FIBB_HUMAN
ID FIBB_HUMAN Reviewed; 491 AA.
AC P02675; A0JLR9; B2R7G3; Q32Q65; Q3KPF2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 244.
DE RecName: Full=Fibrinogen beta chain;
DE Contains:
DE RecName: Full=Fibrinopeptide B;
DE Contains:
DE RecName: Full=Fibrinogen beta chain;
DE Flags: Precursor;
GN Name=FGB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=6688356; DOI=10.1021/bi00282a032;
RA Chung D.W., Que B.G., Rixon M.W., Mace M. Jr., Davie E.W.;
RT "Characterization of complementary deoxyribonucleic acid and genomic
RT deoxyribonucleic acid for the beta chain of human fibrinogen.";
RL Biochemistry 22:3244-3250(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2102623; DOI=10.1007/978-1-4615-3806-6_3;
RA Chung D.W., Harris J.E., Davie E.W.;
RT "Nucleotide sequences of the three genes coding for human fibrinogen.";
RL Adv. Exp. Med. Biol. 281:39-48(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chung D.W., Harris J.E., Davie E.W.;
RT "Nucleotide sequences of the three genes coding for human fibrinogen.";
RL (In) Liu C.Y., Chien S. (eds.);
RL Fibrinogen, thrombosis, coagulation and fibrinolysis, pp.39-48, Plenum
RL Press, New York (1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-100; HIS-170; LEU-265
RP AND LYS-478.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
RX PubMed=6575700; DOI=10.1111/j.1749-6632.1983.tb23265.x;
RA Chung D.W., Rixon M.W., Que B.G., Davie E.W.;
RT "Cloning of fibrinogen genes and their cDNA.";
RL Ann. N. Y. Acad. Sci. 408:449-456(1983).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RX PubMed=3029722; DOI=10.1093/nar/15.4.1615;
RA Huber P., Dalmon J., Courtois G., Laurent M., Assouline Z., Marguerie G.;
RT "Characterization of the 5'-flanking region for the human fibrinogen beta
RT gene.";
RL Nucleic Acids Res. 15:1615-1625(1987).
RN [10]
RP PROTEIN SEQUENCE OF 31-491, AND PYROGLUTAMATE FORMATION AT GLN-31.
RX PubMed=420779; DOI=10.1021/bi00568a011;
RA Watt K.W.K., Takagi T., Doolittle R.F.;
RT "Amino acid sequence of the beta chain of human fibrinogen.";
RL Biochemistry 18:68-76(1979).
RN [11]
RP PROTEIN SEQUENCE OF 31-491, AND GLYCOSYLATION AT ASN-394.
RA Henschen A., Lottspeich F., Southan C., Topfer-Petersen E.;
RT "Human fibrinogen: sequence, sulfur bridges, glycosylation and some
RT structural variants.";
RL (In) Peeters H. (eds.);
RL Protides of the biological fluids, Proc. 28th colloquium, pp.51-56,
RL Pergamon Press, Oxford (1980).
RN [12]
RP PROTEIN SEQUENCE OF 31-148, AND DISULFIDE BONDS.
RX PubMed=936108; DOI=10.1016/0049-3848(76)90245-0;
RA Blombaeck B., Hessel B., Hogg D.;
RT "Disulfide bridges in NH2-terminal part of human fibrinogen.";
RL Thromb. Res. 8:639-658(1976).
RN [13]
RP PROTEIN SEQUENCE OF 31-44.
RA Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M.;
RT "Studies on fibrinopeptides from primates.";
RL Acta Chem. Scand. 19:1788-1789(1965).
RN [14]
RP PROTEIN SEQUENCE OF 45-53.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [15]
RP PROTEIN SEQUENCE OF 54-72; 164-178 AND 225-239, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [16]
RP REVIEW, AND DISULFIDE BONDS.
RX PubMed=6575689; DOI=10.1111/j.1749-6632.1983.tb23232.x;
RA Henschen A., Lottspeich F., Kehl M., Southan C.;
RT "Covalent structure of fibrinogen.";
RL Ann. N. Y. Acad. Sci. 408:28-43(1983).
RN [17]
RP DISULFIDE BONDS.
