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 27-MAR-2024, entry version 253. 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 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 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 CYS-44 AND 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 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 228. 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 BindingDB; P02675; -. 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 UniLectin; P02675; -. DR CarbonylDB; P02675; -. DR GlyConnect; 157; 4 N-Linked glycans. DR GlyConnect; 159; 31 N-Linked glycans (1 site). DR GlyCosmos; P02675; 3 sites, 33 glycans. DR GlyGen; P02675; 7 sites, 42 N-linked glycans (2 sites), 3 O-linked glycans (3 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 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; 9606-ENSP00000306099; -. DR PeptideAtlas; P02675; -. DR PRIDE; P02675; -. DR ProteomicsDB; 51544; -. DR Pumba; P02675; -. DR ABCD; P02675; 8 sequenced antibodies. DR Antibodypedia; 855; 661 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 AGR; HGNC:3662; -. 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; CIHADPD; -. DR OrthoDB; 3134470at2759; -. DR PhylomeDB; P02675; -. DR TreeFam; TF336658; -. DR BioCyc; MetaCyc:ENSG00000171564-MONOMER; -. 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 1148 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 119 other cell types or tissues. DR ExpressionAtlas; P02675; baseline and differential. 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:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI: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:UniProtKB. 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; 1.20.5.50; -; 2. DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1. DR InterPro; IPR037579; Fibrinogen. 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; IPR020837; Fibrinogen_CS. DR NCBIfam; NF040941; GGGWT_bact; 1. DR PANTHER; PTHR47221; FIBRINOGEN ALPHA CHAIN; 1. DR PANTHER; PTHR47221:SF2; FIBRINOGEN BETA CHAIN; 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; Fibrinogen C-terminal domain-like; 1. DR SUPFAM; SSF58010; Fibrinogen coiled-coil and central regions; 1. DR PROSITE; PS00514; FIBRINOGEN_C_1; 1. DR PROSITE; PS51406; FIBRINOGEN_C_2; 1. DR SWISS-2DPAGE; P02675; -. DR UCD-2DPAGE; P02675; -. DR Genevisible; P02675; HS. 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 FT Milano-2; defective thrombin binding resulting in decreased FT release of fibrinopeptide B; 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 //