(data stored in ACNUC19913 zone)

HOGENOM: MOUSE8_PE162

ID   MOUSE8_PE162                         STANDARD;      PRT;   446 AA.
AC   MOUSE8_PE162; P70375; Q61109;
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: Full=Serum
DE   prothrombin conversion accelerator;Contains: RecName: Full=Factor VII
DE   light chain;Contains: RecName: Full=Factor VII heavy chain;Flags:
DE   Precursor; (MOUSE8.PE162).
GN   Name=F7; Synonyms=Cf7;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE8.PE162.
CC       Mus musculus chromosome 8 NCBIM37  sequence 1..131738871 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA7_MOUSE
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).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium (By
CC       similarity).
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains
CC       (By similarity).
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   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000031443;ENSMUST00000033820;ENSMUSP00000033820.
DR   EMBL; AK089402; - ;
DR   EMBL; AK154742; - ;
DR   EMBL; AK171362; - ;
DR   EMBL; BC061149; - ;
DR   EMBL; CH466566; - ;
DR   EMBL; U44795; - ;
DR   EMBL; U66079; - ;
DR   UniProtKB/Swiss-Prot; P70375; Q61109; -.
DR   EMBL; U44795; AAC52570.1; -; mRNA.
DR   EMBL; U66079; AAC33796.1; -; Genomic_DNA.
DR   EMBL; BC061149; AAH61149.1; -; mRNA.
DR   IPI; IPI00307890; -.
DR   RefSeq; NP_034302.2; NM_010172.3.
DR   UniGene; Mm.4827; -.
DR   ProteinModelPortal; P70375; -.
DR   SMR; P70375; 49-184, 194-445.
DR   STRING; P70375; -.
DR   MEROPS; S01.215; -.
DR   PRIDE; P70375; -.
DR   Ensembl; ENSMUST00000033820; ENSMUSP00000033820; ENSMUSG00000031443.
DR   GeneID; 14068; -.
DR   KEGG; mmu:14068; -.
DR   CTD; 2155; -.
DR   MGI; MGI:109325; F7.
DR   eggNOG; roNOG14960; -.
DR   InParanoid; P70375; -.
DR   OMA; GHFGVYT; -.
DR   OrthoDB; EOG4HX51H; -.
DR   PhylomeDB; P70375; -.
DR   Reactome; REACT_24972; Circadian Clock (mouse).
DR   NextBio; 285056; -.
DR   ArrayExpress; P70375; -.
DR   Bgee; P70375; -.
DR   CleanEx; MM_F7; -.
DR   Genevestigator; P70375; -.
DR   GermOnline; ENSMUSG00000031443; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; FALSE_NEG.
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; MOUSE8.PE162; -.
KW   ENSMUSG000000314435old_1320000031; ENSMUSP000000338201old_1320000031;
KW   Q542C2_MOUSE; AK089402; AK154742; AK171362; BC061149; CH466566; U44795;
KW   U66079;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation;
KW   Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW   Signal; Zymogen.
SQ   SEQUENCE   446 AA;  UNKNOWN MW;  UNKNOWN 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
//

If you have problems or comments...

PBIL Back to PBIL home page