RX PubMed=891553; DOI=10.1111/j.1432-1033.1977.tb11704.x;
RA Gaardlund B., Hessel B., Marguerie G., Murano G., Blombaeck B.;
RT "Primary structure of human fibrinogen. Characterization of disulfide-
RT containing cyanogen-bromide fragments.";
RL Eur. J. Biochem. 77:595-610(1977).
RN [18]
RP DISULFIDE BONDS.
RA Doolittle R.F., Takagi T., Watt K.W.K., Bouma H. III, Cottrell B.A.,
RA Cassman K.G., Goldbaum D.M., Doolittle L.R., Friezner S.J.;
RT "The structures of fibrinogen and fibrin.";
RL (In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H. (eds.);
RL Regulatory proteolytic enzymes and their inhibitors, pp.163-172, Pergamon
RL Press, New York (1978).
RN [19]
RP REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, AND LIGANDS.
RX PubMed=6383194; DOI=10.1146/annurev.bi.53.070184.001211;
RA Doolittle R.F.;
RT "Fibrinogen and fibrin.";
RL Annu. Rev. Biochem. 53:195-229(1984).
RN [20]
RP INTERACTION WITH FBLN1.
RX PubMed=7642629; DOI=10.1074/jbc.270.33.19458;
RA Tran H., Tanaka A., Litvinovich S.V., Medved L.V., Haudenschild C.C.,
RA Argraves W.S.;
RT "The interaction of fibulin-1 with fibrinogen. A potential role in
RT hemostasis and thrombosis.";
RL J. Biol. Chem. 270:19458-19464(1995).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [22]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [23]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [24]
RP CLEAVAGE BY HEMENTIN AND PLASMIN.
RX PubMed=2143188; DOI=10.1016/s0021-9258(18)77401-2;
RA Kirschbaum N.E., Budzynski A.Z.;
RT "A unique proteolytic fragment of human fibrinogen containing the A alpha
RT COOH-terminal domain of the native molecule.";
RL J. Biol. Chem. 265:13669-13676(1990).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 164-491, DISULFIDE BONDS, AND
RP SUBUNIT.
RX PubMed=9333233; DOI=10.1038/38947;
RA Spraggon G., Everse S.J., Doolittle R.F.;
RT "Crystal structures of fragment D from human fibrinogen and its crosslinked
RT counterpart from fibrin.";
RL Nature 389:455-462(1997).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 164-491 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-394, SUBUNIT, COILED COIL DOMAIN,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9628725; DOI=10.1021/bi9804129;
RA Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F.;
RT "Crystal structure of fragment double-D from human fibrin with two
RT different bound ligands.";
RL Biochemistry 37:8637-8642(1998).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 164-491 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-394, SUBUNIT, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND COILED COIL DOMAIN.
RX PubMed=10074346; DOI=10.1021/bi982626w;
RA Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F.;
RT "Conformational changes in fragments D and double-D from human fibrin(ogen)
RT upon binding the peptide ligand Gly-His-Arg-Pro-amide.";
RL Biochemistry 38:2941-2946(1999).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-491 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-394, SUBUNIT, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND COILED COIL DOMAIN.
RX PubMed=19296670; DOI=10.1021/bi802205g;
RA Kollman J.M., Pandi L., Sawaya M.R., Riley M., Doolittle R.F.;
RT "Crystal structure of human fibrinogen.";
RL Biochemistry 48:3877-3886(2009).
RN [31]
RP VARIANT BALTIMORE-2 LYS-478.
RX PubMed=3194892; DOI=10.1016/0049-3848(88)90096-5;
RA Schmelzer C.H., Ebert R.F., Bell W.R.;
RT "A polymorphism at B beta 448 of fibrinogen identified during structural
RT studies of fibrinogen Baltimore II.";
RL Thromb. Res. 52:173-177(1988).
RN [32]
RP VARIANT ISE ARG-45.
RX PubMed=2018836;
RA Yoshida N., Wada H., Morita K., Hirata H., Matsuda M., Yamazumi K.,
RA Asakura S., Shirakawa S.;
RT "A new congenital abnormal fibrinogen Ise characterized by the replacement
RT of B beta glycine-15 by cysteine.";
RL Blood 77:1958-1963(1991).
