FIBG_HUMAN
ID FIBG_HUMAN Reviewed; 453 AA.
AC P02679; A8K057; P04469; P04470; Q53Y18; Q96A14; Q96KJ3; Q9UC62; Q9UC63;
AC Q9UCF3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 3.
DT 03-AUG-2022, entry version 257.
DE RecName: Full=Fibrinogen gamma chain;
DE Flags: Precursor;
GN Name=FGG; ORFNames=PRO2061;
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=6688357; DOI=10.1021/bi00282a033;
RA Chung D.W., Chan W.-Y., Davie E.W.;
RT "Characterization of a complementary deoxyribonucleic acid coding for the
RT gamma chain of human fibrinogen.";
RL Biochemistry 22:3250-3256(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
RX PubMed=2990550; DOI=10.1021/bi00329a041;
RA Rixon M.W., Chung D.W., Davie E.W.;
RT "Nucleotide sequence of the gene for the gamma chain of human fibrinogen.";
RL Biochemistry 24:2077-2086(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
RC TISSUE=Liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 33 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-140 AND ARG-191.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
RC TISSUE=Skeletal muscle;
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 [9]
RP PROTEIN SEQUENCE OF 27-437.
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 [10]
RP PROTEIN SEQUENCE OF 27-41.
RC TISSUE=Platelet;
RX PubMed=8509453; DOI=10.1083/jcb.121.6.1329;
RA Bertagnolli M.E., Beckerle M.C.;
RT "Evidence for the selective association of a subpopulation of GPIIb-IIIa
RT with the actin cytoskeletons of thrombin-activated platelets.";
RL J. Cell Biol. 121:1329-1342(1993).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-286.
RC TISSUE=Liver;
RX PubMed=1685103; DOI=10.3109/10425179109020801;
RA Marchetti L., Zanelli T., Malcovati M., Tenchini M.L.;
RT "Polymorphism of the human gamma chain fibrinogen gene.";
RL DNA Seq. 1:419-422(1991).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 209-270.
RX PubMed=6689067; DOI=10.1093/nar/11.21.7427;
RA Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S.;
RT "Isolation and characterisation of cDNA clones for the A alpha- and gamma-
RT chains of human fibrinogen.";
RL Nucleic Acids Res. 11:7427-7434(1983).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-437 (ISOFORMS GAMMA-A AND
RP GAMMA-B).
RX PubMed=6092346; DOI=10.1016/s0021-9258(18)90821-5;
RA Fornace A.J. Jr., Cummings D.E., Comeau C.M., Kant J.A., Crabtree G.R.;
RT "Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near
RT the 3' end of the gene produces gamma A and gamma B forms of gamma-
RT fibrinogen.";
RL J. Biol. Chem. 259:12826-12830(1984).
RN [14]
RP PROTEIN SEQUENCE OF 291-310, AND VARIANTS BARCELONA-3/BARCELONA-4 HIS-301
RP AND VILLAJOYOSA CYS-301.
RC TISSUE=Blood;
RX PubMed=7654933; DOI=10.1097/00001721-199505000-00002;
RA Borrell M., Gari M., Coll I., Vallve C., Tirado I., Soria J.M., Sala N.,
RA Munoz C., Oliver A., Garcia A.;
RT "Abnormal polymerization and normal binding of plasminogen and t-PA in
RT three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275-->His)
RT and Villajoyosa (gamma Arg 275-->Cys).";
RL Blood Coagul. Fibrinolysis 6:198-206(1995).
RN [15]
RP PROTEIN SEQUENCE OF 411-453 (ISOFORM GAMMA-B).
RX PubMed=7306501; DOI=10.1021/bi00524a036;
RA Wolfenstein-Todel C., Mosesson M.W.;
RT "Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain
RT variant (gamma').";
RL Biochemistry 20:6146-6149(1981).
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.
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 [18]
RP 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 [19]
RP QUATERNARY STRUCTURE, AND DISULFIDE BONDS.
RX PubMed=6860649; DOI=10.1021/bi00278a003;
RA Hoeprich P.D., Doolittle R.F.;
RT "Dimeric half-molecules of human fibrinogen are joined through disulfide
RT bonds in an antiparallel orientation.";
RL Biochemistry 22:2049-2055(1983).
RN [20]
RP SULFATION.
RX PubMed=1892842; DOI=10.1021/bi00103a004;
RA Farrel D.H., Mulvihill E.R., Huang S., Chung D.W., Davie E.W.;
RT "Recombinant human fibrinogen and sulfation of the gamma' chain.";
RL Biochemistry 30:9414-9420(1991).
RN [21]
RP SULFATION AT TYR-444 AND TYR-448.
RX PubMed=11307817;
RA Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., Mosesson M.W.;
RT "The amino acid sequence in fibrin responsible for high affinity thrombin
RT binding.";
RL Thromb. Haemost. 85:470-474(2001).
RN [22]
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 [23]
RP POLYMERIZATION SITE.
