Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]

 FA7_RAT                 Reviewed;         446 AA.
 Q8K3U6;
 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
 01-OCT-2002, sequence version 1.
 23-FEB-2022, entry version 149.
 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;
 Rattus norvegicus (Rat).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
 Murinae; Rattus.
 NCBI_TaxID=10116;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 STRAIN=Sprague-Dawley;
 Murphy K., Ramaker M.;
 "Nucleotide sequence of the cDNA encoding rat coagulation factor VII.";
 Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
 -!- 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:
     Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
       factor Xa.; EC=3.4.21.21;
 -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by a
     disulfide bond. {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
 -!- TISSUE SPECIFICITY: Plasma.
 -!- 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; AF532184; AAM95967.1; -; mRNA.
 RefSeq; NP_690059.1; NM_152846.1.
 SMR; Q8K3U6; -.
 STRING; 10116.ENSRNOP00000038466; -.
 MEROPS; S01.215; -.
 GlyGen; Q8K3U6; 4 sites.
 PaxDb; Q8K3U6; -.
 Ensembl; ENSRNOT00000037806; ENSRNOP00000038466; ENSRNOG00000032737.
 GeneID; 260320; -.
 KEGG; rno:260320; -.
 UCSC; RGD:628678; rat.
 CTD; 2155; -.
 RGD; 628678; F7.
 eggNOG; ENOG502QRGI; Eukaryota.
 GeneTree; ENSGT00940000154474; -.
 HOGENOM; CLU_006842_19_5_1; -.
 InParanoid; Q8K3U6; -.
 OMA; ENFWRTY; -.
 OrthoDB; 1314811at2759; -.
 PhylomeDB; Q8K3U6; -.
 TreeFam; TF327329; -.
 Reactome; R-RNO-140834; Extrinsic Pathway of Fibrin Clot Formation.
 Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
 Reactome; R-RNO-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
 Reactome; R-RNO-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
 PRO; PR:Q8K3U6; -.
 Proteomes; UP000002494; Chromosome 16.
 Bgee; ENSRNOG00000032737; Expressed in liver and 16 other tissues.
 GO; GO:0005615; C:extracellular space; IDA:RGD.
 GO; GO:1905286; C:serine-type peptidase complex; ISO:RGD.
 GO; GO:0031982; C:vesicle; IDA:RGD.
 GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
 GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
 GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
 GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
 GO; GO:0007596; P:blood coagulation; IDA:RGD.
 GO; GO:0007623; P:circadian rhythm; IEP:RGD.
 GO; GO:0030194; P:positive regulation of blood coagulation; IDA:RGD.
 GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:RGD.
 GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISO:RGD.
 GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:RGD.
 GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
 GO; GO:0016485; P:protein processing; ISO:RGD.
 GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEP:RGD.
 GO; GO:0061476; P:response to anticoagulant; IDA:RGD.
 GO; GO:1905217; P:response to astaxanthin; IDA:RGD.
 GO; GO:0010037; P:response to carbon dioxide; IEP:RGD.
 GO; GO:0070723; P:response to cholesterol; IDA:RGD.
 GO; GO:0032355; P:response to estradiol; IEP:RGD.
 GO; GO:0043627; P:response to estrogen; IEP:RGD.
 GO; GO:0033595; P:response to genistein; IEP:RGD.
 GO; GO:0060416; P:response to growth hormone; IEP:RGD.
 GO; GO:0009725; P:response to hormone; IEP:RGD.
 GO; GO:0001666; P:response to hypoxia; IEP:RGD.
 GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
 GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
 GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
 GO; GO:1904400; P:response to Thyroid stimulating hormone; IEP:RGD.
 GO; GO:1905225; P:response to thyrotropin-releasing hormone; IEP:RGD.
 GO; GO:0097068; P:response to thyroxine; IEP:RGD.
 GO; GO:0032571; P:response to vitamin K; IEP:RGD.
 CDD; cd00190; Tryp_SPc; 1.
 Gene3D; 2.40.10.10; -; 2.
 Gene3D; 4.10.740.10; -; 1.
 InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
 InterPro; IPR001881; EGF-like_Ca-bd_dom.
 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; IPR043504; Peptidase_S1_PA_chymotrypsin.
 InterPro; IPR001314; Peptidase_S1A.
 InterPro; IPR001254; Trypsin_dom.