RN [33]
RP INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN THR-98.
RX PubMed=1634610; DOI=10.1172/jci115841;
RA Koopman J., Haverkate F., Lord S.T., Grimbergen J., Mannucci P.M.;
RT "Molecular basis of fibrinogen Naples associated with defective thrombin
RT binding and thrombophilia. Homozygous substitution of B beta 68
RT Ala-->Thr.";
RL J. Clin. Invest. 90:238-244(1992).
RN [34]
RP VARIANTS IJMUIDEN CYS-44 AND NIJMEGEN CYS-74.
RX PubMed=1565641; DOI=10.1073/pnas.89.8.3478;
RA Koopman J., Haverkate F., Grimbergen J., Engesser L., Novakova I.,
RA Kerst A.F.J.A., Lord S.T.;
RT "Abnormal fibrinogens IJmuiden (B beta Arg14-->Cys) and Nijmegen (B beta
RT Arg44-->Cys) form disulfide-linked fibrinogen-albumin complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3478-3482(1992).
RN [35]
RP VARIANT NEW YORK-1 39-GLY--LEU-102 DEL.
RX PubMed=3156856; DOI=10.1016/s0021-9258(18)89277-8;
RA Liu C.Y., Koehn J.A., Morgan F.J.;
RT "Characterization of fibrinogen New York 1. A dysfunctional fibrinogen with
RT a deletion of B beta(9-72) corresponding exactly to exon 2 of the gene.";
RL J. Biol. Chem. 260:4390-4396(1985).
RN [36]
RP VARIANTS GLU-2; LEU-265 AND LYS-478.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [37]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [38]
RP VARIANTS CAFBN ARG-383 AND ASP-430.
RX PubMed=10666208;
RA Duga S., Asselta R., Santagostino E., Zeinali S., Simonic T., Malcovati M.,
RA Mannucci P.M., Tenchini M.L.;
RT "Missense mutations in the human beta fibrinogen gene cause congenital
RT afibrinogenemia by impairing fibrinogen secretion.";
RL Blood 95:1336-1341(2000).
RN [39]
RP VARIANT CAFBN CYS-196.
RX PubMed=11468164; DOI=10.1182/blood.v98.3.661;
RA Lounes K.C., Lefkowitz J.B., Henschen-Edman A.H., Coates A.I.,
RA Hantgan R.R., Lord S.T.;
RT "The impaired polymerization of fibrinogen Longmont (Bbeta166Arg-->Cys) is
RT not improved by removal of disulfide-linked dimers from a mixture of dimers
RT and cysteine-linked monomers.";
RL Blood 98:661-666(2001).
RN [40]
RP VARIANT CAFBN GLN-202.
RX PubMed=15070683; DOI=10.1182/blood-2003-10-3725;
RA Asselta R., Duga S., Spena S., Peyvandi F., Castaman G., Malcovati M.,
RA Mannucci P.M., Tenchini M.L.;
RT "Missense or splicing mutation? The case of a fibrinogen Bbeta-chain
RT mutation causing severe hypofibrinogenemia.";
RL Blood 103:3051-3054(2004).
RN [41]
RP VARIANTS CAFBN ARG-95 AND LYS-407, AND CHARACTERIZATION OF VARIANTS CAFBN
RP ARG-95 AND LYS-407.
RX PubMed=25427968; DOI=10.1160/th14-07-0629;
RA Asselta R., Plate M., Robusto M., Borhany M., Guella I., Solda G.,
RA Afrasiabi A., Menegatti M., Shamsi T., Peyvandi F., Duga S.;
RT "Clinical and molecular characterisation of 21 patients affected by
RT quantitative fibrinogen deficiency.";
RL Thromb. Haemost. 113:567-576(2015).
CC -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG),
CC polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC function in hemostasis as one of the primary components of blood clots.
CC In addition, functions during the early stages of wound repair to
CC stabilize the lesion and guide cell migration during re-
CC epithelialization. Was originally thought to be essential for platelet
CC aggregation, based on in vitro studies using anticoagulated blood.