RX PubMed=6592597; DOI=10.1073/pnas.81.19.5980;
RA Horwitz B.H., Varadi A., Scheraga H.A.;
RT "Localization of a fibrin gamma-chain polymerization site within segment
RT Thr-374 to Glu-396 of human fibrinogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5980-5984(1984).
RN [24]
RP POLYMERIZATION SITE.
RX PubMed=6451630; DOI=10.1016/s0021-9258(19)69643-2;
RA Olexa S.A., Budzynski A.Z.;
RT "Localization of a fibrin polymerization site.";
RL J. Biol. Chem. 256:3544-3549(1981).
RN [25]
RP PLATELET AGGREGATION SITE.
RX PubMed=6326808; DOI=10.1021/bi00303a028;
RA Kloczewiak M., Timmons S., Lukas T.J., Hawiger J.;
RT "Platelet receptor recognition site on human fibrinogen. Synthesis and
RT structure-function relationship of peptides corresponding to the carboxy-
RT terminal segment of the gamma chain.";
RL Biochemistry 23:1767-1774(1984).
RN [26]
RP PLATELET AGGREGATION SITE.
RX PubMed=6325435; DOI=10.1016/s0021-9258(18)91019-7;
RA Plow E.F., Srouji A.H., Meyer D., Marguerie G., Ginsberg M.H.;
RT "Evidence that three adhesive proteins interact with a common recognition
RT site on activated platelets.";
RL J. Biol. Chem. 259:5388-5391(1984).
RN [27]
RP CALCIUM-BINDING SITE.
RX PubMed=3160702; DOI=10.1016/s0021-9258(17)39297-9;
RA Dang C.V., Ebert R.F., Bell W.R.;
RT "Localization of a fibrinogen calcium binding site between gamma-subunit
RT positions 311 and 336 by terbium fluorescence.";
RL J. Biol. Chem. 260:9713-9719(1985).
RN [28]
RP CHROMATOGRAPHIC COMPARISON OF GAMMA-A AND GAMMA-B CHAINS.
RX PubMed=6933547; DOI=10.1073/pnas.77.9.5069;
RA Wolfenstein-Todel C., Mosesson M.W.;
RT "Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-
RT terminal sequence in a normal gamma chain variant (gamma').";
RL Proc. Natl. Acad. Sci. U.S.A. 77:5069-5073(1980).
RN [29]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [30]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
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 [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
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 [32]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [33]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
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 [34]
RP GLYCOSYLATION AT ASN-78.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [35]
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 [36]
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 [37]
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 [38]
RP PHOSPHORYLATION AT SER-68.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 169-433 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=9016719; DOI=10.1016/s0969-2126(97)00171-8;
RA Yee V.C., Pratt K.P., Cote H.C.F., le Trong I., Chung D.W., Davie E.W.,
RA Stenkamp R.E., Teller D.C.;
RT "Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of
RT human fibrinogen.";
RL Structure 5:125-138(1997).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 169-433 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=9207064; DOI=10.1073/pnas.94.14.7176;
RA Pratt K.P., Cote H.C.F., Chung D.W., Stenkamp R.E., Davie E.W.;
RT "The primary fibrin polymerization pocket: three-dimensional structure of a
RT 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-
RT Arg-Pro.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7176-7181(1997).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 114-432 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, AND 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 [42]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 114-432 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, AND TISSUE
RP 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 [43]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 114-432 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [44]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 27-433 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [45]
RP VARIANT ASAHI THR-336.
RX PubMed=2496144; DOI=10.1172/jci114056;
RA Yamazumi K., Shimura K., Terukina S., Takahashi N., Matsuda M.;
RT "A gamma methionine-310 to threonine substitution and consequent N-
RT glycosylation at gamma asparagine-308 identified in a congenital
RT dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen
RT Asahi.";
RL J. Clin. Invest. 83:1590-1597(1989).
RN [46]
RP VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3
RP TYR-356.
RX PubMed=1421174;
RA Mimuro J., Muramatsu S., Maekawa H., Sakata Y., Kaneko M., Yoshitake S.,
RA Okuma M., Ito Y., Takeda Y., Matsuda M.;
RT "Gene analyses of abnormal fibrinogens with a mutation in the gamma
RT chain.";
RL Int. J. Hematol. 56:129-134(1992).
RN [47]
RP INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN VAL-318.
RX PubMed=2257302;
RA Bantia S., Mane S.M., Bell W.R., Dang C.V.;
RT "Fibrinogen Baltimore I: polymerization defect associated with a gamma
RT 292Gly-->Val (GGC-->GTC) mutation.";
RL Blood 76:2279-2283(1990).
RN [48]
RP VARIANT BALTIMORE-3 ILE-334.
RX PubMed=2328317;
RA Bantia S., Bell W.R., Dang C.V.;
RT "Polymerization defect of fibrinogen Baltimore III due to a gamma
RT Asn308-->Ile mutation.";
RL Blood 75:1659-1663(1990).
RN [49]
RP VARIANT BERN-1 LYS-363.
RX PubMed=8400260;
RA Steinmann C., Reber P., Jungo M., Laemmle B., Heinemann G., Wermuth B.,
RA Furlan M.;
RT "Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for
RT defective fibrin monomer polymerization.";
RL Blood 82:2104-2108(1993).
