(data stored in ACNUC19913 zone)

HOGENOM: RAT16_PE861

ID   RAT16_PE861                          STANDARD;      PRT;   446 AA.
AC   RAT16_PE861; Q8K3U6;
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; (RAT16.PE861).
GN   Name=F7;
OS   RATTUS NORVEGICUS.
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; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT16.PE861.
CC       Rattus norvegicus chromosome 16 RGSC3.4  sequence 1..90238779
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA7_RAT
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 (By similarity).
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:Rattus_norvegicus;ENSRNOG00000032737;ENSRNOT00000037806;ENSRNOP00000038466.
DR   EMBL; AF532184; - ;
DR   UniProtKB/Swiss-Prot; Q8K3U6; -.
DR   EMBL; AF532184; AAM95967.1; -; mRNA.
DR   IPI; IPI00202610; -.
DR   RefSeq; NP_690059.1; NM_152846.1.
DR   UniGene; Rn.86416; -.
DR   ProteinModelPortal; Q8K3U6; -.
DR   SMR; Q8K3U6; 61-183, 194-440.
DR   STRING; Q8K3U6; -.
DR   MEROPS; S01.215; -.
DR   PRIDE; Q8K3U6; -.
DR   Ensembl; ENSRNOT00000037806; ENSRNOP00000038466; ENSRNOG00000032737.
DR   GeneID; 260320; -.
DR   KEGG; rno:260320; -.
DR   NMPDR; fig|10116.3.peg.12777; -.
DR   UCSC; NM_152846; rat.
DR   CTD; 2155; -.
DR   RGD; 628678; F7.
DR   eggNOG; roNOG14960; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; Q8K3U6; -.
DR   OMA; GHFGVYT; -.
DR   OrthoDB; EOG4HX51H; -.
DR   PhylomeDB; Q8K3U6; -.
DR   NextBio; 624347; -.
DR   Genevestigator; Q8K3U6; -.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0042598; C:vesicular fraction; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005102; F:receptor binding; IPI:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR   GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR   GO; GO:0031100; P:organ regeneration; IEP:RGD.
DR   GO; GO:0030194; P:positive regulation of blood coagulation; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0043627; P:response to estrogen stimulus; IEP:RGD.
DR   GO; GO:0060416; P:response to growth hormone stimulus; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0032571; P:response to vitamin K; IEP:RGD.
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; RAT16.PE861; -.
KW   ENSRNOG00000032737820036002503210000011;
KW   F7; FA7_RAT; AF532184;
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;
     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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