CC However subsequent studies have shown that it is not absolutely
CC required for thrombus formation in vivo. Enhances expression of SELP in
CC activated platelets. Maternal fibrinogen is essential for successful
CC pregnancy. Fibrin deposition is also associated with infection, where
CC it protects against IFNG-mediated hemorrhage. May also facilitate the
CC antibacterial immune response via both innate and T-cell mediated
CC pathways. {ECO:0000250|UniProtKB:E9PV24}.
CC -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC head to head conformation with the N-termini in a small central domain.
CC {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670,
CC ECO:0000269|PubMed:9333233, ECO:0000269|PubMed:9628725}.
CC -!- INTERACTION:
CC P02675; PRO_0000037566 [P27958]; Xeno; NbExp=4; IntAct=EBI-1034445, EBI-6377335;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10074346,
CC ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
CC {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670,
CC ECO:0000269|PubMed:9628725}.
CC -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains
CC connects the central nodule to the C-terminal domains (distal nodules).
CC The long C-terminal ends of the alpha chains fold back, contributing a
CC fourth strand to the coiled coil structure.
CC {ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670,
CC ECO:0000269|PubMed:9628725}.
CC -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which
CC cleaves fibrinopeptides A and B from alpha and beta chains, and thus
CC exposes the N-terminal polymerization sites responsible for the
CC formation of the soft clot. The soft clot is converted into the hard
CC clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine
CC cross-linking between gamma chains (stronger) and between alpha chains
CC (weaker) of different monomers. {ECO:0000269|PubMed:2143188}.
CC -!- DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare
CC autosomal recessive disorder is characterized by bleeding that varies
CC from mild to severe and by complete absence or extremely low levels of
CC plasma and platelet fibrinogen. {ECO:0000269|PubMed:10666208,
CC ECO:0000269|PubMed:11468164, ECO:0000269|PubMed:15070683,
CC ECO:0000269|PubMed:25427968}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Patients with congenital
CC fibrinogen abnormalities can manifest different clinical pictures. Some
CC cases are clinically silent, some show a tendency toward bleeding and
CC some show a predisposition for thrombosis with or without bleeding.
CC -!- DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A
CC disorder characterized by qualitative abnormalities (dysfibrinogenemia)
CC of the circulating fibrinogen. Affected individuals are frequently
CC asymptomatic, but some patients have bleeding diathesis, thromboembolic
CC complications, or both. In some cases, dysfibrinogenemia is associated
CC with low circulating fibrinogen levels (hypodysfibrinogenemia).
CC {ECO:0000269|PubMed:1634610}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07030.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Fibrinogen entry;
CC URL="https://en.wikipedia.org/wiki/Fibrinogen";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/fgb/";
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DR EMBL; J00129; AAA52429.1; -; mRNA.
DR EMBL; J00131; AAA98115.1; -; Genomic_DNA.
DR EMBL; J00130; AAA98115.1; JOINED; Genomic_DNA.
DR EMBL; J00132; AAA98116.1; -; Genomic_DNA.
DR EMBL; J00133; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M64983; AAA18024.2; -; Genomic_DNA.
DR EMBL; AF388026; AAK62470.1; -; Genomic_DNA.
DR EMBL; AK312972; BAG35810.1; -; mRNA.
DR EMBL; CH471056; EAX04932.1; -; Genomic_DNA.
DR EMBL; BC007030; AAH07030.1; ALT_SEQ; mRNA.
DR EMBL; BC106760; AAI06761.1; -; mRNA.
DR EMBL; BC107766; AAI07767.1; -; mRNA.
DR EMBL; AH002694; AAA52445.1; -; Genomic_DNA.
DR EMBL; X05018; CAA28674.1; -; Genomic_DNA.
DR CCDS; CCDS3786.1; -.
DR PIR; B43568; FGHUB.
DR RefSeq; NP_001171670.1; NM_001184741.1.
DR RefSeq; NP_005132.2; NM_005141.4.
DR PDB; 1FZA; X-ray; 2.90 A; B/E=164-491.
DR PDB; 1FZB; X-ray; 2.90 A; B/E=164-491.
DR PDB; 1FZC; X-ray; 2.30 A; B/E=164-491.
DR PDB; 1FZE; X-ray; 3.00 A; B/E=164-491.
