FA7_RAT
ID FA7_RAT Reviewed; 446 AA.
AC Q8K3U6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Murphy K., Ramaker M.;
RT "Nucleotide sequence of the cDNA encoding rat coagulation factor VII.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma.
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; AF532184; AAM95967.1; -; mRNA.
DR RefSeq; NP_690059.1; NM_152846.1.
DR AlphaFoldDB; Q8K3U6; -.
DR SMR; Q8K3U6; -.
DR STRING; 10116.ENSRNOP00000038466; -.
DR MEROPS; S01.215; -.
DR GlyGen; Q8K3U6; 4 sites.
DR PaxDb; Q8K3U6; -.
DR Ensembl; ENSRNOT00000037806; ENSRNOP00000038466; ENSRNOG00000032737.
DR GeneID; 260320; -.
DR KEGG; rno:260320; -.
DR UCSC; RGD:628678; rat.
DR CTD; 2155; -.
DR RGD; 628678; F7.
DR eggNOG; ENOG502QRGI; Eukaryota.
DR GeneTree; ENSGT00940000154474; -.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; Q8K3U6; -.
DR OMA; DDQFQDY; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q8K3U6; -.
DR TreeFam; TF327329; -.
DR Reactome; R-RNO-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-RNO-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-RNO-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR PRO; PR:Q8K3U6; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000032737; Expressed in liver and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
DR GO; GO:1905286; C:serine-type peptidase complex; ISO:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:RGD.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:RGD.
DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEP:RGD.
DR GO; GO:0061476; P:response to anticoagulant; IDA:RGD.
DR GO; GO:1905217; P:response to astaxanthin; IDA:RGD.
DR GO; GO:0010037; P:response to carbon dioxide; IEP:RGD.
DR GO; GO:0070723; P:response to cholesterol; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0033595; P:response to genistein; IEP:RGD.
DR GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR GO; GO:1904400; P:response to Thyroid stimulating hormone; IEP:RGD.
DR GO; GO:1905225; P:response to thyrotropin-releasing hormone; IEP:RGD.
DR GO; GO:0097068; P:response to thyroxine; IEP:RGD.
DR GO; GO:0032571; P:response to vitamin K; IEP:RGD.
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 2: Evidence at transcript level;
KW Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..41
FT /evidence="ECO:0000255"
FT /id="PRO_0000027738"
FT CHAIN 42..193
FT /note="Factor VII light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027739"
FT CHAIN 194..446
FT /note="Factor VII heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027740"
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 101
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000250"
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"
SQ 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
