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[1]
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PROTEIN SEQUENCE OF 1-36.
DOI=10.1016/0005-2795(76)90138-0; PubMed=999898 [NCBI, ExPASy, EBI, Israel, Japan]
Cottrell B.A.,
Doolittle R.F.;
"Amino acid sequences of lamprey fibrinopeptides A and B and characterizations of the junctions split by lamprey and mammalian thrombins.";
Biochim. Biophys. Acta 453:426-438(1976).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] OF 37-477.
DOI=10.1021/bi00369a026; PubMed=3790537 [NCBI, ExPASy, EBI, Israel, Japan]
Bohonus V.L.,
Doolittle R.F.,
Pontes M.,
Strong D.D.;
"Complementary DNA sequence of lamprey fibrinogen beta chain.";
Biochemistry 25:6512-6516(1986).
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[3]
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X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 155-477.
DOI=10.1021/bi020299t; PubMed=12162736 [NCBI, ExPASy, EBI, Israel, Japan]
Yang Z.,
Spraggon G.,
Pandi L.,
Everse S.J.,
Riley M.,
Doolittle R.F.;
"Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide.";
Biochemistry 41:10218-10224(2002).
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[4]
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X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 155-477.
DOI=10.1021/bi026666i; PubMed=12501189 [NCBI, ExPASy, EBI, Israel, Japan]
Yang Z.,
Pandi L.,
Doolittle R.F.;
"The crystal structure of fragment double-D from cross-linked lamprey fibrin reveals isopeptide linkages across an unexpected D-D interface.";
Biochemistry 41:15610-15617(2002).
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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. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
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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: 477 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 54270 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: B8A95E7E32D09D18 [This is a checksum on the sequence] |
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10 20 30 40 50 60
EDLSLVGQPE NDYDTGDDBT AADPDSNNTA AALDVRRPLP SGTRVRRPPL RHRRLAPGAV
70 80 90 100 110 120
MSRDPPASPR PQEAQKAIRD EGGCMLPESD LGVLCPTGCE LREELLKQRD PVRYKISMLK
130 140 150 160 170 180
QNLTYFINSF DRMASDSNTL KQNVQTLRRR LNSRSSTHVN AQKEIENRYK EVKIRIESTV
190 200 210 220 230 240
AGSLRSMKSV LEHLRAKMQR MEEAIKTQKE LCSAPCTVNC RVPVVSGMHC EDIYRNGGRT
250 260 270 280 290 300
SEAYYIQPDL FSEPYKVFCD MESHGGGWTV VQNRVDGSSN FARDWNTYKA EFGNIAFGNG
310 320 330 340 350 360
KSICNIPGEY WLGTKTVHQL TKQHTQQVLF DMSDWEGSSV YAQYASFRPE NEAQGYRLWV
370 380 390 400 410 420
EDYSGNAGNA LLEGATQLMG DNRTMTIHNG MQFSTFDRDN DNWNPGDPTK HCSREDAGGW
430 440 450 460 470
WYNRCHAANP NGRYYWGGIY TKEQADYGTD DGVVWMNWKG SWYSMRQMAM KLRPKWP
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P02678 in FASTA format |
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ExPASy Home page
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