DR PDB; 1FZF; X-ray; 2.70 A; B/E=164-491, M/N/S/T=45-48.
DR PDB; 1FZG; X-ray; 2.50 A; B/E=164-491.
DR PDB; 1LT9; X-ray; 2.80 A; B/E=179-491.
DR PDB; 1LTJ; X-ray; 2.80 A; B/E=179-491.
DR PDB; 1N86; X-ray; 3.20 A; B/E=164-491, I/J=45-51.
DR PDB; 1N8E; X-ray; 4.50 A; B/E=164-491.
DR PDB; 1RE3; X-ray; 2.45 A; B/E=179-491.
DR PDB; 1RE4; X-ray; 2.70 A; B/E=179-491.
DR PDB; 1RF0; X-ray; 2.81 A; B/E=179-491.
DR PDB; 1RF1; X-ray; 2.53 A; B/E=179-491.
DR PDB; 2A45; X-ray; 3.65 A; H/K=45-135.
DR PDB; 2FFD; X-ray; 2.89 A; B/E=179-491.
DR PDB; 2H43; X-ray; 2.70 A; B/E=164-491.
DR PDB; 2HLO; X-ray; 2.60 A; B/E=164-491.
DR PDB; 2HOD; X-ray; 2.90 A; B/E/H/K=164-491.
DR PDB; 2HPC; X-ray; 2.90 A; B/E/H/K=164-491.
DR PDB; 2OYH; X-ray; 2.40 A; B/E=179-491.
DR PDB; 2OYI; X-ray; 2.70 A; B/E=179-491.
DR PDB; 2Q9I; X-ray; 2.80 A; B/E=164-491.
DR PDB; 2XNX; X-ray; 3.30 A; B/E/H/K=164-491.
DR PDB; 2XNY; X-ray; 7.50 A; B/E=164-491.
DR PDB; 2Z4E; X-ray; 2.70 A; B/E=164-489.
DR PDB; 3BVH; X-ray; 2.60 A; B/E=191-488.
DR PDB; 3E1I; X-ray; 2.30 A; B/E=164-491.
DR PDB; 3GHG; X-ray; 2.90 A; B/E/H/K=31-491.
DR PDB; 3H32; X-ray; 3.60 A; B/E=31-488.
DR PDB; 3HUS; X-ray; 3.04 A; B/E=179-491.
DR PDB; 6ATZ; X-ray; 2.70 A; E/F=69-79.
DR PDB; 6BIJ; X-ray; 2.10 A; C=69-81.
DR PDB; 6BIL; X-ray; 2.40 A; C=69-81.
DR PDB; 6V0Y; X-ray; 2.70 A; C=69-81.
DR PDB; 6V13; X-ray; 2.75 A; C=69-81.
DR PDB; 6V15; X-ray; 2.80 A; C=69-81.
DR PDB; 6V18; X-ray; 2.35 A; C=69-81.
DR PDB; 6V19; X-ray; 2.60 A; C=69-81.
DR PDB; 6V1A; X-ray; 2.29 A; C=69-81.
DR PDBsum; 1FZA; -.
DR PDBsum; 1FZB; -.
DR PDBsum; 1FZC; -.
DR PDBsum; 1FZE; -.
DR PDBsum; 1FZF; -.
DR PDBsum; 1FZG; -.
DR PDBsum; 1LT9; -.
DR PDBsum; 1LTJ; -.
DR PDBsum; 1N86; -.
DR PDBsum; 1N8E; -.
DR PDBsum; 1RE3; -.
DR PDBsum; 1RE4; -.
DR PDBsum; 1RF0; -.
DR PDBsum; 1RF1; -.
DR PDBsum; 2A45; -.
DR PDBsum; 2FFD; -.
DR PDBsum; 2H43; -.
DR PDBsum; 2HLO; -.
DR PDBsum; 2HOD; -.
DR PDBsum; 2HPC; -.
DR PDBsum; 2OYH; -.
DR PDBsum; 2OYI; -.
DR PDBsum; 2Q9I; -.
DR PDBsum; 2XNX; -.
DR PDBsum; 2XNY; -.
DR PDBsum; 2Z4E; -.
DR PDBsum; 3BVH; -.
DR PDBsum; 3E1I; -.
