(data stored in ACNUC19913 zone)

HOGENOM: RABITUN1197_PE1

ID   RABITUN1197_PE1                      STANDARD;      PRT;   368 AA.
AC   RABITUN1197_PE1; P98139; P79224;
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   Flags: Fragments;
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; (RABITUN1197.PE1).
GN   Name=F7;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABITUN1197.PE1.
CC       Oryctolagus cuniculus chromosome Un1197 oryCun2 full sequence 1..25213
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA7_RABIT
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:Oryctolagus_cuniculus;ENSOCUG00000021021;ENSOCUT00000028291;ENSOCUP00000024648.
DR   EMBL; U77477; - ;
DR   UniProtKB/Swiss-Prot; P98139; P79224; -.
DR   EMBL; U77477; AAB37326.1; -; mRNA.
DR   PIR; I46932; I46932.
DR   RefSeq; NP_001076148.1; NM_001082679.1.
DR   UniGene; Ocu.2617; -.
DR   ProteinModelPortal; P98139; -.
DR   SMR; P98139; 40-181, 192-444.
DR   MEROPS; S01.215; -.
DR   Ensembl; ENSOCUT00000028291; ENSOCUP00000024648; ENSOCUG00000021021.
DR   GeneID; 100009399; -.
DR   CTD; 2155; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   OrthoDB; EOG4HX51H; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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; 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; RABITUN1197.PE1; -.
KW   ENSOCUG00000021021820036002503210000011;
KW   FA7_RABIT; U77477;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
SQ   SEQUENCE   368 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     KQFWITYNDG DQCASNPCQN GGSCEDQIQS YICFCLADFE GRNCEKNKND QLICMYENGG
     CEQYCSDHVG SQRSCRCHEG YTLLPNGVSC TPTVDYPCGK VPALEKRGAS NPQGRIVGGK
     VCPKGECPWQ AALMNGSTLL CGGSLLDTHW VVSAAHCFDK LSSLRNLTIV LGEHDLSEHE
     GDEQVRHVAQ LIMPDKYVPG KTDHDIALLR LLQPAVLTNN VVPLCLPERN FSESTLATIR
     FSRVSGWGQL LYRGALAREL MAIDVPRLMT QDCVEQSEHK PGSPEVTGNM FCAGYLDGSK
     DACKGDSGGP HATSYHGTWY LTGVVSWGEG CAAVGHVGVY TRVSRYTEWL SRLMRSKLHH
     GIQRHPFP
//

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