RN [50]
RP VARIANT KYOTO-1 LYS-334.
RX PubMed=2971046; DOI=10.1016/s0021-9258(18)68321-8;
RA Yoshida N., Terukina S., Okuma M., Moroi M., Aoki N., Matsuda M.;
RT "Characterization of an apparently lower molecular weight gamma-chain
RT variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by
RT lysine which causes accelerated cleavage of fragment D1 by plasmin and the
RT generation of a new plasmin cleavage site.";
RL J. Biol. Chem. 263:13848-13856(1988).
RN [51]
RP VARIANT KYOTO-3 TYR-356.
RX PubMed=2819242;
RA Terukina S., Yamazumi K., Okamoto K., Yamashita H., Ito Y., Matsuda M.;
RT "Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic
RT acid-330 to tyrosine substitution manifesting impaired fibrin monomer
RT polymerization.";
RL Blood 74:2681-2687(1989).
RN [52]
RP VARIANT DYSFIBRIN VAL-356.
RX PubMed=3708159;
RA Reber P., Furlan M., Rupp C., Kehl M., Henschen A., Mannucci P.M.,
RA Beck E.A.;
RT "Characterization of fibrinogen Milano I: amino acid exchange gamma 330
RT Asp-->Val impairs fibrin polymerization.";
RL Blood 67:1751-1756(1986).
RN [53]
RP VARIANT MILANO-5 CYS-301.
RX PubMed=7841300;
RA Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B.,
RA Redaelli R., Baudo F., Furlan M.;
RT "Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275
RT Arg-->Cys substitution.";
RL Blood Coagul. Fibrinolysis 5:463-471(1994).
RN [54]
RP VARIANT MILANO-7 CYS-384.
RX PubMed=8080993;
RA Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B.,
RA Redaelli R., Baudo F., Furlan M.;
RT "A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes
RT defective fibrin polymerization.";
RL Blood 84:1874-1880(1994).
RN [55]
RP VARIANT NAGOYA-1 ARG-355.
RX PubMed=2738036; DOI=10.1093/oxfordjournals.jbchem.a122601;
RA Miyata T., Furukawa K., Iwanaga S., Takamatsu J., Saito H.;
RT "Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the
RT gamma-chain that impairs the polymerization of fibrin monomer.";
RL J. Biochem. 105:10-14(1989).
RN [56]
RP VARIANT OSAKA-2 CYS-301.
RX PubMed=2971042; DOI=10.1016/s0021-9258(18)68281-x;
RA Terukina S., Matsuda M., Hirata H., Takeda Y., Miyata T., Takao T.,
RA Shimonishi Y.;
RT "Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen,
RT 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at
RT the mutation site.";
RL J. Biol. Chem. 263:13579-13587(1988).
RN [57]
RP VARIANT OSAKA-3 HIS-301.
RX PubMed=1455400;
RA Yoshida N., Imoka S., Hirata H., Matsuda M., Asakura S.;
RT "Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma
RT arginine-275 by histidine has an apparently higher molecular weight gamma-
RT chain variant.";
RL Thromb. Haemost. 68:534-538(1992).
RN [58]
RP VARIANT OSAKA-5 GLY-401.
RX PubMed=1733971; DOI=10.1016/s0021-9258(18)45943-1;
RA Yoshida N., Hirata H., Morigami Y., Imaoka S., Matsuda M., Yamazumi K.,
RA Asakura S.;
RT "Characterization of an abnormal fibrinogen Osaka V with the replacement of
RT gamma-arginine 375 by glycine. The lack of high affinity calcium binding to
RT D-domains and the lack of protective effect of calcium on fibrinolysis.";
RL J. Biol. Chem. 267:2753-2759(1992).
RN [59]
RP VARIANT PARIS-1 GLY-377 DELINS
RP VAL-MET-CYS-GLY-GLU-ALA-LEU-PRO-MET-LEU-LYS-ASP-PRO-CYS-TYR-SER.
RX PubMed=8470043;
RA Rosenberg J.B., Newman P.J., Mosesson M.W., Guillin M.-C., Amrani D.L.;
RT "Paris I dysfibrinogenemia: a point mutation in intron 8 results in
RT insertion of a 15 amino acid sequence in the fibrinogen gamma-chain.";
RL Thromb. Haemost. 69:217-220(1993).
RN [60]
RP VARIANT TOCHIGI CYS-301.
RX PubMed=3337908;
RA Yoshida N., Ota K., Moroi M., Matsuda M.;
RT "An apparently higher molecular weight gamma-chain variant in a new
RT congenital abnormal fibrinogen Tochigi characterized by the replacement of
RT gamma arginine-275 by cysteine.";
RL Blood 71:480-487(1988).
RN [61]
RP VARIANT VLISSINGEN 345-ASN-ASP-346 DEL.
