(data stored in ACNUC19913 zone)

HOGENOM: HS13_PE1077

ID   HS13_PE1077                          STANDARD;      PRT;   466 AA.
AC   HS13_PE1077;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Coagulation factor VII; EC=3.4.21 21;AltName:
DE   Full=Proconvertin;AltName: Full=Serum prothrombin conversion accelerator;
DE   Short=SPCA;AltName: INN=Eptacog alfa;Contains: RecName: Full=Factor VII
DE   light chain;Contains: RecName: Full=Factor VII heavy chain;Flags:
DE   Precursor; (HS13.PE1077).
GN   Name=F7;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS13.PE1077.
CC       Homo sapiens chromosome 13 GRCh37  sequence 1..115109878 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA7_HUMAN
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.
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.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P08709-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P08709-2; Sequence=VSP_005387;
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   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC   -!- DISEASE: Defects in F7 are the cause of factor VII deficiency
CC       (FA7D) [MIM:227500]. A hemorrhagic disease with variable
CC       presentation. The clinical picture can be very severe, with the
CC       early occurrence of intracerebral hemorrhages or repeated
CC       hemarthroses, or, in contrast, moderate with cutaneous-mucosal
CC       hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a
CC       surgical intervention. Finally, numerous subjects are completely
CC       asymptomatic despite very low factor VII levels.
CC   -!- PHARMACEUTICAL: Available under the names Niastase or Novoseven
CC       (Novo Nordisk). Used for the treatment of bleeding episodes in
CC       hemophilia A or B patients with antibodies to coagulation factors
CC       VIII or IX.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Factor VII entry;
CC       URL="http://en.wikipedia.org/wiki/Factor_VII";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/F7";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/f7/";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F7";
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000057593;ENST00000375581;ENSP00000364731.
DR   EMBL; AF466933; - ;
DR   EMBL; AK298404; - ;
DR   EMBL; AL137002; - ;
DR   EMBL; AY212252; - ;
DR   EMBL; AY423856; - ;
DR   EMBL; BC130468; - ;
DR   EMBL; DQ142911; - ;
DR   EMBL; EF421855; - ;
DR   EMBL; EF445049; - ;
DR   EMBL; EF467243; - ;
DR   EMBL; EF467244; - ;
DR   EMBL; EU557239; - ;
DR   EMBL; J02933; - ;
DR   EMBL; M13232; - ;
DR   EMBL; U14580; - ;
DR   UniProtKB/Swiss-Prot; P08709; B0YJC8; Q14339; Q5JVF1; Q5JVF2; Q9UD52; Q9UD53; Q9UD54; -.
DR   EMBL; M13232; AAA88040.1; -; mRNA.
DR   EMBL; M13232; AAA88041.1; -; mRNA.
DR   EMBL; J02933; AAA51983.1; -; Genomic_DNA.
DR   EMBL; DQ142911; ABD17891.1; -; Genomic_DNA.
DR   EMBL; AY212252; AAP33841.1; -; Genomic_DNA.
DR   EMBL; EU557239; ACB87203.1; -; mRNA.
DR   EMBL; AF466933; AAL66184.1; -; Genomic_DNA.
DR   EMBL; EF445049; ACA06107.1; -; Genomic_DNA.
DR   EMBL; EF445049; ACA06108.1; -; Genomic_DNA.
DR   EMBL; AL137002; CAI41381.1; -; Genomic_DNA.
DR   EMBL; AL137002; CAI41382.1; -; Genomic_DNA.
DR   EMBL; BC130468; AAI30469.1; -; mRNA.
DR   IPI; IPI00329555; -.
DR   IPI; IPI00798065; -.
DR   PIR; A28322; KFHU7.
DR   RefSeq; NP_000122.1; NM_000131.3.
DR   RefSeq; NP_062562.1; NM_019616.2.
DR   UniGene; Hs.36989; -.
DR   PDB; 1BF9; NMR; -; A=105-145.
DR   PDB; 1CVW; X-ray; 2.28 A; H=213-466, L=150-204.
DR   PDB; 1DAN; X-ray; 2.00 A; H=213-466, L=61-212.
DR   PDB; 1DVA; X-ray; 3.00 A; H/I=213-466, L/M=102-202.
DR   PDB; 1F7E; NMR; -; A=105-147.
DR   PDB; 1F7M; NMR; -; A=105-147.
DR   PDB; 1FAK; X-ray; 2.10 A; H=213-466, L=61-212.
DR   PDB; 1FF7; NMR; -; A=105-147.
