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Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]

 FIBA_HUMAN              Reviewed;         866 AA.
P02671; A8K3E4; D3DP14; D3DP15; Q4QQH7; Q9BX62; Q9UCH2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 223.
RecName: Full=Fibrinogen alpha chain;
Contains:
RecName: Full=Fibrinopeptide A;
Contains:
RecName: Full=Fibrinogen alpha chain;
Flags: Precursor;
Name=FGA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 2).
PubMed=1457396; DOI=10.1021/bi00163a002;
Fu Y., Weissbach L., Plant P.W., Oddoux C., Cao Y., Liang T.J.,
Roy S.N., Redman C.M., Grieninger G.;
"Carboxy-terminal-extended variant of the human fibrinogen alpha
subunit: a novel exon conferring marked homology to beta and gamma
subunits.";
Biochemistry 31:11968-11972(1992).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Chung D.W., Grieninger G.;
"Fibrinogen DNA and protein sequences.";
(In) Ebert R.F. (eds.);
Index of variant human fibrinogens, pp.13-24, CRC Press, Boca Raton
(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-6; ALA-331 AND
ALA-456.
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ALA-331.
TISSUE=Heart;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE OF 1-655 (ISOFORM 1).
TISSUE=Liver;
PubMed=2102623;
Chung D.W., Harris J.E., Davie E.W.;
"Nucleotide sequences of the three genes coding for human
fibrinogen.";
Adv. Exp. Med. Biol. 281:39-48(1990).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=6575389; DOI=10.1073/pnas.80.13.3953;
Kant J.A., Lord S.T., Crabtree G.R.;
"Partial mRNA sequences for human A alpha, B beta, and gamma
fibrinogen chains: evolutionary and functional implications.";
Proc. Natl. Acad. Sci. U.S.A. 80:3953-3957(1983).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-629.
PubMed=6688355; DOI=10.1021/bi00282a031;
Rixon M.W., Chan W.-Y., Davie E.W., Chung D.W.;
"Characterization of a complementary deoxyribonucleic acid coding for
the alpha chain of human fibrinogen.";
Biochemistry 22:3237-3244(1983).
[10]
PROTEIN SEQUENCE OF 20-629.
Henschen A., Lottspeich F., Southan C., Topfer-Petersen E.;
"Human fibrinogen: sequence, sulfur bridges, glycosylation and some
structural variants.";
(In) Peeters H. (eds.);
Protides of the biological fluids, Proc. 28th colloquium, pp.51-56,
Pergamon Press, Oxford (1980).
[11]
PROTEIN SEQUENCE OF 20-629, DISULFIDE BONDS, AND SUBUNIT.
PubMed=518846; DOI=10.1021/bi00591a024;
Watt K.W.K., Cottrell B.A., Strong D.D., Doolittle R.F.;
"Amino acid sequence studies on the alpha chain of human fibrinogen.
Overlapping sequences providing the complete sequence.";
Biochemistry 18:5410-5416(1979).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 110-156.
PubMed=6689067; DOI=10.1093/nar/11.21.7427;
Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S.;
"Isolation and characterisation of cDNA clones for the A alpha- and
gamma-chains of human fibrinogen.";
Nucleic Acids Res. 11:7427-7434(1983).
[13]
NUCLEOTIDE SEQUENCE OF 605-644 (ISOFORM 2).
PubMed=6575700; DOI=10.1111/j.1749-6632.1983.tb23265.x;
Chung D.W., Rixon M.W., Que B.G., Davie E.W.;
"Cloning of fibrinogen genes and their cDNA.";
Ann. N. Y. Acad. Sci. 408:449-456(1983).
[14]
PROTEIN SEQUENCE OF 20-35.
Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M.;
"Studies on fibrinopeptides from primates.";
Acta Chem. Scand. 19:1788-1789(1965).
[15]
DISULFIDE BONDS, AND SUBUNIT.
PubMed=741445; DOI=10.1016/0049-3848(78)90142-1;
Bouma H., Takagi T., Doolittle R.F.;
"The arrangement of disulfide bonds in fragment D from human
fibrinogen.";
Thromb. Res. 13:557-562(1978).
[16]
CROSS-LINKING ACCEPTOR SITES.
PubMed=518845; DOI=10.1021/bi00591a023;
Cottrell B.A., Strong D.D., Watt K.W.K., Doolittle R.F.;
"Amino acid sequence studies on the alpha chain of human fibrinogen.
Exact location of cross-linking acceptor sites.";
Biochemistry 18:5405-5410(1979).
[17]
CROSS-LINKING ACCEPTOR SITES.
PubMed=632262;
Fretto L.J., Ferguson E.W., Steinman H.M., McKee P.A.;
"Localization of the alpha-chain cross-link acceptor sites of human
fibrin.";
J. Biol. Chem. 253:2184-2195(1978).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[19]
DISULFIDE BONDS, AND SUBUNIT.