RX PubMed=2071611; DOI=10.1016/s0021-9258(18)98861-7;
RA Koopman J., Haverkate F., Briet E., Lord S.T.;
RT "A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in
RT the gamma-chain gene, causing defective calcium binding and impaired fibrin
RT polymerization.";
RL J. Biol. Chem. 266:13456-13461(1991).
RN [62]
RP VARIANT BERGAMO-2/ESSEN/HAIFA/PERUGIA HIS-301.
RX PubMed=3563970;
RA Reber P., Furlan M., Henschen A., Kaudewitz H., Barbui T., Hilgard P.,
RA Nenci G.G., Berrettini M., Beck E.A.;
RT "Three abnormal fibrinogen variants with the same amino acid substitution
RT (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and Perugia.";
RL Thromb. Haemost. 56:401-406(1986).
RN [63]
RP INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN HIS-301.
RX PubMed=2976995;
RA Yamazumi K., Terukina S., Onohara S., Matsuda M.;
RT "Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga'
RT with an Arg-275 to His substitution.";
RL Thromb. Haemost. 60:476-480(1988).
RN [64]
RP VARIANT MILANO-12 ARG-191.
RX PubMed=11435303; DOI=10.1182/blood.v98.2.351;
RA Bolliger-Stucki B., Lord S.T., Furlan M.;
RT "Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid
RT substitutions, A-alpha R16C and gamma G165R.";
RL Blood 98:351-357(2001).
RN [65]
RP VARIANTS ARG-191 AND VAL-410.
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 [66]
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 [67]
RP VARIANT HILLSBOROUGH ASP-335.
RX PubMed=11986213; DOI=10.1182/blood.v99.10.3597;
RA Mullin J.L., Brennan S.O., Ganly P.S., George P.M.;
RT "Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with
RT impaired clotting.";
RL Blood 99:3597-3601(2002).
RN [68]
RP VARIANT DYSFIBRIN PRO-404.
RX PubMed=15632207; DOI=10.1182/blood-2004-04-1621;
RA Keller M.A., Martinez J., Baradet T.C., Nagaswami C., Chernysh I.N.,
RA Borowski M.K., Surrey S., Weisel J.W.;
RT "Fibrinogen Philadelphia, a hypodysfibrinogenemia characterized by abnormal
RT polymerization and fibrinogen hypercatabolism due to gamma S378P
RT mutation.";
RL Blood 105:3162-3168(2005).
RN [69]
RP INVOLVEMENT IN CAFBN; VARIANTS CAFBN PRO-303; HIS-327; ASP-345 AND TRP-401,
RP AND CHARACTERIZATION OF VARIANTS CAFBN PRO-303; HIS-327 AND ASP-345.
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: Together with fibrinogen alpha (FGA) and fibrinogen beta
CC (FGB), polymerizes to form an insoluble fibrin matrix. 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 via an ITGB3-dependent pathway. Maternal fibrinogen
CC is essential for successful pregnancy. Fibrin deposition is also
CC associated with infection, where it protects against IFNG-mediated
CC hemorrhage. May also facilitate the antibacterial immune response via
CC both innate and T-cell mediated pathways.
CC {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:6860649, ECO:0000269|PubMed:9016719,
CC ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233,
CC ECO:0000269|PubMed:9628725}.
CC -!- INTERACTION:
CC P02679; P75358: gapA; Xeno; NbExp=2; IntAct=EBI-1034422, EBI-2259469;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10074346,
CC ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Gamma-B; Synonyms=Gamma';
CC IsoId=P02679-1; Sequence=Displayed;
CC Name=Gamma-A;
CC IsoId=P02679-2; Sequence=VSP_001537;
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:19296670, 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 -!- PTM: Sulfation of C-terminal tyrosines increases affinity for thrombin.
CC {ECO:0000269|PubMed:11307817, ECO:0000269|PubMed:1892842}.
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:25427968}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Patients with congenital fibrinogen abnormalities can manifest
CC different clinical pictures. Some cases are clinically silent, some
CC show a tendency toward bleeding and some show a predisposition for
CC 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:15632207, ECO:0000269|PubMed:2257302,
CC ECO:0000269|PubMed:2976995, ECO:0000269|PubMed:3708159}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The gamma-chain carries the main binding site for the
CC platelet receptor.
CC -!- MISCELLANEOUS: [Isoform Gamma-B]: Present in about 10% of the
CC fibrinogen molecules in plasma but absent from those in the platelets.
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/fgg/";
CC ---------------------------------------------------------------------------
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DR EMBL; M10014; AAB59530.1; -; Genomic_DNA.
DR EMBL; M10014; AAB59531.1; -; Genomic_DNA.
DR EMBL; AF118092; AAF22036.1; -; mRNA.
DR EMBL; AF350254; AAK19751.2; -; Genomic_DNA.
DR EMBL; AF350254; AAK19752.2; -; Genomic_DNA.
DR EMBL; AK289422; BAF82111.1; -; mRNA.
DR EMBL; AK290824; BAF83513.1; -; mRNA.
DR EMBL; BT007081; AAP35744.1; -; mRNA.
DR EMBL; CH471056; EAX04917.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04919.1; -; Genomic_DNA.