DR PDBsum; 3GHG; -.
DR PDBsum; 3H32; -.
DR PDBsum; 3HUS; -.
DR PDBsum; 6ATZ; -.
DR PDBsum; 6BIJ; -.
DR PDBsum; 6BIL; -.
DR PDBsum; 6V0Y; -.
DR PDBsum; 6V13; -.
DR PDBsum; 6V15; -.
DR PDBsum; 6V18; -.
DR PDBsum; 6V19; -.
DR PDBsum; 6V1A; -.
DR AlphaFoldDB; P02675; -.
DR SMR; P02675; -.
DR BioGRID; 108535; 222.
DR ComplexPortal; CPX-1922; Fibrinogen complex.
DR ComplexPortal; CPX-6225; Fibrin complex.
DR CORUM; P02675; -.
DR DIP; DIP-385N; -.
DR IntAct; P02675; 117.
DR MINT; P02675; -.
DR STRING; 9606.ENSP00000306099; -.
DR ChEMBL; CHEMBL2048; -.
DR DrugBank; DB04919; Alfimeprase.
DR DrugBank; DB13151; Anti-inhibitor coagulant complex.
DR DrugBank; DB11571; Human thrombin.
DR DrugBank; DB11311; Prothrombin.
DR DrugBank; DB00364; Sucralfate.
DR DrugBank; DB11300; Thrombin.
DR DrugBank; DB11572; Thrombin alfa.
DR CarbonylDB; P02675; -.
DR GlyConnect; 157; 4 N-Linked glycans.
DR GlyConnect; 159; 31 N-Linked glycans (1 site).
DR GlyGen; P02675; 6 sites, 39 N-linked glycans (2 sites), 2 O-linked glycans (2 sites).
DR iPTMnet; P02675; -.
DR PhosphoSitePlus; P02675; -.
DR SwissPalm; P02675; -.
DR BioMuta; FGB; -.
DR DMDM; 399492; -.
DR DOSAC-COBS-2DPAGE; P02675; -.
DR OGP; P02675; -.
DR REPRODUCTION-2DPAGE; IPI00298497; -.
DR REPRODUCTION-2DPAGE; P02675; -.
DR SWISS-2DPAGE; P02675; -.
DR UCD-2DPAGE; P02675; -.
DR CPTAC; non-CPTAC-1119; -.
DR CPTAC; non-CPTAC-1120; -.
DR CPTAC; non-CPTAC-2665; -.
DR EPD; P02675; -.
DR jPOST; P02675; -.
DR MassIVE; P02675; -.
DR PaxDb; P02675; -.
DR PeptideAtlas; P02675; -.
DR PRIDE; P02675; -.
DR ProteomicsDB; 51544; -.
DR ABCD; P02675; 8 sequenced antibodies.
DR Antibodypedia; 855; 607 antibodies from 38 providers.
DR DNASU; 2244; -.
DR Ensembl; ENST00000302068.9; ENSP00000306099.4; ENSG00000171564.12.
DR GeneID; 2244; -.
DR KEGG; hsa:2244; -.
DR MANE-Select; ENST00000302068.9; ENSP00000306099.4; NM_005141.5; NP_005132.2.
DR CTD; 2244; -.
DR DisGeNET; 2244; -.
DR GeneCards; FGB; -.
DR HGNC; HGNC:3662; FGB.
DR HPA; ENSG00000171564; Tissue enriched (liver).
DR MalaCards; FGB; -.
DR MIM; 134830; gene.
DR MIM; 202400; phenotype.
DR MIM; 616004; phenotype.
DR neXtProt; NX_P02675; -.
DR OpenTargets; ENSG00000171564; -.
DR Orphanet; 98880; Familial afibrinogenemia.
DR Orphanet; 98881; Familial dysfibrinogenemia.
DR Orphanet; 248408; Familial hypodysfibrinogenemia.
DR Orphanet; 101041; Familial hypofibrinogenemia.
DR PharmGKB; PA163; -.
DR VEuPathDB; HostDB:ENSG00000171564; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158122; -.
DR HOGENOM; CLU_038628_13_0_1; -.
DR InParanoid; P02675; -.