PubMed=936108; DOI=10.1016/0049-3848(76)90245-0;
Blombaeck B., Hessel B., Hogg D.;
"Disulfide bridges in NH2-terminal part of human fibrinogen.";
Thromb. Res. 8:639-658(1976).
[20]
REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, AND LIGANDS.
PubMed=6383194; DOI=10.1146/annurev.bi.53.070184.001211;
Doolittle R.F.;
"Fibrinogen and fibrin.";
Annu. Rev. Biochem. 53:195-229(1984).
[21]
CROSS-LINKING SITE FOR ALPHA-2-PLASMIN INHIBITOR.
PubMed=2877981;
Kimura S., Aoki N.;
"Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor.";
J. Biol. Chem. 261:15591-15595(1986).
[22]
PHOSPHORYLATION.
PubMed=6318767; DOI=10.1016/0006-291X(83)91247-0;
Itarte E., Plana M., Guasch M.D., Martos C.;
"Phosphorylation of fibrinogen by casein kinase 1.";
Biochem. Biophys. Res. Commun. 117:631-636(1983).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-412 AND SER-609, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[25]
HYDROXYLATION AT PRO-565.
PubMed=19696023; DOI=10.1074/jbc.M109.041749;
Ono M., Matsubara J., Honda K., Sakuma T., Hashiguchi T., Nose H.,
Nakamori S., Okusaka T., Kosuge T., Sata N., Nagai H., Ioka T.,
Tanaka S., Tsuchida A., Aoki T., Shimahara M., Yasunami Y., Itoi T.,
Moriyasu F., Negishi A., Kuwabara H., Shoji A., Hirohashi S.,
Yamada T.;
"Prolyl 4-hydroxylation of alpha-fibrinogen: a novel protein
modification revealed by plasma proteomics.";
J. Biol. Chem. 284:29041-29049(2009).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[27]
CLEAVAGE BY HEMENTIN AND PLASMIN.
PubMed=2143188;
Kirschbaum N.E., Budzynski A.Z.;
"A unique proteolytic fragment of human fibrinogen containing the A
alpha COOH-terminal domain of the native molecule.";
J. Biol. Chem. 265:13669-13676(1990).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
GLYCOSYLATION AT THR-320 AND SER-351.
PubMed=23050552; DOI=10.1021/pr3005937;
Zauner G., Hoffmann M., Rapp E., Koeleman C.A., Dragan I.,
Deelder A.M., Wuhrer M., Hensbergen P.J.;
"Glycoproteomic analysis of human fibrinogen reveals novel regions of
O-glycosylation.";
J. Proteome Res. 11:5804-5814(2012).
[30]
LACK OF GLYCOSYLATION.
PubMed=23151259; DOI=10.1021/pr300813h;
Adamczyk B., Struwe W.B., Ercan A., Nigrovic P.A., Rudd P.M.;
"Characterization of fibrinogen glycosylation and its importance for
serum/plasma N-glycome analysis.";
J. Proteome Res. 12:444-454(2013).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-50; SER-281;
SER-291; SER-294; THR-412; SER-451; SER-501; THR-505 AND SER-609, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
PHOSPHORYLATION AT SER-45; SER-56; SER-364; SER-524; SER-560 AND
SER-609.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[33]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-39.
PubMed=1560020;
Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P.;
"The structure of residues 7-16 of the A alpha-chain of human
fibrinogen bound to bovine thrombin at 2.3-A resolution.";
J. Biol. Chem. 267:7911-7920(1992).
[34]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 130-216, DISULFIDE BONDS,
AND SUBUNIT.
PubMed=9333233; DOI=10.1038/38947;
Spraggon G., Everse S.J., Doolittle R.F.;
"Crystal structures of fragment D from human fibrinogen and its
crosslinked counterpart from fibrin.";
Nature 389:455-462(1997).
[35]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-216, SUBUNIT, DISULFIDE
BONDS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND COILED COIL
DOMAIN.
PubMed=9628725; DOI=10.1021/bi9804129;
Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F.;
"Crystal structure of fragment double-D from human fibrin with two
different bound ligands.";
Biochemistry 37:8637-8642(1998).
[36]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 666-866 IN COMPLEX WITH
CALCIUM IONS, GLYCOSYLATION AT ASN-686, DISULFIDE BONDS, AND SUBUNIT.
PubMed=9689040; DOI=10.1073/pnas.95.16.9099;
Spraggon G., Applegate D., Everse S.J., Zhang J.Z., Veerapandian L.,
Redman C., Doolittle R.F., Grieninger G.;
"Crystal structure of a recombinant alphaEC domain from human
fibrinogen-420.";
Proc. Natl. Acad. Sci. U.S.A. 95:9099-9104(1998).
[37]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 130-216, AND DISULFIDE
BONDS.
PubMed=10074346; DOI=10.1021/bi982626w;
Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F.;
"Conformational changes in fragments D and double-D from human
fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.";
Biochemistry 38:2941-2946(1999).