DR EMBL; BC007044; AAH07044.1; -; mRNA.
DR EMBL; BC021674; AAH21674.1; -; mRNA.
DR EMBL; X51473; CAA35837.1; -; mRNA.
DR EMBL; X00086; CAA24944.1; -; mRNA.
DR EMBL; K02569; AAA52430.1; -; Genomic_DNA.
DR EMBL; K02569; AAA52431.1; -; Genomic_DNA.
DR CCDS; CCDS3788.1; -. [P02679-1]
DR CCDS; CCDS47153.1; -. [P02679-2]
DR PIR; A90470; FGHUG.
DR PIR; A90494; FGHUGB.
DR RefSeq; NP_000500.2; NM_000509.5. [P02679-2]
DR RefSeq; NP_068656.2; NM_021870.2. [P02679-1]
DR PDB; 1DUG; X-ray; 1.80 A; A/B=424-433.
DR PDB; 1FIB; X-ray; 2.10 A; A=169-433.
DR PDB; 1FIC; X-ray; 2.50 A; A/B=169-433.
DR PDB; 1FID; X-ray; 2.10 A; A=169-433.
DR PDB; 1FZA; X-ray; 2.90 A; C/F=114-432.
DR PDB; 1FZB; X-ray; 2.90 A; C/F=114-432.
DR PDB; 1FZC; X-ray; 2.30 A; C/F=114-432.
DR PDB; 1FZE; X-ray; 3.00 A; C/F=114-432.
DR PDB; 1FZF; X-ray; 2.70 A; C/F=114-432.
DR PDB; 1FZG; X-ray; 2.50 A; C/F=114-432.
DR PDB; 1LT9; X-ray; 2.80 A; C/F=122-432.
DR PDB; 1LTJ; X-ray; 2.80 A; C/F=122-432.
DR PDB; 1N86; X-ray; 3.20 A; C/F=114-433.
DR PDB; 1N8E; X-ray; 4.50 A; C/F=114-433.
DR PDB; 1RE3; X-ray; 2.45 A; C/F=122-432.
DR PDB; 1RE4; X-ray; 2.70 A; C/F=122-432.
DR PDB; 1RF0; X-ray; 2.81 A; C/F=122-432.
DR PDB; 1RF1; X-ray; 2.53 A; C/F=122-432.
DR PDB; 2A45; X-ray; 3.65 A; I/L=27-71.
DR PDB; 2FFD; X-ray; 2.89 A; C/F=122-432.
DR PDB; 2FIB; X-ray; 2.01 A; A=169-433.
DR PDB; 2H43; X-ray; 2.70 A; C/F=115-433.
DR PDB; 2HLO; X-ray; 2.60 A; C/F=114-433.
DR PDB; 2HOD; X-ray; 2.90 A; C/F/I/L=115-433.
DR PDB; 2HPC; X-ray; 2.90 A; C/F/I/L=115-433.
DR PDB; 2HWL; X-ray; 2.40 A; P=439-452.
DR PDB; 2OYH; X-ray; 2.40 A; C/F=122-432.
DR PDB; 2OYI; X-ray; 2.70 A; C/F=122-432.
DR PDB; 2Q9I; X-ray; 2.80 A; C/F=114-433.
DR PDB; 2VDO; X-ray; 2.51 A; C=426-433.
DR PDB; 2VDP; X-ray; 2.80 A; C=428-433.
DR PDB; 2VDQ; X-ray; 2.59 A; C=426-433.
DR PDB; 2VDR; X-ray; 2.40 A; C=428-433.
DR PDB; 2VR3; X-ray; 1.95 A; C/D=425-433.
DR PDB; 2XNX; X-ray; 3.30 A; C/F/I/L=114-432.
DR PDB; 2XNY; X-ray; 7.50 A; C/F=114-432.
DR PDB; 2Y7L; X-ray; 1.49 A; B=421-433.
DR PDB; 2Z4E; X-ray; 2.70 A; C/F=114-433.
DR PDB; 3BVH; X-ray; 2.60 A; C/F=128-420.
DR PDB; 3E1I; X-ray; 2.30 A; C/F=114-432.
DR PDB; 3FIB; X-ray; 2.10 A; A=170-418.
DR PDB; 3GHG; X-ray; 2.90 A; C/F/I/L=27-433.
DR PDB; 3H32; X-ray; 3.60 A; C/F=121-433.
DR PDB; 3HUS; X-ray; 3.04 A; C/F=122-432.
DR PDB; 4B60; X-ray; 1.83 A; C/D=421-433.
DR PDBsum; 1DUG; -.
DR PDBsum; 1FIB; -.
DR PDBsum; 1FIC; -.
DR PDBsum; 1FID; -.
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; 2FIB; -.
DR PDBsum; 2H43; -.
DR PDBsum; 2HLO; -.
DR PDBsum; 2HOD; -.
DR PDBsum; 2HPC; -.
DR PDBsum; 2HWL; -.
DR PDBsum; 2OYH; -.
DR PDBsum; 2OYI; -.
DR PDBsum; 2Q9I; -.