 InterPro; IPR018114; TRYPSIN_HIS.
 InterPro; IPR033116; TRYPSIN_SER.
 PANTHER; PTHR24278:SF26; PTHR24278:SF26; 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.
 2: Evidence at transcript level;
 Blood coagulation; Calcium; Cleavage on pair of basic residues;
 Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
 Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
 Secreted; Serine protease; Signal; Zymogen.
 SIGNAL          1..24
                 /evidence="ECO:0000255"
 PROPEP          25..41
                 /evidence="ECO:0000255"
                 /id="PRO_0000027738"
 CHAIN           42..193
                 /note="Factor VII light chain"
                 /evidence="ECO:0000250"
                 /id="PRO_0000027739"
 CHAIN           194..446
                 /note="Factor VII heavy chain"
                 /evidence="ECO:0000250"
                 /id="PRO_0000027740"
 DOMAIN          42..86
                 /note="Gla"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 DOMAIN          87..123
                 /note="EGF-like 1; calcium-binding"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
 DOMAIN          128..169
                 /note="EGF-like 2"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
 DOMAIN          194..433
                 /note="Peptidase S1"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
 ACT_SITE        234
                 /note="Charge relay system"
                 /evidence="ECO:0000250"
 ACT_SITE        283
                 /note="Charge relay system"
                 /evidence="ECO:0000250"
 ACT_SITE        385
                 /note="Charge relay system"
                 /evidence="ECO:0000250"
 BINDING         379
                 /note="Substrate"
                 /evidence="ECO:0000250"
 SITE            193..194
                 /note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
                 thrombin"
                 /evidence="ECO:0000250"
 MOD_RES         47
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         48
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         55
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         57
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         60
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         61
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         66
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         67
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         70
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         76
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000250|UniProtKB:P22457,
                 ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         104
                 /note="(3R)-3-hydroxyaspartate"
                 /evidence="ECO:0000250"
 CARBOHYD        93
                 /note="O-linked (Glc...) serine; alternate"
                 /evidence="ECO:0000250|UniProtKB:P08709"
 CARBOHYD        93
                 /note="O-linked (Xyl...) serine; alternate"
                 /evidence="ECO:0000250|UniProtKB:P08709"
 CARBOHYD        101
                 /note="O-linked (Fuc) threonine"
                 /evidence="ECO:0000250"
 CARBOHYD        186
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        244
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 DISULFID        58..63
                 /evidence="ECO:0000250"
 DISULFID        91..102
                 /evidence="ECO:0000250"
 DISULFID        96..111
                 /evidence="ECO:0000250"
 DISULFID        113..122
                 /evidence="ECO:0000250"
 DISULFID        132..143
                 /evidence="ECO:0000250"
 DISULFID        139..153
                 /evidence="ECO:0000250"
 DISULFID        155..168
                 /evidence="ECO:0000250"
 DISULFID        176..303
                 /evidence="ECO:0000250"
 DISULFID        200..205
                 /evidence="ECO:0000250"
 DISULFID        219..235
                 /evidence="ECO:0000250"
 DISULFID        351..370
                 /evidence="ECO:0000250"
 DISULFID        381..409
                 /evidence="ECO:0000250"
 SEQUENCE   446 AA;  50399 MW;  292985EBF119C0AA CRC64;
 MVPQTHGLLL LYFLLQLQGP LGAVVFITQE EAHGVLHRQR RANSLLEELW SSSLERECNE
 ERCSFEEARE IFKSPERTKQ FWTIYSDGDQ CASNPCQNGG TCQDHLKSYV CFCPLDFEGR
 NCEKNKNEQL ICANENGDCD QYCRDHVGTK RTCSCHEDYV LQPDEVSCKP KVEYPCGRIP
 VVEKRNFSRP QGRIVGGYVC PKGECPWQAV LKFNEALLCG AVLLDTRWIV TAAHCFDKFG
 KLVNITVVLG EHDFSEKEGT EQVRLVEQVI MPNKYTRGRT DHDIALVRLH RPVTFTDYVV
 PLCLPERAFS ENTLASIRFS RVSGWGQLLD RGATALELMV IEVPRLMTQD CLEHAKHSAN
 TPRITENMFC AGYMDGTKDA CKGDSGGPHA THYHGTWYLT GVVSWGEGCA AIGHIGVYTR
 VSQYIDWLVK YMDSKLRVGI SRVSLL

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