[38]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20-581, SUBUNIT, DISULFIDE
BONDS, COILED COIL DOMAIN, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=19296670; DOI=10.1021/bi802205g;
Kollman J.M., Pandi L., Sawaya M.R., Riley M., Doolittle R.F.;
"Crystal structure of human fibrinogen.";
Biochemistry 48:3877-3886(2009).
[39]
VARIANT KYOTO-2 LEU-37.
PubMed=2070049;
Yoshida N., Okuma M., Hirata H., Matsuda M., Yamazumi K., Asakura S.;
"Fibrinogen Kyoto II, a new congenitally abnormal molecule,
characterized by the replacement of A alpha proline-18 by leucine.";
Blood 78:149-153(1991).
[40]
VARIANT LIMA SER-160.
PubMed=1634621; DOI=10.1172/JCI115857;
Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H.,
Takahashi N., Arocha-Pinango C.L., Rodriguez S., Nagy H.,
Perez-Requejo J.L., Matsuda M.;
"Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-
141 to serine substitution associated with extra N-glycosylation at A
alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-
facilitated plasminogen activation catalyzed by tissue-type
plasminogen activator.";
J. Clin. Invest. 90:67-76(1992).
[41]
GLYCOSYLATION AT ASN-453 (VARIANT ASN-453), AND VARIANT CARACAS-2
ASN-453.
PubMed=1675636;
Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H.,
Takahashi N., de Bosch N.B., Carvajal Z., Ojeda A.,
Arocha-Pinango C.L., Matsuda M.;
"An A alpha Ser-434 to N-glycosylated Asn substitution in a
dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin
gel formation.";
J. Biol. Chem. 266:11575-11581(1991).
[42]
INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN CYS-573.
PubMed=8473507; DOI=10.1172/JCI116371;
Koopman J., Haverkate F., Grimbergen J., Lord S.T., Mosesson M.W.,
Diorio J.P., Siebenlist K.S., Legrand C., Soria J., Soria C.,
Caen J.P.;
"Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its
association with abnormal fibrin polymerization and thrombophilia.";
J. Clin. Invest. 91:1637-1643(1993).
[43]
VARIANT AMYL8 LEU-573.
PubMed=8097946; DOI=10.1038/ng0393-252;
Benson M.D., Liepnieks J., Uemichi T., Wheeler G., Correa R.;
"Hereditary renal amyloidosis associated with a mutant fibrinogen
alpha-chain.";
Nat. Genet. 3:252-255(1993).
[44]
VARIANT OSAKA IV HIS-35.
PubMed=8461606; DOI=10.1007/BF00308999;
Yamazumi K., Terukina S., Matsuda M., Kanbayashi J., Sakon M.,
Tsujinaka T.;
"Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a
patient originally reported in relation to surgery, now defined to
have an A alpha arginine-16 to histidine substitution.";
Surg. Today 23:45-50(1993).
[45]
VARIANT CANTERBURY ASP-39.
PubMed=8675656; DOI=10.1172/JCI118356;
Brennan S.O., Hammonds B., George P.M.;
"Aberrant hepatic processing causes removal of activation peptide and
primary polymerisation site from fibrinogen Canterbury (A-alpha 20
Val-to-Asp).";
J. Clin. Invest. 96:2854-2858(1995).
[46]
VARIANTS ALA-331 AND GLU-446.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[47]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[48]
INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN CYS-35.
PubMed=16846481; DOI=10.1111/j.1365-2141.2006.06129.x;
Flood V.H., Al-Mondhiry H.A., Farrell D.H.;
"The fibrinogen Aalpha R16C mutation results in fibrinolytic
resistance.";
Br. J. Haematol. 134:220-226(2006).
[49]
INVOLVEMENT IN CAFBN; VARIANTS CAFBN ARG-55; PRO-129 AND TRP-184, AND
CHARACTERIZATION OF VARIANTS CAFBN ARG-55; PRO-129 AND TRP-184.
PubMed=25427968; DOI=10.1160/TH14-07-0629;
Asselta R., Plate M., Robusto M., Borhany M., Guella I., Solda G.,
Afrasiabi A., Menegatti M., Shamsi T., Peyvandi F., Duga S.;
"Clinical and molecular characterisation of 21 patients affected by
quantitative fibrinogen deficiency.";
Thromb. Haemost. 113:567-576(2015).
-!- FUNCTION: Cleaved by the protease thrombin to yield monomers
which, together with fibrinogen beta (FGB) and fibrinogen gamma
(FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a
major function in hemostasis as one of the primary components of
blood clots. In addition, functions during the early stages of
wound repair to stabilize the lesion and guide cell migration
during re-epithelialization. Was originally thought to be
essential for platelet aggregation, based on in vitro studies
using anticoagulated blood. However, subsequent studies have shown
that it is not absolutely required for thrombus formation in vivo.
