##gff-version 3
Q8K0E8	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8K0E8	UniProtKB	Peptide	20	34	.	.	.	ID=PRO_0000009078;Note=Fibrinopeptide B;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8K0E8	UniProtKB	Chain	35	481	.	.	.	ID=PRO_0000009077;Note=Fibrinogen beta chain	
Q8K0E8	UniProtKB	Domain	222	478	.	.	.	Note=Fibrinogen C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00739	
Q8K0E8	UniProtKB	Region	22	81	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8K0E8	UniProtKB	Region	35	37	.	.	.	Note=Beta-chain polymerization%2C binding distal domain of another fibrin;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8K0E8	UniProtKB	Coiled coil	149	213	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8K0E8	UniProtKB	Compositional bias	29	48	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8K0E8	UniProtKB	Site	34	35	.	.	.	Note=Cleavage%3B by thrombin%3B to release fibrinopeptide B;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8K0E8	UniProtKB	Glycosylation	384	384	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8K0E8	UniProtKB	Disulfide bond	213	213	.	.	.	Note=Interchain (with alpha chain);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00739	
Q8K0E8	UniProtKB	Disulfide bond	217	217	.	.	.	Note=Interchain (with gamma chain);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00739	
Q8K0E8	UniProtKB	Disulfide bond	221	306	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00739	
Q8K0E8	UniProtKB	Disulfide bond	231	260	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00739	
Q8K0E8	UniProtKB	Disulfide bond	414	427	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00739