(data stored in ACNUC19913 zone)

HOGENOM: PANTR13_116_PE14

ID   PANTR13_116_PE14                     STANDARD;      PRT;   390 AA.
AC   PANTR13_116_PE14; Q2F9P2;
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; (PANTR13_116.PE14).
GN   Name=F7;
OS   PAN TROGLODYTES.
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; Pan.
OX   NCBI_TaxID=9598;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PANTR13_116.PE14.
CC       Pan troglodytes chromosome 13 CHIMP2.1 partial sequence
CC       114141611..115141610 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA7_PANTR
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   -!- 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:Pan_troglodytes;ENSPTRG00000006049;ENSPTRT00000011112;ENSPTRP00000010284.
DR   UniProtKB/Swiss-Prot; Q2F9P2; -.
DR   EMBL; DQ142914; ABD17894.1; -; Genomic_DNA.
DR   EMBL; DQ142915; ABD17895.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q2F9P2; -.
DR   SMR; Q2F9P2; 61-202, 213-466.
DR   STRING; Q2F9P2; -.
DR   MEROPS; S01.215; -.
DR   eggNOG; maNOG13655; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; Q2F9P2; -.
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; PANTR13_116.PE14; -.
KW   ENSPTRG00000006049-2caffold_90100000011;
KW   FA7_PANTR;
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   390 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVSQALRLLC LLLGLQGCLA AKLFWISYSD GDQCASSPCQ NGGSCKDQLQ SYICFCLPAF
     EGRNCETYKD DQLICVNENG GCEQYCSDHT GTKRSCRCHE GYSLLADGVS CTPTVEYPCG
     KIPILEKRNA SKPQGRIVGG KVCPKGECPW QVLLLVNGAQ LCGGTLINTI WVVSAAHCFD
     KIKNWRNLIA VLGEHDLSEH DGDEQSRRVA QVIIPSTYIP GTTNHDIALL RLHQPVVLTD
     HVVPLCLPER AFSERTLAFV RFSLVSGWGQ LLDRGATALE LMVLNVPRLM TQDCLQQSRK
     VGDSPNITEY MFCAGYSDGS KDSCKGDSGG PHATHYRGTW YLTGIVSWGQ GCASVGHFGV
     YTRVSQYIEW LQKLMRSEPR PGVLLRAPFP
//

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