Enhances expression of SELP in activated platelets via an ITGB3-
dependent pathway. Maternal fibrinogen is essential for successful
pregnancy. Fibrin deposition is also associated with infection,
where it protects against IFNG-mediated hemorrhage. May also
facilitate the immune response via both innate and T-cell mediated
pathways. {ECO:0000250|UniProtKB:E9PV24}.
-!- 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. {ECO:0000269|PubMed:518846,
ECO:0000269|PubMed:741445, ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:936108, ECO:0000269|PubMed:9628725,
ECO:0000269|PubMed:9689040}.
-!- INTERACTION:
P02647:APOA1; NbExp=2; IntAct=EBI-348571, EBI-701692;
Q8IXL6:FAM20C; NbExp=2; IntAct=EBI-348571, EBI-7147442;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9628725}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha-E;
IsoId=P02671-1; Sequence=Displayed;
Name=2; Synonyms=Alpha;
IsoId=P02671-2; Sequence=VSP_001531, VSP_001532;
Note=Ref.3 (AAK31372) sequence is in conflict in positions:
640:PSLSP->LPCPPRLS. {ECO:0000305};
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
{ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
-!- 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. {ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9628725, ECO:0000305}.
-!- PTM: The alpha chain is normally not N-glycosylated
(PubMed:23151259), even though glycosylation at Asn-686 was
observed when a fragment of the protein was expressed in insect
cells (PubMed:9689040). It is well known that heterologous
expression of isolated domains can lead to adventitious protein
modifications. Besides, glycosylation at Asn-686 is supported by
large-scale glycoproteomics studies (PubMed:16335952 and
PubMed:19159218), but the evidence is still quite tenuous. Most
likely, Asn-686 is not glycosylated in the healthy human body, or
only with low efficiency. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23151259,
ECO:0000269|PubMed:9689040, ECO:0000305}.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:23050552}.
-!- PTM: Forms F13A-mediated cross-links between a glutamine and the
epsilon-amino group of a lysine residue, forming fibronectin-
fibrinogen heteropolymers.
-!- PTM: About one-third of the alpha chains in the molecules in blood
were found to be phosphorylated.
-!- 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. {ECO:0000269|PubMed:2143188}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare
autosomal recessive disorder is characterized by bleeding that
varies from mild to severe and by complete absence or extremely
low levels of plasma and platelet fibrinogen.
{ECO:0000269|PubMed:25427968}. Note=The disease is caused by
mutations affecting the gene represented in this entry. The
majority of cases of afibrinogenemia are due to truncating
mutations. Variations in position Arg-35 (the site of cleavage of
fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.
-!- DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A form of hereditary
generalized amyloidosis. Clinical features include extensive
visceral amyloid deposits, renal amyloidosis resulting in
nephrotic syndrome, arterial hypertension, hepatosplenomegaly,
cholestasis, petechial skin rash. There is no involvement of the
nervous system. {ECO:0000269|PubMed:8097946}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A
disorder characterized by qualitative abnormalities
(dysfibrinogenemia) of the circulating fibrinogen. Affected
individuals are frequently asymptomatic, but some patients have
bleeding diathesis, thromboembolic complications, or both. In some
cases, dysfibrinogenemia is associated with low circulating
fibrinogen levels (hypodysfibrinogenemia).
{ECO:0000269|PubMed:16846481, ECO:0000269|PubMed:8473507}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=FGA";
-!- WEB RESOURCE: Name=Wikipedia; Note=Fibrinogen entry;
URL="https://en.wikipedia.org/wiki/Fibrinogen";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/fga/";
-----------------------------------------------------------------------
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EMBL; M64982; AAA17056.1; -; Genomic_DNA.
EMBL; M64982; AAA17055.1; -; Genomic_DNA.
EMBL; M58569; AAC97142.1; -; Transcribed_RNA.
EMBL; M58569; AAC97143.1; -; Transcribed_RNA.
EMBL; AF361104; AAK31372.1; -; Genomic_DNA.
EMBL; AF361104; AAK31373.1; -; Genomic_DNA.
EMBL; AK290559; BAF83248.1; -; mRNA.
EMBL; CH471056; EAX04925.1; -; Genomic_DNA.
EMBL; CH471056; EAX04926.1; -; Genomic_DNA.
EMBL; CH471056; EAX04927.1; -; Genomic_DNA.
EMBL; CH471056; EAX04928.1; -; Genomic_DNA.
EMBL; BC098280; AAH98280.1; -; mRNA.
EMBL; BC099706; AAH99706.1; -; mRNA.
EMBL; BC099720; AAH99720.1; -; mRNA.
EMBL; BC101935; AAI01936.1; -; mRNA.
EMBL; J00128; AAA52427.1; -; mRNA.
EMBL; J00127; AAA52426.1; -; mRNA.
EMBL; K02272; AAA52428.1; -; mRNA.
EMBL; M26878; AAA52444.1; -; mRNA.
CCDS; CCDS3787.1; -. [P02671-1]
CCDS; CCDS47152.1; -. [P02671-2]
PIR; A93956; FGHUA.
