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[1]
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PROTEIN SEQUENCE.
DOI=10.1016/0049-3848(75)90106-1; PubMed=1198547 [NCBI, ExPASy, EBI, Israel, Japan]
Birken S.,
Wilner G.D.,
Canfield R.E.;
"Studies of the structure of canine fibrinogen.";
Thromb. Res. 7:599-610(1975).
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[2]
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PROTEIN SEQUENCE OF 1-19.
Blombaeck B.,
Blombaeck M.,
Grondahl N.J.;
"Studies on fibrinopeptides from mammals.";
Acta Chem. Scand. 19:1789-1791(1965).
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[3]
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PROTEIN SEQUENCE OF 1-19.
PubMed=5727635 [NCBI, ExPASy, EBI, Israel, Japan]
Krajewski T.,
Blombaeck B.;
"The location of tyrosine-O-sulphate in fibrinopeptides.";
Acta Chem. Scand. 22:1339-1346(1968).
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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: 31 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 3731 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: A043727257698156 [This is a checksum on the sequence] |
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10 20 30
HYYDDTDEEE RIVSTVDARG HRPLDKKREE A
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P02677 in FASTA format |
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ExPASy Home page
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