; GO:1905217; P:response to astaxanthin; ISO:MGI.
DR   GO; GO:0010037; P:response to carbon dioxide; IEA:Ensembl.
DR   GO; GO:0070723; P:response to cholesterol; ISO:MGI.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0033595; P:response to genistein; IEA:Ensembl.
DR   GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
DR   GO; GO:1904400; P:response to Thyroid stimulating hormone; IEA:Ensembl.
DR   GO; GO:1905225; P:response to thyrotropin-releasing hormone; IEA:Ensembl.
DR   GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
DR   GO; GO:0032571; P:response to vitamin K; IEA:Ensembl.
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; SSF57196; EGF/Laminin; 2.
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; 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.
DR   Genevisible; P70375; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW   Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..41
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027732"
FT   CHAIN           42..193
FT                   /note="Factor VII light chain"
FT                   /id="PRO_0000027733"
FT   CHAIN           194..446
FT                   /note="Factor VII heavy chain"
FT                   /id="PRO_0000027734"
FT   DOMAIN          42..86
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          87..123
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          128..169
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          194..433
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        234
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        283
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        385
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            193..194
FT                   /note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
FT                   thrombin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         47
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         48
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         55
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         57
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         60
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         61
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
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         70
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         104
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        93
FT                   /note="O-linked (Glc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08709"
FT   CARBOHYD        93
FT                   /note="O-linked (Xyl...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08709"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        113..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..143
FT                   /evidence="ECO:0000250"
FT   DISULFID        139..153
FT                   /evidence="ECO:0000250"
FT   DISULFID        155..168
FT                   /evidence="ECO:0000250"
FT   DISULFID        176..303
FT                   /evidence="ECO:0000250"
FT   DISULFID        200..205
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..235
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..370
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..409
FT                   /evidence="ECO:0000250"
FT   CONFLICT        99
FT                   /note="G -> V (in Ref. 2; AAC52570)"
FT                   /evidence="ECO:0000305"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:5KXH"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:5KXH"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:5KXH"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:5KXH"
SQ   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
//