PIR; D44234; D44234.
RefSeq; NP_000499.1; NM_000508.4. [P02671-1]
RefSeq; NP_068657.1; NM_021871.3. [P02671-2]
UniGene; Hs.351593; -.
UniGene; Hs.612036; -.
PDB; 1BBR; X-ray; 2.30 A; F/G/I=26-35.
PDB; 1DM4; X-ray; 2.50 A; C=26-35.
PDB; 1FPH; X-ray; 2.50 A; F=26-35.
PDB; 1FZA; X-ray; 2.90 A; A/D=130-216.
PDB; 1FZB; X-ray; 2.90 A; A/D=130-216.
PDB; 1FZC; X-ray; 2.30 A; A/D=130-216.
PDB; 1FZD; X-ray; 2.10 A; A/B/C/D/E/F/G/H=666-866.
PDB; 1FZE; X-ray; 3.00 A; A/D=130-216.
PDB; 1FZF; X-ray; 2.70 A; A/D=130-216.
PDB; 1FZG; X-ray; 2.50 A; A/D=130-216.
PDB; 1LT9; X-ray; 2.80 A; A/D=145-210.
PDB; 1LTJ; X-ray; 2.80 A; A/D=145-210.
PDB; 1N86; X-ray; 3.20 A; A/D=130-216.
PDB; 1N8E; X-ray; 4.50 A; A/D=130-218.
PDB; 1RE3; X-ray; 2.45 A; A/D=145-210.
PDB; 1RE4; X-ray; 2.70 A; A/D=145-210.
PDB; 1RF0; X-ray; 2.81 A; A/D=145-210.
PDB; 1RF1; X-ray; 2.53 A; A/D=145-210.
PDB; 1YCP; X-ray; 2.50 A; F/N=20-42.
PDB; 2A45; X-ray; 3.65 A; G/J=36-92.
PDB; 2FFD; X-ray; 2.89 A; A/D=145-210.
PDB; 2H43; X-ray; 2.70 A; A/D=130-216.
PDB; 2HLO; X-ray; 2.60 A; A/D=130-216.
PDB; 2HOD; X-ray; 2.90 A; A/D/G/J=130-216.
PDB; 2HPC; X-ray; 2.90 A; A/D/G/J=130-216.
PDB; 2OYH; X-ray; 2.40 A; A/D=145-210.
PDB; 2OYI; X-ray; 2.70 A; A/D=145-210.
PDB; 2Q9I; X-ray; 2.80 A; A/D=130-216.
PDB; 2XNX; X-ray; 3.30 A; A/D/G/J=130-216.
PDB; 2XNY; X-ray; 7.50 A; A/D=130-216.
PDB; 2Z4E; X-ray; 2.70 A; A/D=130-216.
PDB; 3AT0; X-ray; 2.50 A; B=332-347.
PDB; 3BVH; X-ray; 2.60 A; A/D=148-209.
PDB; 3E1I; X-ray; 2.30 A; A/D=130-216.
PDB; 3GHG; X-ray; 2.90 A; A/D/G/J=20-581.
PDB; 3H32; X-ray; 3.60 A; A/D=20-216.
PDB; 3HUS; X-ray; 3.04 A; A/D=145-210.
PDB; 4F27; X-ray; 1.92 A; Q=336-347.
PDB; 5CFA; X-ray; 1.45 A; C/D=580-594.
PDBsum; 1BBR; -.
PDBsum; 1DM4; -.
PDBsum; 1FPH; -.
PDBsum; 1FZA; -.
PDBsum; 1FZB; -.
PDBsum; 1FZC; -.
PDBsum; 1FZD; -.
PDBsum; 1FZE; -.
PDBsum; 1FZF; -.
PDBsum; 1FZG; -.
PDBsum; 1LT9; -.
PDBsum; 1LTJ; -.
PDBsum; 1N86; -.
PDBsum; 1N8E; -.
PDBsum; 1RE3; -.
PDBsum; 1RE4; -.
PDBsum; 1RF0; -.
PDBsum; 1RF1; -.
PDBsum; 1YCP; -.
PDBsum; 2A45; -.
PDBsum; 2FFD; -.
PDBsum; 2H43; -.
PDBsum; 2HLO; -.
PDBsum; 2HOD; -.
PDBsum; 2HPC; -.
PDBsum; 2OYH; -.
PDBsum; 2OYI; -.
PDBsum; 2Q9I; -.
PDBsum; 2XNX; -.
PDBsum; 2XNY; -.
PDBsum; 2Z4E; -.
PDBsum; 3AT0; -.
PDBsum; 3BVH; -.
PDBsum; 3E1I; -.
PDBsum; 3GHG; -.
PDBsum; 3H32; -.
PDBsum; 3HUS; -.
PDBsum; 4F27; -.
PDBsum; 5CFA; -.
ProteinModelPortal; P02671; -.