DR PDBsum; 2VDO; -.
DR PDBsum; 2VDP; -.
DR PDBsum; 2VDQ; -.
DR PDBsum; 2VDR; -.
DR PDBsum; 2VR3; -.
DR PDBsum; 2XNX; -.
DR PDBsum; 2XNY; -.
DR PDBsum; 2Y7L; -.
DR PDBsum; 2Z4E; -.
DR PDBsum; 3BVH; -.
DR PDBsum; 3E1I; -.
DR PDBsum; 3FIB; -.
DR PDBsum; 3GHG; -.
DR PDBsum; 3H32; -.
DR PDBsum; 3HUS; -.
DR PDBsum; 4B60; -.
DR AlphaFoldDB; P02679; -.
DR BMRB; P02679; -.
DR SMR; P02679; -.
DR BioGRID; 108557; 124.
DR ComplexPortal; CPX-1922; Fibrinogen complex.
DR ComplexPortal; CPX-6225; Fibrin complex.
DR CORUM; P02679; -.
DR DIP; DIP-29644N; -.
DR IntAct; P02679; 32.
DR MINT; P02679; -.
DR STRING; 9606.ENSP00000336829; -.
DR ChEMBL; CHEMBL2364709; -.
DR DrugBank; DB11571; Human thrombin.
DR DrugBank; DB00364; Sucralfate.
DR DrugBank; DB11300; Thrombin.
DR DrugBank; DB11572; Thrombin alfa.
DR CarbonylDB; P02679; -.
DR GlyConnect; 157; 4 N-Linked glycans.
DR GlyConnect; 160; 13 N-Linked glycans (1 site), 1 O-Linked glycan (1 site).
DR GlyGen; P02679; 4 sites, 28 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P02679; -.
DR PhosphoSitePlus; P02679; -.
DR BioMuta; FGG; -.
DR DMDM; 20178280; -.
DR DOSAC-COBS-2DPAGE; P02679; -.
DR OGP; P02679; -.
DR REPRODUCTION-2DPAGE; IPI00219713; -.
DR REPRODUCTION-2DPAGE; P02679; -.
DR SWISS-2DPAGE; P02679; -.
DR CPTAC; non-CPTAC-1121; -.
DR EPD; P02679; -.
DR jPOST; P02679; -.
DR MassIVE; P02679; -.
DR MaxQB; P02679; -.
DR PaxDb; P02679; -.
DR PeptideAtlas; P02679; -.
DR PRIDE; P02679; -.
DR ProteomicsDB; 51545; -. [P02679-1]
DR ProteomicsDB; 51546; -. [P02679-2]
DR ABCD; P02679; 9 sequenced antibodies.
DR Antibodypedia; 16774; 725 antibodies from 37 providers.
DR DNASU; 2266; -.
DR Ensembl; ENST00000336098.8; ENSP00000336829.3; ENSG00000171557.17. [P02679-1]
DR Ensembl; ENST00000404648.7; ENSP00000384860.3; ENSG00000171557.17. [P02679-2]
DR GeneID; 2266; -.
DR KEGG; hsa:2266; -.
DR MANE-Select; ENST00000336098.8; ENSP00000336829.3; NM_021870.3; NP_068656.2.
DR UCSC; uc003iog.4; human. [P02679-1]
DR CTD; 2266; -.
DR DisGeNET; 2266; -.
DR GeneCards; FGG; -.
DR HGNC; HGNC:3694; FGG.
DR HPA; ENSG00000171557; Tissue enriched (liver).
DR MalaCards; FGG; -.
DR MIM; 134850; gene.
DR MIM; 202400; phenotype.
DR MIM; 616004; phenotype.
DR neXtProt; NX_P02679; -.
DR OpenTargets; ENSG00000171557; -.
DR Orphanet; 98880; Familial afibrinogenemia.
DR Orphanet; 98881; Familial dysfibrinogenemia.
DR Orphanet; 248408; Familial hypodysfibrinogenemia.
DR Orphanet; 101041; Familial hypofibrinogenemia.
DR PharmGKB; PA430; -.
DR VEuPathDB; HostDB:ENSG00000171557; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158467; -.
DR HOGENOM; CLU_038628_13_0_1; -.
DR InParanoid; P02679; -.
DR OMA; TYHNGMR; -.
DR OrthoDB; 751651at2759; -.
DR PhylomeDB; P02679; -.
DR TreeFam; TF336658; -.
DR PathwayCommons; P02679; -.
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-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
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-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR SignaLink; P02679; -.
DR SIGNOR; P02679; -.
DR BioGRID-ORCS; 2266; 23 hits in 1068 CRISPR screens.
DR ChiTaRS; FGG; human.
DR EvolutionaryTrace; P02679; -.
DR GeneWiki; FGG; -.
DR GenomeRNAi; 2266; -.
DR Pharos; P02679; Tbio.
DR PRO; PR:P02679; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P02679; protein.
DR Bgee; ENSG00000171557; Expressed in right lobe of liver and 97 other tissues.
DR ExpressionAtlas; P02679; baseline and differential.
