##gff-version 3 P70375 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P70375 UniProtKB Propeptide 25 41 . . . ID=PRO_0000027732;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70375 UniProtKB Chain 42 193 . . . ID=PRO_0000027733;Note=Factor VII light chain P70375 UniProtKB Chain 194 446 . . . ID=PRO_0000027734;Note=Factor VII heavy chain P70375 UniProtKB Domain 42 86 . . . Note=Gla;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Domain 87 123 . . . Note=EGF-like 1%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 P70375 UniProtKB Domain 128 169 . . . Note=EGF-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 P70375 UniProtKB Domain 194 433 . . . Note=Peptidase S1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00274 P70375 UniProtKB Active site 234 234 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Active site 283 283 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Active site 385 385 . . . Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Binding site 379 379 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Site 193 194 . . . Note=Cleavage%3B by factor Xa%2C factor XIIa%2C factor IXa%2C or thrombin;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Modified residue 47 47 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 48 48 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 55 55 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 57 57 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 60 60 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 61 61 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 66 66 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 67 67 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 70 70 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 76 76 . . . Note=4-carboxyglutamate;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P22457,ECO:0000255|PROSITE-ProRule:PRU00463 P70375 UniProtKB Modified residue 104 104 . . . Note=(3R)-3-hydroxyaspartate;Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Glycosylation 93 93 . . . Note=O-linked (Glc...) serine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08709 P70375 UniProtKB Glycosylation 93 93 . . . Note=O-linked (Xyl...) serine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08709 P70375 UniProtKB Glycosylation 186 186 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70375 UniProtKB Glycosylation 244 244 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P70375 UniProtKB Disulfide bond 58 63 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 91 102 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 96 111 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 113 122 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 132 143 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 139 153 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 155 168 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 176 303 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 200 205 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 219 235 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 351 370 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Disulfide bond 381 409 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P70375 UniProtKB Sequence conflict 99 99 . . . Note=G->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P70375 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5KXH P70375 UniProtKB Beta strand 101 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5KXH P70375 UniProtKB Beta strand 108 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5KXH P70375 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5KXH