DR   PDB; 1FFM; NMR; -; A=105-147.
DR   PDB; 1J9C; X-ray; 2.90 A; H=213-466, L=108-202.
DR   PDB; 1JBU; X-ray; 2.00 A; H=213-466, L=150-212.
DR   PDB; 1KLI; X-ray; 1.69 A; H=213-466, L=144-212.
DR   PDB; 1KLJ; X-ray; 2.44 A; H=213-466, L=144-212.
DR   PDB; 1NL8; Model; -; H=213-466, M=61-202.
DR   PDB; 1O5D; X-ray; 2.05 A; H=213-466, L=61-212.
DR   PDB; 1QFK; X-ray; 2.80 A; H=213-466, L=109-212.
DR   PDB; 1W0Y; X-ray; 2.50 A; H=213-466, L=61-202.
DR   PDB; 1W2K; X-ray; 3.00 A; H=213-466, L=61-202.
DR   PDB; 1W7X; X-ray; 1.80 A; H=213-466, L=150-204.
DR   PDB; 1W8B; X-ray; 3.00 A; H=213-466, L=148-204.
DR   PDB; 1WQV; X-ray; 2.50 A; H=213-466, L=61-212.
DR   PDB; 1WSS; X-ray; 2.60 A; H=213-466, L=61-212.
DR   PDB; 1WTG; X-ray; 2.20 A; H=213-466, L=61-212.
DR   PDB; 1WUN; X-ray; 2.40 A; H=213-466, L=61-212.
DR   PDB; 1WV7; X-ray; 2.70 A; H=213-466, L=61-212.
DR   PDB; 1YGC; X-ray; 2.00 A; H=213-466, L=150-212.
DR   PDB; 1Z6J; X-ray; 2.00 A; H=213-466, L=61-202.
DR   PDB; 2A2Q; X-ray; 1.80 A; H=213-466, L=61-212.
DR   PDB; 2AEI; X-ray; 2.52 A; H=213-466, L=61-212.
DR   PDB; 2AER; X-ray; 1.87 A; H=213-466, L=61-202.
DR   PDB; 2B7D; X-ray; 2.24 A; H=213-466, L=61-212.
DR   PDB; 2B8O; X-ray; 2.80 A; H=213-466, L=61-202.
DR   PDB; 2BZ6; X-ray; 1.60 A; H=213-466, L=150-202.
DR   PDB; 2C4F; X-ray; 1.72 A; H=213-466, L=61-202.
DR   PDB; 2EC9; X-ray; 2.00 A; H=213-466, L=61-202.
DR   PDB; 2F9B; X-ray; 2.54 A; H=213-466, L=61-212.
DR   PDB; 2FIR; X-ray; 2.00 A; H=213-466, L=61-202.
DR   PDB; 2FLB; X-ray; 1.95 A; H=213-466, L=61-212.
DR   PDB; 2FLR; X-ray; 2.35 A; H=213-466, L=61-212.
DR   PDB; 2PUQ; X-ray; 2.05 A; H=213-466, L=109-202.
DR   PDB; 2ZP0; X-ray; 2.70 A; H=213-466, L=61-212.
DR   PDB; 2ZWL; X-ray; 2.20 A; H=213-466, L=61-212.
DR   PDB; 2ZZU; X-ray; 2.50 A; H=213-466, L=61-212.
DR   PDB; 3ELA; X-ray; 2.20 A; H=213-466, L=61-212.
DR   PDBsum; 1BF9; -.
DR   PDBsum; 1CVW; -.
DR   PDBsum; 1DAN; -.
DR   PDBsum; 1DVA; -.
DR   PDBsum; 1F7E; -.
DR   PDBsum; 1F7M; -.
DR   PDBsum; 1FAK; -.
DR   PDBsum; 1FF7; -.
DR   PDBsum; 1FFM; -.
DR   PDBsum; 1J9C; -.
DR   PDBsum; 1JBU; -.
DR   PDBsum; 1KLI; -.
DR   PDBsum; 1KLJ; -.
DR   PDBsum; 1NL8; -.
DR   PDBsum; 1O5D; -.
DR   PDBsum; 1QFK; -.
DR   PDBsum; 1W0Y; -.
DR   PDBsum; 1W2K; -.
DR   PDBsum; 1W7X; -.
DR   PDBsum; 1W8B; -.
DR   PDBsum; 1WQV; -.
DR   PDBsum; 1WSS; -.
DR   PDBsum; 1WTG; -.
DR   PDBsum; 1WUN; -.