DR Genevisible; P02679; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
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:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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: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:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0005198; F:structural molecule activity; IDA:BHF-UCL.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:ComplexPortal.
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:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
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:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
DR GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; IDA:BHF-UCL.
DR GO; GO:0036345; P:platelet maturation; IEA:Ensembl.
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; IMP:BHF-UCL.
DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
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; IPR020837; Fibrinogen_CS.
DR InterPro; IPR037581; Fibrinogen_gamma.
DR PANTHER; PTHR19143:SF338; PTHR19143:SF338; 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; Alternative splicing; Blood coagulation; Calcium;
KW Coiled coil; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Hemostasis; Isopeptide bond; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:8509453, ECO:0000269|Ref.9"
FT CHAIN 27..453
FT /note="Fibrinogen gamma chain"
FT /id="PRO_0000009099"
FT DOMAIN 170..416
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 400..422
FT /note="Gamma-chain polymerization, binding amino end of
FT another fibrin alpha chain"
FT REGION 423..437
FT /note="Platelet aggregation and Staphylococcus clumping"
FT REGION 424..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719,
FT ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FID"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719,
FT ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FID"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719,
FT ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FID"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719,
FT ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FID"
FT SITE 84..85
FT /note="Cleavage; by plasmin; to break down fibrin clots"
FT SITE 88..89
FT /note="Cleavage; by plasmin; to break down fibrin clots"
FT SITE 102..103
FT /note="Cleavage; by hementin; to prevent blood coagulation"
FT MOD_RES 68
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 444
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:11307817"
FT MOD_RES 448
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:11307817"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine; in variant Asahi"
FT DISULFID 34
FT /note="Interchain (with C-35)"
FT /evidence="ECO:0000269|PubMed:19296670,
FT ECO:0007744|PDB:3GHG"
FT DISULFID 35
FT /note="Interchain (with C-34)"
FT /evidence="ECO:0000269|PubMed:19296670,
FT ECO:0007744|PDB:3GHG"
FT DISULFID 45
FT /note="Interchain (with C-110 in beta chain)"
FT /evidence="ECO:0000305|PubMed:6575689"
FT DISULFID 49
FT /note="Interchain (with C-64 in alpha chain)"
FT /evidence="ECO:0000305|PubMed:6575689"
FT DISULFID 161
FT /note="Interchain (with C-227 in beta chain)"
FT /evidence="ECO:0000305|PubMed:6575689"
FT DISULFID 165
FT /note="Interchain (with C-180 in alpha chain)"
FT /evidence="ECO:0000305|PubMed:6575689"
FT DISULFID 179..208
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719,
FT ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FID"
FT DISULFID 352..365
FT /evidence="ECO:0000269|PubMed:10074346,
FT ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719,
FT ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233,
FT ECO:0000269|PubMed:9628725, ECO:0007744|PDB:1FID"
FT CROSSLNK 424
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-432)"
FT CROSSLNK 432
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-424)"
FT VAR_SEQ 434..453
FT /note="VRPEHPAETEYDSLYPEDDL -> AGDV (in isoform Gamma-A)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2990550,
FT ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_001537"
FT VARIANT 77
FT /note="E -> G (in dbSNP:rs11551835)"
FT /id="VAR_049066"
FT VARIANT 140
FT /note="Y -> H (in dbSNP:rs2066870)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_033930"
FT VARIANT 191
FT /note="G -> R (in Milano-12; dbSNP:rs6063)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:11435303, ECO:0000269|Ref.6"
FT /id="VAR_014170"
FT VARIANT 301
FT /note="R -> C (in Tochigi/Osaka-2/Milano-5/Villajoyosa;
FT dbSNP:rs121913087)"
FT /evidence="ECO:0000269|PubMed:1421174,
FT ECO:0000269|PubMed:2971042, ECO:0000269|PubMed:3337908,
FT ECO:0000269|PubMed:7654933, ECO:0000269|PubMed:7841300"
FT /id="VAR_002409"
FT VARIANT 301
FT /note="R -> H (in DYSFIBRIN; fibrinogen Bergamo-2/Essen/
FT Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4;
FT dbSNP:rs121913088)"
FT /evidence="ECO:0000269|PubMed:1455400,
FT ECO:0000269|PubMed:2976995, ECO:0000269|PubMed:3563970,
FT ECO:0000269|PubMed:7654933"
FT /id="VAR_002410"
FT VARIANT 303
FT /note="T -> P (in CAFBN; hypofibrinogenemia; heterozygous;
FT no effect on fibrinogen complex assembly; impaired
FT fibrinogen complex secretion)"
FT /evidence="ECO:0000269|PubMed:25427968"
FT /id="VAR_072726"
FT VARIANT 318
FT /note="G -> V (in DYSFIBRIN; fibrinogen Baltimore-1;
FT impaired polymerization; dbSNP:rs121913089)"
FT /evidence="ECO:0000269|PubMed:2257302"
FT /id="VAR_002411"
