FA7_MOUSE
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 03-AUG-2022, entry version 208.
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 GlyGen; P70375; 3 sites.
DR PhosphoSitePlus; P70375; -.
DR SwissPalm; P70375; -.
DR CPTAC; non-CPTAC-3914; -.
DR PaxDb; P70375; -.
DR PeptideAtlas; P70375; -.
DR PRIDE; P70375; -.
DR ProteomicsDB; 271849; -.
DR Antibodypedia; 11679; 671 antibodies from 37 providers.
DR DNASU; 14068; -.
DR Ensembl; ENSMUST00000033820; ENSMUSP00000033820; ENSMUSG00000031443.
DR GeneID; 14068; -.
DR KEGG; mmu:14068; -.
DR UCSC; uc009kwr.2; mouse.
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; DDQFQDY; -.
DR OrthoDB; 1314811at2759; -.
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 74 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 34 other tissues.
DR ExpressionAtlas; P70375; baseline and differential.
DR Genevisible; P70375; MM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; 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; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0002543; P:activation of blood coagulation via clotting cascade; IC:ComplexPortal.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0007598; P:blood coagulation, extrinsic pathway; IC:ComplexPortal.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IC:ComplexPortal.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IC:ComplexPortal.
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:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEA:Ensembl.
DR GO; GO:0061476; P:response to anticoagulant; ISO:MGI.
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 GO; GO:0009611; P:response to wounding; IC:ComplexPortal.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
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; 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 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
