|
|
|
|
|
|
[1]
|
PROTEIN SEQUENCE OF 1-4.
Blombaeck B.,
Doolittle R.F.;
"The sequence of amino acids at the N-terminal end of bovine fibrinopeptide B.";
Acta Chem. Scand. 17:1816-1819(1963).
|
[2]
|
PROTEIN SEQUENCE OF 5-21.
Sjoquist J.,
Blombaeck B.,
Wallen P.;
"Amino acid sequence of bovine fibrinopeptides.";
Ark. Kemi 16:425-436(1960).
|
[3]
|
PROTEIN SEQUENCE OF 22-53.
DOI=10.1016/0003-9861(79)90068-7; PubMed=434821 [NCBI, ExPASy, EBI, Israel, Japan]
Martinelli R.A.,
Inglis A.S.,
Rubira M.R.,
Hageman T.C.,
Hurrell J.G.R.,
Leach S.J.,
Scheraga H.A.;
"Amino acid sequences of portions of the alpha and beta chains of bovine fibrinogen.";
Arch. Biochem. Biophys. 192:27-32(1979).
|
[4]
|
NUCLEOTIDE SEQUENCE [MRNA] OF 44-468.
PubMed=6262803 [NCBI, ExPASy, EBI, Israel, Japan]
Chung D.W.,
Rixon M.W.,
McGillivray R.T.A.,
Davie E.W.;
"Characterization of a cDNA clone coding for the beta chain of bovine fibrinogen.";
Proc. Natl. Acad. Sci. U.S.A. 78:1466-1470(1981).
|
[5]
|
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 61-468.
DOI=10.1016/0022-2836(91)90739-S; PubMed=1942070 [NCBI, ExPASy, EBI, Israel, Japan]
Rao S.P.,
Poojary M.D.,
Elliott B.W. Jr.,
Melanson L.A.,
Oriel B.,
Cohen C.;
"Fibrinogen structure in projection at 18 A resolution. Electron density by co-ordinated cryo-electron microscopy and X-ray crystallography.";
J. Mol. Biol. 222:89-98(1991).
|
[6]
|
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 61-116.
DOI=10.1073/pnas.211439798; PubMed=11593005 [NCBI, ExPASy, EBI, Israel, Japan]
Madrazo J.,
Brown J.H.,
Litvinovich S.,
Dominguez R.,
Yakovlev S.,
Medved L.,
Cohen C.;
"Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 98:11967-11972(2001).
|
|
|
|
- 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.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 468 AA [This is the length of the unprocessed precursor] |
Molecular weight: 53340 Da [This is the MW of the unprocessed precursor] |
CRC64: 2DED42F443AA4B37 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
QFPTDYDEGQ DDRPKVGLGA RGHRPYDKKK EEAPSLRPVP PPISGGGYRA RPATATVGQK
70 80 90 100 110 120
KVERKPPDAD GCLHADPDLG VLCPTGCKLQ DTLVRQERPI RKSIEDLRNT VDSVSRTSSS
130 140 150 160 170 180
TFQYITLLKN MWKGRQNQVQ DNENVVNEYS SHLEKHQLYI DETVKNNIPT KLRVLRSILE
190 200 210 220 230 240
NLRSKIQKLE SDVSTQMEYC RTPCTVTCNI PVVSGKECEK IIRNEGETSE MYLIQPEDSS
250 260 270 280 290 300
KPYRVYCDMK TEKGGWTVIQ NRQDGSVDFG RKWDPYKQGF GNIATNAEGK KYCGVPGEYW
310 320 330 340 350 360
LGNDRISQLT NMGPTKLLIE MEDWKGDKVT ALYEGFTVQN EANKYQLSVS KYKGTAGNAL
370 380 390 400 410 420
IEGASQLVGE NRTMTIHNSM FFSTYDRDND GWKTTDPRKQ CSKEDGGGWW YNRCHAANPN
430 440 450 460
GRYYWGGAYT WDMAKHGTDD GVVWMNWQGS WYSMKKMSMK IRPYFPEQ
|
P02676 in FASTA format |
|
ExPASy Home page
SIB Switzerland
