(data stored in ACNUC19913 zone)

SWISSPROT: 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   07-JUN-2017, entry version 127.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   VII.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Initiates the extrinsic pathway of blood coagulation.
CC       Serine protease that circulates in the blood in a zymogen form.
CC       Factor VII is converted to factor VIIa by factor Xa, factor XIIa,
CC       factor IXa, or thrombin by minor proteolysis. In the presence of
CC       tissue factor and calcium ions, factor VIIa then converts factor X
CC       to factor Xa by limited proteolysis. Factor VIIa will also convert
CC       factor IX to factor IXa in the presence of tissue factor and
CC       calcium (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor
CC       X to form factor Xa.
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by
CC       a disulfide bond. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC       {ECO:0000250}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AF532184; AAM95967.1; -; mRNA.
DR   RefSeq; NP_690059.1; NM_152846.1.
DR   UniGene; Rn.86416; -.
DR   ProteinModelPortal; Q8K3U6; -.
DR   SMR; Q8K3U6; -.
DR   STRING; 10116.ENSRNOP00000038466; -.
DR   MEROPS; S01.215; -.
DR   PaxDb; Q8K3U6; -.
DR   PRIDE; 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; ENOG410IIMB; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00760000118890; -.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; Q8K3U6; -.
DR   KO; K01320; -.
DR   OMA; CEQYCSD; -.
DR   OrthoDB; EOG091G0AH5; -.
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; -.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:1905286; C:serine-type peptidase complex; IEA:Ensembl.
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:0001948; F:glycoprotein binding; IEA:Ensembl.
DR   GO; GO:0005102; F:receptor binding; IPI:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
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; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24256:SF375; PTHR24256:SF375; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 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;
DR   PRODOM; Q8K3U6.
DR   SWISS-2DPAGE; Q8K3U6.
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; 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       {ECO:0000255}.
FT   PROPEP       25     41       {ECO:0000255}.
FT                                /FTId=PRO_0000027738.
FT   CHAIN        42    193       Factor VII light chain. {ECO:0000250}.
FT                                /FTId=PRO_0000027739.
FT   CHAIN       194    446       Factor VII heavy chain. {ECO:0000250}.
FT                                /FTId=PRO_0000027740.
FT   DOMAIN       42     86       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       87    123       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      128    169       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      194    433       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    234    234       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    283    283       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    385    385       Charge relay system. {ECO:0000250}.
FT   BINDING     379    379       Substrate. {ECO:0000250}.
FT   SITE        193    194       Cleavage; by factor Xa, factor XIIa,
FT                                factor IXa, or thrombin. {ECO:0000250}.
FT   MOD_RES      47     47       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      48     48       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      55     55       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      57     57       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      61     61       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      67     67       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      70     70       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      76     76       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P22457,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     104    104       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD     93     93       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000250}.
FT   CARBOHYD     93     93       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000250}.
FT   CARBOHYD    101    101       O-linked (Fuc) threonine. {ECO:0000250}.
FT   CARBOHYD    186    186       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    244    244       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58     63       {ECO:0000250}.
FT   DISULFID     91    102       {ECO:0000250}.
FT   DISULFID     96    111       {ECO:0000250}.
FT   DISULFID    113    122       {ECO:0000250}.
FT   DISULFID    132    143       {ECO:0000250}.
FT   DISULFID    139    153       {ECO:0000250}.
FT   DISULFID    155    168       {ECO:0000250}.
FT   DISULFID    176    303       {ECO:0000250}.
FT   DISULFID    200    205       {ECO:0000250}.
FT   DISULFID    219    235       {ECO:0000250}.
FT   DISULFID    351    370       {ECO:0000250}.
FT   DISULFID    381    409       {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
//

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