SMR; P02671; -.
BioGrid; 108534; 29.
CORUM; P02671; -.
DIP; DIP-29643N; -.
IntAct; P02671; 19.
MINT; MINT-1033042; -.
STRING; 9606.ENSP00000306361; -.
ChEMBL; CHEMBL2364709; -.
DrugBank; DB04919; Alfimeprase.
DrugBank; DB00009; Alteplase.
DrugBank; DB05099; Ancrod.
DrugBank; DB00029; Anistreplase.
DrugBank; DB05675; EP-2104R.
DrugBank; DB00015; Reteplase.
DrugBank; DB00364; Sucralfate.
DrugBank; DB00031; Tenecteplase.
iPTMnet; P02671; -.
PhosphoSitePlus; P02671; -.
SwissPalm; P02671; -.
UniCarbKB; P02671; -.
BioMuta; FGA; -.
DMDM; 1706799; -.
OGP; P02671; -.
SWISS-2DPAGE; P02671; -.
MaxQB; P02671; -.
PaxDb; P02671; -.
PeptideAtlas; P02671; -.
PRIDE; P02671; -.
DNASU; 2243; -.
Ensembl; ENST00000302053; ENSP00000306361; ENSG00000171560. [P02671-1]
Ensembl; ENST00000403106; ENSP00000385981; ENSG00000171560. [P02671-2]
GeneID; 2243; -.
KEGG; hsa:2243; -.
UCSC; uc003iod.2; human. [P02671-1]
CTD; 2243; -.
DisGeNET; 2243; -.
EuPathDB; HostDB:ENSG00000171560.14; -.
GeneCards; FGA; -.
HGNC; HGNC:3661; FGA.
HPA; CAB016776; -.
HPA; HPA051370; -.
HPA; HPA064755; -.
MalaCards; FGA; -.
MIM; 105200; phenotype.
MIM; 134820; gene+phenotype.
MIM; 202400; phenotype.
MIM; 616004; phenotype.
neXtProt; NX_P02671; -.
OpenTargets; ENSG00000171560; -.
Orphanet; 98880; Familial afibrinogenemia.
Orphanet; 98881; Familial dysfibrinogenemia.
Orphanet; 248408; Familial hypodysfibrinogenemia.
Orphanet; 101041; Familial hypofibrinogenemia.
Orphanet; 93562; Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
PharmGKB; PA429; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00830000128240; -.
HOGENOM; HOG000285947; -.
HOVERGEN; HBG005668; -.
InParanoid; P02671; -.
KO; K03903; -.
OMA; PGSTGTW; -.
OrthoDB; EOG091G03M1; -.
PhylomeDB; P02671; -.
TreeFam; TF351984; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; P02671; -.
ChiTaRS; FGA; human.
EvolutionaryTrace; P02671; -.
GeneWiki; Fibrinogen_alpha_chain; -.
GenomeRNAi; 2243; -.
PMAP-CutDB; P02671; -.
PRO; PR:P02671; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000171560; -.
CleanEx; HS_FGA; -.
ExpressionAtlas; P02671; baseline and differential.
Genevisible; P02671; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005577; C:fibrinogen complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031091; C:platelet alpha granule; IDA:BHF-UCL.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; IEA:InterPro.
GO; GO:0005102; F:receptor binding; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IDA:BHF-UCL.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0072377; P:blood coagulation, common pathway; IMP:BHF-UCL.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0043623; P:cellular protein complex assembly; IDA:BHF-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
GO; GO:0043152; P:induction of bacterial agglutination; IDA:CACAO.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:2000261; P:negative regulation of blood coagulation, common pathway; TAS:BHF-UCL.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0045921; P:positive regulation of exocytosis; IDA:BHF-UCL.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; NAS:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; IMP:UniProtKB.
GO; GO:0051258; P:protein polymerization; IDA:BHF-UCL.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
CDD; cd00087; FReD; 1.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR021996; Fibrinogen_aC.
InterPro; IPR020837; Fibrinogen_CS.
Pfam; PF08702; Fib_alpha; 1.
Pfam; PF12160; Fibrinogen_aC; 1.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SMART; SM01212; Fib_alpha; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00514; FIBRINOGEN_C_1; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Amyloid;
Amyloidosis; Blood coagulation; Calcium; Coiled coil;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Hemostasis; Hydroxylation; Immunity;
Innate immunity; Isopeptide bond; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:518846,
ECO:0000269|Ref.10, ECO:0000269|Ref.14}.
PEPTIDE 20 35 Fibrinopeptide A.
/FTId=PRO_0000009021.
CHAIN 36 866 Fibrinogen alpha chain.
/FTId=PRO_0000009022.
DOMAIN 623 864 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
REGION 36 38 Alpha-chain polymerization, binding
distal domain of another fibrin gamma
chain.
COILED 68 631 {ECO:0000305|PubMed:19296670}.