DR   PDBsum; 1WV7; -.
DR   PDBsum; 1YGC; -.
DR   PDBsum; 1Z6J; -.
DR   PDBsum; 2A2Q; -.
DR   PDBsum; 2AEI; -.
DR   PDBsum; 2AER; -.
DR   PDBsum; 2B7D; -.
DR   PDBsum; 2B8O; -.
DR   PDBsum; 2BZ6; -.
DR   PDBsum; 2C4F; -.
DR   PDBsum; 2EC9; -.
DR   PDBsum; 2F9B; -.
DR   PDBsum; 2FIR; -.
DR   PDBsum; 2FLB; -.
DR   PDBsum; 2FLR; -.
DR   PDBsum; 2PUQ; -.
DR   PDBsum; 2ZP0; -.
DR   PDBsum; 2ZWL; -.
DR   PDBsum; 2ZZU; -.
DR   PDBsum; 3ELA; -.
DR   ProteinModelPortal; P08709; -.
DR   SMR; P08709; 68-466.
DR   DIP; DIP-6135N; -.
DR   IntAct; P08709; 11.
DR   MINT; MINT-1155299; -.
DR   STRING; P08709; -.
DR   MEROPS; S01.215; -.
DR   GlycoSuiteDB; P08709; -.
DR   PRIDE; P08709; -.
DR   Ensembl; ENST00000346342; ENSP00000329546; ENSG00000057593.
DR   Ensembl; ENST00000375581; ENSP00000364731; ENSG00000057593.
DR   GeneID; 2155; -.
DR   KEGG; hsa:2155; -.
DR   NMPDR; fig|9606.3.peg.9116; -.
DR   UCSC; uc001vsv.1; human.
DR   CTD; 2155; -.
DR   GeneCards; GC13P094198; -.
DR   H-InvDB; HIX0037323; -.
DR   HGNC; HGNC:3544; F7.
DR   HPA; HPA004826; -.
DR   MIM; 227500; phenotype.
DR   MIM; 613878; gene.
DR   neXtProt; NX_P08709; -.
DR   Orphanet; 327; Congenital factor VII deficiency.
DR   PharmGKB; PA160; -.
DR   InParanoid; P08709; -.
DR   OMA; GHFGVYT; -.
DR   OrthoDB; EOG4HX51H; -.
DR   PhylomeDB; P08709; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   Reactome; REACT_24941; Circadian Clock.
DR   Reactome; REACT_604; Hemostasis.
DR   DrugBank; DB00100; Coagulation Factor IX.
DR   DrugBank; DB00036; Coagulation factor VIIa.
DR   DrugBank; DB00170; Menadione.
DR   NextBio; 8705; -.
DR   PMAP-CutDB; P08709; -.
DR   ArrayExpress; P08709; -.
DR   Bgee; P08709; -.
DR   CleanEx; HS_F7; -.
DR   Genevestigator; P08709; -.
DR   GermOnline; ENSG00000057593; Homo sapiens.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0001948; F:glycoprotein binding; IPI:BHF-UCL.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR   GO; GO:0006916; P:anti-apoptosis; TAS:BHF-UCL.
DR   GO; GO:0007598; P:blood coagulation, extrinsic pathway; EXP:Reactome.
DR   GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling cascade; IDA:BHF-UCL.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; TAS:Reactome.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 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; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   SUPFAM; SSF57630; VitK_dep_GLA; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 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   HOGENOMDNA; HS13.PE1077; -.
KW   ENSG000000575931755old_1320000031; ENSP000003647317901old_1320000031;
KW   A3RKG7_HUMAN; A3RMR0_HUMAN; A3RMR1_HUMAN; B4DPM2_HUMAN; Q6TDG2_HUMAN;
KW   AF466933; AK298404; AL137002; AY212252; AY423856; BC130468; DQ142911;
KW   EF445049; EF467243; EF467244; EU557239; J02933; M13232; U14580;
KW   3D-structure; Alternative splicing; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase;
KW   Hydroxylation; Pharmaceutical; Polymorphism; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Zymogen.
SQ   SEQUENCE   466 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE AHGVLHRRRR
     ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF WISYSDGDQC ASSPCQNGGS
     CKDQLQSYIC FCLPAFEGRN CETHKDDQLI CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL
     LADGVSCTPT VEYPCGKIPI LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG
     TLINTIWVVS AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN
     HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR GATALELMVL
     NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC KGDSGGPHAT HYRGTWYLTG
     IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL MRSEPRPGVL LRAPFP
//

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