DR OMA; VYPDAGG; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; P02675; -.
DR TreeFam; TF336658; -.
DR PathwayCommons; P02675; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR SignaLink; P02675; -.
DR SIGNOR; P02675; -.
DR BioGRID-ORCS; 2244; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; FGB; human.
DR EvolutionaryTrace; P02675; -.
DR GeneWiki; Fibrinogen_beta_chain; -.
DR GenomeRNAi; 2244; -.
DR Pharos; P02675; Tbio.
DR PRO; PR:P02675; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P02675; protein.
DR Bgee; ENSG00000171564; Expressed in right lobe of liver and 117 other tissues.
DR ExpressionAtlas; P02675; baseline and differential.
DR Genevisible; P02675; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0005577; C:fibrinogen complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031091; C:platelet alpha granule; IDA:BHF-UCL.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IDA:BHF-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:ComplexPortal.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:BHF-UCL.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
DR GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
DR GO; GO:0043152; P:induction of bacterial agglutination; IDA:CACAO.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
DR GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0045921; P:positive regulation of exocytosis; IDA:BHF-UCL.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:BHF-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; NAS:BHF-UCL.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:BHF-UCL.
DR GO; GO:0051258; P:protein polymerization; IDA:BHF-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR InterPro; IPR037580; Fibrinogen_beta.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF332; PTHR19143:SF332; 1.
DR Pfam; PF08702; Fib_alpha; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SMART; SM01212; Fib_alpha; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Blood coagulation; Coiled coil;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Hemostasis; Immunity; Innate immunity; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:420779,
FT ECO:0000269|PubMed:936108, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.13"
FT PEPTIDE 31..44
FT /note="Fibrinopeptide B"
FT /evidence="ECO:0000269|PubMed:12665801"
FT /id="PRO_0000009070"
FT CHAIN 45..491
FT /note="Fibrinogen beta chain"
FT /id="PRO_0000009071"
FT DOMAIN 232..488
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 44..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..47
FT /note="Beta-chain polymerization, binding distal domain of
FT another fibrin"
FT COILED 157..222
FT /evidence="ECO:0000305|PubMed:10074346,
FT ECO:0000305|PubMed:19296670, ECO:0000305|PubMed:9628725"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 44..45
FT /note="Cleavage; by thrombin; to release fibrinopeptide B"
FT SITE 152..153
FT /note="Cleavage; by plasmin; to break down fibrin clots"
FT SITE 160..161
FT /note="Cleavage; by hementin; to prevent blood coagulation"
FT SITE 163..164
FT /note="Cleavage; by plasmin; to break down fibrin clots"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:420779"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9628725,
FT ECO:0000269|Ref.11"
FT DISULFID 95
FT /note="Interchain (with C-55 in alpha chain)"
FT /evidence="ECO:0000269|PubMed:19296670"
FT DISULFID 106
FT /note="Interchain (with C-68 in alpha chain)"
FT /evidence="ECO:0000269|PubMed:19296670"
FT DISULFID 110
FT /note="Interchain (with C-45 in gamma chain)"
FT /evidence="ECO:0000305|PubMed:6575689"
FT DISULFID 223
FT /note="Interchain (with C-184 in alpha chain)"
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FZC"
FT DISULFID 227
FT /note="Interchain (with C-161 in gamma chain)"
FT DISULFID 231..316
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FZC"
FT DISULFID 241..270
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FZC"
FT DISULFID 424..437
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FZC"
FT VARIANT 2
FT /note="K -> E (in dbSNP:rs6053)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014169"
FT VARIANT 39..102
FT /note="Missing (in New York-1)"
FT /evidence="ECO:0000269|PubMed:3156856"
FT /id="VAR_002402"
FT VARIANT 44
FT /note="R -> C (in Christchurch-2, Seattle-1 and Ijmuiden;
FT dbSNP:rs121909616)"
FT /evidence="ECO:0000269|PubMed:1565641"
FT /id="VAR_002403"