METAL 791 791 Calcium. {ECO:0000244|PDB:1FZD,
ECO:0000269|PubMed:9689040}.
METAL 793 793 Calcium. {ECO:0000244|PDB:1FZD,
ECO:0000269|PubMed:9689040}.
METAL 795 795 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1FZD,
ECO:0000269|PubMed:9689040}.
METAL 797 797 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1FZD,
ECO:0000269|PubMed:9689040}.
SITE 35 36 Cleavage; by thrombin; to release
fibrinopeptide A.
SITE 100 101 Cleavage; by plasmin; to break down
fibrin clots.
SITE 121 122 Cleavage; by hementin; to prevent blood
coagulation.
SITE 123 124 Cleavage; by plasmin; to break down
fibrin clots.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:16807684}.
MOD_RES 45 45 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 56 56 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 364 364 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 412 412 Phosphothreonine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:24275569}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 501 501 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 505 505 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 524 524 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 560 560 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 565 565 4-hydroxyproline; by P4HA1.
{ECO:0000269|PubMed:19696023}.
MOD_RES 609 609 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
CARBOHYD 320 320 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23050552}.
CARBOHYD 351 351 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:23050552}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine; in
variant Caracas-2.
{ECO:0000269|PubMed:1675636}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9689040}.
DISULFID 47 47 Interchain.
{ECO:0000269|PubMed:19296670}.
DISULFID 55 55 Interchain (with C-95 in beta chain).
{ECO:0000269|PubMed:19296670}.
DISULFID 64 64 Interchain (with C-49 in gamma chain).
{ECO:0000269|PubMed:19296670}.
DISULFID 68 68 Interchain (with C-106 in beta chain).
{ECO:0000269|PubMed:19296670}.
DISULFID 180 180 Interchain (with C-165 in gamma chain).
{ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:741445,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
DISULFID 184 184 Interchain (with C-223 in beta chain).
{ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:741445,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
DISULFID 461 491 {ECO:0000250|UniProtKB:P02672}.
DISULFID 799 812 {ECO:0000244|PDB:1FZD,
ECO:0000269|PubMed:9689040}.
CROSSLNK 322 322 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-41 in alpha-2-
antiplasmin).
CROSSLNK 347 347 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-?).
CROSSLNK 385 385 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-?).
CROSSLNK 527 527 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-?). {ECO:0000255}.
CROSSLNK 558 558 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-?). {ECO:0000255}.
CROSSLNK 575 575 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-?). {ECO:0000255}.
CROSSLNK 581 581 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-?). {ECO:0000255}.
CROSSLNK 599 599 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-?). {ECO:0000255}.
VAR_SEQ 631 644 DCDDVLQTHPSGTQ -> GIHTSPLGKPSLSP (in
isoform 2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:6575389}.
/FTId=VSP_001531.
VAR_SEQ 645 866 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:6575389}.
/FTId=VSP_001532.
VARIANT 6 6 I -> V (in dbSNP:rs2070025).
{ECO:0000269|Ref.3}.
/FTId=VAR_011609.
VARIANT 26 26 D -> N (in Lille-1; dbSNP:rs121909604).
/FTId=VAR_002390.
VARIANT 31 31 G -> V (in Rouen-1; dbSNP:rs121909605).
/FTId=VAR_002391.
VARIANT 35 35 R -> C (in DYSFIBRIN; fibrinogen Metz 1/
Hershey III; dbSNP:rs121909606).
{ECO:0000269|PubMed:16846481}.
/FTId=VAR_002392.
VARIANT 35 35 R -> H (in dbSNP:rs121909607).
{ECO:0000269|PubMed:8461606}.
/FTId=VAR_002393.
VARIANT 37 37 P -> L (in Kyoto-2; dbSNP:rs121909609).
{ECO:0000269|PubMed:2070049}.
/FTId=VAR_002394.
VARIANT 38 38 R -> G (in Aarhus-1; dbSNP:rs121909608).
/FTId=VAR_002397.
VARIANT 38 38 R -> N (in Munich-1; requires 2
nucleotide substitutions).
/FTId=VAR_002395.
VARIANT 38 38 R -> S (in Detroit-1).
/FTId=VAR_002396.
VARIANT 39 39 V -> D (in Canterbury;
dbSNP:rs121909614).
{ECO:0000269|PubMed:8675656}.
/FTId=VAR_010730.
VARIANT 55 55 C -> R (in CAFBN; hypofibrinogenemia;
heterozygous; decreased fibrinogen
complex assembly; no effect on fibrinogen
complex secretion).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072721.
VARIANT 66 66 S -> T.
/FTId=VAR_002398.
VARIANT 129 129 R -> P (in CAFBN; hypofibrinogenemia;
heterozygous; no effect on fibrinogen
complex assembly; no effect on fibrinogen
complex secretion).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072722.
VARIANT 160 160 R -> S (in Lima).
{ECO:0000269|PubMed:1634621}.
/FTId=VAR_002399.