FT VARIANT 327
FT /note="D -> H (in CAFBN; hypofibrinogenemia; heterozygous;
FT no effect on fibrinogen complex assembly; no effect on
FT fibrinogen complex secretion)"
FT /evidence="ECO:0000269|PubMed:25427968"
FT /id="VAR_072727"
FT VARIANT 334
FT /note="N -> I (in Baltimore-3; impaired polymerization;
FT dbSNP:rs121913090)"
FT /evidence="ECO:0000269|PubMed:2328317"
FT /id="VAR_002413"
FT VARIANT 334
FT /note="N -> K (in Kyoto-1; causes accelerated cleavage by
FT plasmin)"
FT /evidence="ECO:0000269|PubMed:1421174,
FT ECO:0000269|PubMed:2971046"
FT /id="VAR_002412"
FT VARIANT 335
FT /note="G -> D (in Hillsborough; prolonged thrombin clotting
FT time)"
FT /evidence="ECO:0000269|PubMed:11986213"
FT /id="VAR_015853"
FT VARIANT 336
FT /note="M -> T (in Asahi; impaired polymerization;
FT dbSNP:rs121913091)"
FT /evidence="ECO:0000269|PubMed:1421174,
FT ECO:0000269|PubMed:2496144"
FT /id="VAR_002414"
FT VARIANT 345..346
FT /note="Missing (in Vlissingen; defective calcium binding
FT and impaired polymerization)"
FT /evidence="ECO:0000269|PubMed:2071611"
FT /id="VAR_002415"
FT VARIANT 345
FT /note="N -> D (in CAFBN; hypofibrinogenemia; heterozygous;
FT no effect on fibrinogen complex assembly; decreased
FT fibrinogen complex secretion)"
FT /evidence="ECO:0000269|PubMed:25427968"
FT /id="VAR_072728"
FT VARIANT 355
FT /note="Q -> R (in Nagoya-1; impaired polymerization;
FT dbSNP:rs121913092)"
FT /evidence="ECO:0000269|PubMed:2738036"
FT /id="VAR_002416"
FT VARIANT 356
FT /note="D -> V (in DYSFIBRIN; fibrinogen Milano-1; impaired
FT polymerization; dbSNP:rs121913094)"
FT /evidence="ECO:0000269|PubMed:3708159"
FT /id="VAR_002418"
FT VARIANT 356
FT /note="D -> Y (in Kyoto-3; impaired polymerization;
FT dbSNP:rs121913093)"
FT /evidence="ECO:0000269|PubMed:1421174,
FT ECO:0000269|PubMed:2819242"
FT /id="VAR_002417"
FT VARIANT 363
FT /note="N -> K (in Bern-1; impaired polymerization)"
FT /evidence="ECO:0000269|PubMed:8400260"
FT /id="VAR_002419"
FT VARIANT 377
FT /note="G -> VMCGEALPMLKDPCYS (in Paris-1; impaired
FT polymerization)"
FT /evidence="ECO:0000269|PubMed:8470043"
FT /id="VAR_002420"
FT VARIANT 384
FT /note="S -> C (in Milano-7; impaired polymerization)"
FT /evidence="ECO:0000269|PubMed:8080993"
FT /id="VAR_002421"
FT VARIANT 401
FT /note="R -> G (in Osaka-5; dbSNP:rs75848804)"
FT /evidence="ECO:0000269|PubMed:1733971"
FT /id="VAR_002422"
FT VARIANT 401
FT /note="R -> W (in CAFBN; hypofibrinogenemia; heterozygous;
FT dbSNP:rs75848804)"
FT /evidence="ECO:0000269|PubMed:25427968"
FT /id="VAR_072729"
FT VARIANT 404
FT /note="S -> P (in DYSFIBRIN; fibrinogen Philadelphia;
FT dbSNP:rs587777720)"
FT /evidence="ECO:0000269|PubMed:15632207"
FT /id="VAR_072621"
FT VARIANT 410
FT /note="M -> V (in dbSNP:rs6061)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014171"
FT CONFLICT 114
FT /note="K -> I (in Ref. 2; AAB59530/AAB59531)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="R -> Y (in Ref. 15; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="Y -> R (in Ref. 15; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3GHG"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3GHG"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3GHG"
FT HELIX 49..94
FT /evidence="ECO:0007829|PDB:3GHG"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3GHG"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:1FZA"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:1FZB"
FT TURN 124..128
FT /evidence="ECO:0007829|PDB:1FZC"
FT HELIX 129..160
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2HLO"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:2FIB"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:2FIB"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1FID"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2HOD"
FT STRAND 216..226
FT /evidence="ECO:0007829|PDB:2FIB"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1FZC"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1FZA"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1RE3"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:2FIB"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2OYI"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:2FIB"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3HUS"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2FIB"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1FIB"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:1FZA"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:2FIB"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2H43"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2HOD"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:2H43"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1FIB"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:2FIB"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:2FIB"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:2FIB"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:1FID"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:4B60"
SQ SEQUENCE 453 AA; 51512 MW; 1787204904E0D4BB CRC64;
MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT
KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM
KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ
DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG
FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW
WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI
GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE DDL
