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[1]
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PROTEIN SEQUENCE.
Mross G.A.,
Doolittle R.F.;
"Amino acid sequence studies on artiodacty fibrinopeptides.";
Arch. Biochem. Biophys. 122:674-684(1967).
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- FUNCTION: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity).
- SUBCELLULAR LOCATION: Secreted.
- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 21 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 2514 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: FCEE75188F0C1627 [This is a checksum on the sequence] |
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