VARIANT 184 184 C -> W (in CAFBN; hypofibrinogenemia;
heterozygous; impaired fibrinogen complex
assembly). {ECO:0000269|PubMed:25427968}.
/FTId=VAR_072723.
VARIANT 331 331 T -> A (in dbSNP:rs6050).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.3}.
/FTId=VAR_011610.
VARIANT 446 446 K -> E (in dbSNP:rs6052).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014168.
VARIANT 453 453 S -> N (in Caracas-2; dbSNP:rs121909610).
{ECO:0000269|PubMed:1675636}.
/FTId=VAR_002400.
VARIANT 456 456 T -> A (in dbSNP:rs2070031).
{ECO:0000269|Ref.3}.
/FTId=VAR_011611.
VARIANT 545 545 E -> V (in AMYL8; dbSNP:rs121909612).
/FTId=VAR_010731.
VARIANT 573 573 R -> C (in DYSFIBRIN; fibrinogen Dusart/
Paris-5; dbSNP:rs121909613).
{ECO:0000269|PubMed:8473507}.
/FTId=VAR_002401.
VARIANT 573 573 R -> L (in AMYL8; dbSNP:rs78506343).
{ECO:0000269|PubMed:8097946}.
/FTId=VAR_010732.
CONFLICT 177 177 I -> V (in Ref. 4; BAF83248).
{ECO:0000305}.
CONFLICT 215 216 SR -> RS (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 299 299 S -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 304 304 S -> G (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 317 318 GT -> SG (in Ref. 11; AA sequence).
{ECO:0000305}.
TURN 27 31 {ECO:0000244|PDB:1BBR}.
STRAND 57 60 {ECO:0000244|PDB:3GHG}.
STRAND 63 65 {ECO:0000244|PDB:3GHG}.
HELIX 67 92 {ECO:0000244|PDB:3GHG}.
HELIX 94 111 {ECO:0000244|PDB:3GHG}.
HELIX 116 129 {ECO:0000244|PDB:3GHG}.
TURN 133 135 {ECO:0000244|PDB:1FZA}.
TURN 139 141 {ECO:0000244|PDB:1FZC}.
HELIX 142 178 {ECO:0000244|PDB:1FZC}.
TURN 179 183 {ECO:0000244|PDB:1FZC}.
STRAND 184 186 {ECO:0000244|PDB:1RE3}.
HELIX 195 209 {ECO:0000244|PDB:1FZC}.
TURN 226 228 {ECO:0000244|PDB:3GHG}.
STRAND 337 343 {ECO:0000244|PDB:4F27}.
STRAND 582 587 {ECO:0000244|PDB:5CFA}.
STRAND 673 681 {ECO:0000244|PDB:1FZD}.
HELIX 689 694 {ECO:0000244|PDB:1FZD}.
HELIX 711 718 {ECO:0000244|PDB:1FZD}.
STRAND 723 729 {ECO:0000244|PDB:1FZD}.
STRAND 735 744 {ECO:0000244|PDB:1FZD}.
TURN 747 751 {ECO:0000244|PDB:1FZD}.
STRAND 753 762 {ECO:0000244|PDB:1FZD}.
TURN 765 768 {ECO:0000244|PDB:1FZD}.
TURN 771 773 {ECO:0000244|PDB:1FZD}.
HELIX 775 778 {ECO:0000244|PDB:1FZD}.
STRAND 793 797 {ECO:0000244|PDB:1FZD}.
HELIX 799 803 {ECO:0000244|PDB:1FZD}.
STRAND 810 812 {ECO:0000244|PDB:1FZD}.
STRAND 814 816 {ECO:0000244|PDB:1FZD}.
STRAND 823 826 {ECO:0000244|PDB:1FZD}.
HELIX 829 831 {ECO:0000244|PDB:1FZD}.
STRAND 840 843 {ECO:0000244|PDB:1FZD}.
HELIX 844 847 {ECO:0000244|PDB:1FZD}.
STRAND 854 861 {ECO:0000244|PDB:1FZD}.
SEQUENCE 866 AA; 94973 MW; EA73A81204D8AEC4 CRC64;
MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS DWPFCSDEDW
NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK DSHSLTTNIM EILRGDFSSA
NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC
RGSCSRALAR EVDLKDYEDQ QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ
LQKVPPEWKA LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS
GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG SPRPGSTGTW
NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS GNARPNNPDW GTFEEVSGNV
SPGTRREYHT EKLVTSKGDK ELRTGKEKVT SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK
EVVTSEDGSD CPEAMDLGTL SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF
VSETESRGSE SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS
YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI KLPGSSKIFS
VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN DEGEGEFWLG NDYLHLLTQR
GSVLRVELED WAGNEAYAEY HFRVGSEAEG YALQVSSYEG TAGDALIEGS VEEGAEYTSH
NNMQFSTFDR DADQWEENCA EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG
VVWVSFRGAD YSLRAVRMKI RPLVTQ


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