(data stored in ACNUC19913 zone)

HOGENOM: BOVINUN_004_2476_PE1

ID   BOVINUN_004_2476_PE1                 STANDARD;      PRT;   447 AA.
AC   BOVINUN_004_2476_PE1; P22457; A6H6Y5; Q58DL3;
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; (BOVINUN_004_2476.PE1).
GN   Name=F7;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from
CC       the HOGENOM CDS BOVINUN_004_2476.PE1.
CC       Bos taurus chromosome Un.004.2476 Btau_4.0 full sequence 1..19509 annot
CC       by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA7_BOVIN
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   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
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:Bos_taurus;ENSBTAG00000035340;ENSBTAT00000049854;ENSBTAP00000046678.
DR   EMBL; BC146045; - ;
DR   EMBL; BT021584; - ;
DR   UniProtKB/Swiss-Prot; P22457; A6H6Y5; Q58DL3; -.
DR   EMBL; BT021584; AAX46431.1; -; mRNA.
DR   EMBL; BC146045; AAI46046.1; -; mRNA.
DR   IPI; IPI00713401; -.
DR   PIR; A31979; KFBO7.
DR   RefSeq; NP_001029978.1; NM_001034806.1.
DR   RefSeq; XP_001250512.1; XM_001250511.2.
DR   UniGene; Bt.37397; -.
DR   ProteinModelPortal; P22457; -.
DR   SMR; P22457; 41-182, 193-445.
DR   MEROPS; S01.215; -.
DR   PRIDE; P22457; -.
DR   Ensembl; ENSBTAT00000009746; ENSBTAP00000009746; ENSBTAG00000007411.
DR   Ensembl; ENSBTAT00000049854; ENSBTAP00000046678; ENSBTAG00000035340.
DR   GeneID; 617960; -.
DR   GeneID; 785517; -.
DR   KEGG; bta:617960; -.
DR   KEGG; bta:785517; -.
DR   CTD; 2155; -.
DR   eggNOG; maNOG13655; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; P22457; -.
DR   OMA; GHFGVYT; -.
DR   OrthoDB; EOG4HX51H; -.
DR   PhylomeDB; P22457; -.
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; 2.
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; BOVINUN_004_2476.PE1; -.
KW   ENSBTAG00000035340fold_1320000031; ENSBTAP00000046678fold_1320000031;
KW   BC146045; BT021584;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW   Signal; Zymogen.
SQ   SEQUENCE   447 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLSQAWALAL LCFLLSLWGS LPAVFLPQEQ ALSILHRPRR ANGFLEELLP GSLERECREE
     LCSFEEAHEI FRNEERTRQF WVSYNDGDQC ASSPCQNGGS CEDQLRSYIC FCPDGFEGRN
     CETDKQSQLI CANDNGGCEQ YCGADPGAGR FCWCHEGYAL QADGVSCAPT VEYPCGKIPV
     LEKRNGSKPQ GRIVGGHVCP KGECPWQAML KLNGALLCGG TLVGPAWVVS AAHCFERLRS
     RGNLTAVLGE HDLSRVEGPE QERRVAQIIV PKQYVPGQTD HDVALLQLAQ PVALGDHVAP
     LCLPDPDFAD QTLAFVRFSA VSGWGQLLER GVTARKLMVV LVPRLLTQDC LQQSRQRPGG
     PVVTDNMFCA GYSDGSKDAC KGDSGGPHAT RFRGTWFLTG VVSWGEGCAA AGHFGIYTRV
     SRYTAWLRQL MGHPPSRQGF FQVPLLP
//

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