FT VARIANT 45
FT /note="G -> R (in Ise)"
FT /evidence="ECO:0000269|PubMed:2018836"
FT /id="VAR_002404"
FT VARIANT 74
FT /note="R -> C (in Nijmegen; dbSNP:rs121909619)"
FT /evidence="ECO:0000269|PubMed:1565641"
FT /id="VAR_002405"
FT VARIANT 95
FT /note="C -> R (in CAFBN; hypofibrinogenemia; heterozygous;
FT decreased fibrinogen complex assembly; no effect on
FT fibrinogen complex secretion)"
FT /evidence="ECO:0000269|PubMed:25427968"
FT /id="VAR_072724"
FT VARIANT 98
FT /note="A -> T (in DYSFIBRIN; fibrinogen Naples and Milano-
FT 2; associated with defective thrombin binding and
FT thrombophilia; dbSNP:rs121909620)"
FT /evidence="ECO:0000269|PubMed:1634610"
FT /id="VAR_002406"
FT VARIANT 100
FT /note="P -> S (in dbSNP:rs2227434)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_013091"
FT VARIANT 170
FT /note="N -> H (in dbSNP:rs2227409)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_013092"
FT VARIANT 196
FT /note="R -> C (in CAFBN; fibrinogen Longmont;
FT dbSNP:rs121909623)"
FT /evidence="ECO:0000269|PubMed:11468164"
FT /id="VAR_016908"
FT VARIANT 202
FT /note="L -> Q (in CAFBN; dbSNP:rs121909624)"
FT /evidence="ECO:0000269|PubMed:15070683"
FT /id="VAR_072620"
FT VARIANT 265
FT /note="P -> L (in dbSNP:rs6054)"
FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.4"
FT /id="VAR_013093"
FT VARIANT 365
FT /note="A -> T (in Pontoise-2; dbSNP:rs121909617)"
FT /id="VAR_002407"
FT VARIANT 383
FT /note="L -> R (in CAFBN; abolishes fibrinogen secretion;
FT dbSNP:rs121909621)"
FT /evidence="ECO:0000269|PubMed:10666208"
FT /id="VAR_016909"
FT VARIANT 407
FT /note="T -> K (in CAFBN; homozygous; heterozygous; no
FT effect on fibrinogen complex assembly; impaired fibrinogen
FT complex secretion)"
FT /evidence="ECO:0000269|PubMed:25427968"
FT /id="VAR_072725"
FT VARIANT 430
FT /note="G -> D (in CAFBN; abolishes fibrinogen secretion;
FT dbSNP:rs121909622)"
FT /evidence="ECO:0000269|PubMed:10666208"
FT /id="VAR_016910"
FT VARIANT 478
FT /note="R -> K (in Baltimore-2; dbSNP:rs4220)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:3194892, ECO:0000269|Ref.4"
FT /id="VAR_002408"
FT CONFLICT 138..139
FT /note="SQ -> QS (in Ref. 11; AA sequence and 12; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..146
FT /note="FQ -> QF (in Ref. 10; AA sequence, 11; AA sequence
FT and 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="P -> A (in Ref. 1; AAA52429)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="I -> T (in Ref. 7; AAI07767)"
FT /evidence="ECO:0000305"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:3GHG"
FT HELIX 109..145
FT /evidence="ECO:0007829|PDB:3GHG"
FT HELIX 147..167
FT /evidence="ECO:0007829|PDB:3GHG"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:3GHG"
FT TURN 182..189
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 190..222
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2HOD"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2OYH"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1FZF"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2H43"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2HOD"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:1FZA"
FT STRAND 351..361
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 370..379
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:2HPC"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:2HOD"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1FZB"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2OYI"
FT TURN 424..428
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:3E1I"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:3BVH"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:3HUS"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:3E1I"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:2OYH"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:1FZC"
SQ SEQUENCE 491 AA; 55928 MW; B92FFB9976AB53C5 CRC64;
MKRMVSWSFH KLKTMKHLLL LLLCVFLVKS QGVNDNEEGF FSARGHRPLD KKREEAPSLR
PAPPPISGGG YRARPAKAAA TQKKVERKAP DAGGCLHADP DLGVLCPTGC QLQEALLQQE
RPIRNSVDEL NNNVEAVSQT SSSSFQYMYL LKDLWQKRQK QVKDNENVVN EYSSELEKHQ
LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE
CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK
QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT
VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP
RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM
SMKIRPFFPQ Q
