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Fibrinogen gamma chain

 FIBG_HUMAN              Reviewed;         453 AA.
P02679; A8K057; P04469; P04470; Q53Y18; Q96A14; Q96KJ3; Q9UC62;
Q9UC63; Q9UCF3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 3.
10-OCT-2018, entry version 232.
RecName: Full=Fibrinogen gamma chain;
Flags: Precursor;
Name=FGG; ORFNames=PRO2061;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6688357; DOI=10.1021/bi00282a033;
Chung D.W., Chan W.-Y., Davie E.W.;
"Characterization of a complementary deoxyribonucleic acid coding for
the gamma chain of human fibrinogen.";
Biochemistry 22:3250-3256(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-A AND
GAMMA-B).
PubMed=2990550; DOI=10.1021/bi00329a041;
Rixon M.W., Chung D.W., Davie E.W.;
"Nucleotide sequence of the gene for the gamma chain of human
fibrinogen.";
Biochemistry 24:2077-2086(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M.,
He F.;
"Functional prediction of the coding sequences of 33 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-140 AND ARG-191.
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 27-437.
Henschen A., Lottspeich F., Southan C., Topfer-Petersen E.;
"Human fibrinogen: sequence, sulfur bridges, glycosylation and some
structural variants.";
(In) Peeters H. (eds.);
Protides of the biological fluids, Proc. 28th colloquium, pp.51-56,
Pergamon Press, Oxford (1980).
[10]
PROTEIN SEQUENCE OF 27-41.
TISSUE=Platelet;
PubMed=8509453; DOI=10.1083/jcb.121.6.1329;
Bertagnolli M.E., Beckerle M.C.;
"Evidence for the selective association of a subpopulation of GPIIb-
IIIa with the actin cytoskeletons of thrombin-activated platelets.";
J. Cell Biol. 121:1329-1342(1993).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 75-286.
TISSUE=Liver;
PubMed=1685103; DOI=10.3109/10425179109020801;
Marchetti L., Zanelli T., Malcovati M., Tenchini M.L.;
"Polymorphism of the human gamma chain fibrinogen gene.";
DNA Seq. 1:419-422(1991).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 209-270.
PubMed=6689067; DOI=10.1093/nar/11.21.7427;
Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S.;
"Isolation and characterisation of cDNA clones for the A alpha- and
gamma-chains of human fibrinogen.";
Nucleic Acids Res. 11:7427-7434(1983).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-437 (ISOFORMS GAMMA-A AND
GAMMA-B).
PubMed=6092346;
Fornace A.J. Jr., Cummings D.E., Comeau C.M., Kant J.A.,
Crabtree G.R.;
"Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing
near the 3' end of the gene produces gamma A and gamma B forms of
gamma-fibrinogen.";
J. Biol. Chem. 259:12826-12830(1984).
[14]
PROTEIN SEQUENCE OF 291-310, AND VARIANTS BARCELONA-3/BARCELONA-4
HIS-301 AND VILLAJOYOSA CYS-301.
TISSUE=Blood;
PubMed=7654933;
Borrell M., Gari M., Coll I., Vallve C., Tirado I., Soria J.M.,
Sala N., Munoz C., Oliver A., Garcia A.;
"Abnormal polymerization and normal binding of plasminogen and t-PA in
three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg
275-->His) and Villajoyosa (gamma Arg 275-->Cys).";
Blood Coagul. Fibrinolysis 6:198-206(1995).
[15]
PROTEIN SEQUENCE OF 411-453 (ISOFORM GAMMA-B).
PubMed=7306501; DOI=10.1021/bi00524a036;
Wolfenstein-Todel C., Mosesson M.W.;
"Carboxy-terminal amino acid sequence of a human fibrinogen gamma-
chain variant (gamma').";
Biochemistry 20:6146-6149(1981).
[16]
REVIEW, AND DISULFIDE BONDS.
PubMed=6575689; DOI=10.1111/j.1749-6632.1983.tb23232.x;
Henschen A., Lottspeich F., Kehl M., Southan C.;
"Covalent structure of fibrinogen.";
Ann. N. Y. Acad. Sci. 408:28-43(1983).
[17]
DISULFIDE BONDS.
Doolittle R.F., Takagi T., Watt K.W.K., Bouma H. III, Cottrell B.A.,
Cassman K.G., Goldbaum D.M., Doolittle L.R., Friezner S.J.;
"The structures of fibrinogen and fibrin.";
(In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H.
(eds.);
Regulatory proteolytic enzymes and their inhibitors, pp.163-172,
Pergamon Press, New York (1978).
[18]
DISULFIDE BONDS.
PubMed=936108; DOI=10.1016/0049-3848(76)90245-0;
Blombaeck B., Hessel B., Hogg D.;
"Disulfide bridges in NH2-terminal part of human fibrinogen.";
Thromb. Res. 8:639-658(1976).
[19]
QUATERNARY STRUCTURE, AND DISULFIDE BONDS.
PubMed=6860649; DOI=10.1021/bi00278a003;
Hoeprich P.D., Doolittle R.F.;
"Dimeric half-molecules of human fibrinogen are joined through
disulfide bonds in an antiparallel orientation.";
Biochemistry 22:2049-2055(1983).
[20]
SULFATION.
PubMed=1892842; DOI=10.1021/bi00103a004;
Farrel D.H., Mulvihill E.R., Huang S., Chung D.W., Davie E.W.;
"Recombinant human fibrinogen and sulfation of the gamma' chain.";
Biochemistry 30:9414-9420(1991).
[21]
SULFATION AT TYR-444 AND TYR-448.
PubMed=11307817;
Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., Mosesson M.W.;
"The amino acid sequence in fibrin responsible for high affinity
thrombin binding.";
Thromb. Haemost. 85:470-474(2001).
[22]
REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, AND LIGANDS.
PubMed=6383194; DOI=10.1146/annurev.bi.53.070184.001211;
Doolittle R.F.;
"Fibrinogen and fibrin.";
Annu. Rev. Biochem. 53:195-229(1984).
[23]
POLYMERIZATION SITE.
PubMed=6592597; DOI=10.1073/pnas.81.19.5980;
Horwitz B.H., Varadi A., Scheraga H.A.;
"Localization of a fibrin gamma-chain polymerization site within
segment Thr-374 to Glu-396 of human fibrinogen.";
Proc. Natl. Acad. Sci. U.S.A. 81:5980-5984(1984).
[24]
POLYMERIZATION SITE.
PubMed=6451630;
Olexa S.A., Budzynski A.Z.;
"Localization of a fibrin polymerization site.";
J. Biol. Chem. 256:3544-3549(1981).
[25]
PLATELET AGGREGATION SITE.
PubMed=6326808; DOI=10.1021/bi00303a028;
Kloczewiak M., Timmons S., Lukas T.J., Hawiger J.;
"Platelet receptor recognition site on human fibrinogen. Synthesis and
structure-function relationship of peptides corresponding to the
carboxy-terminal segment of the gamma chain.";
Biochemistry 23:1767-1774(1984).
[26]
PLATELET AGGREGATION SITE.
PubMed=6325435;
Plow E.F., Srouji A.H., Meyer D., Marguerie G., Ginsberg M.H.;
"Evidence that three adhesive proteins interact with a common
recognition site on activated platelets.";
J. Biol. Chem. 259:5388-5391(1984).
[27]
CALCIUM-BINDING SITE.
PubMed=3160702;
Dang C.V., Ebert R.F., Bell W.R.;
"Localization of a fibrinogen calcium binding site between gamma-
subunit positions 311 and 336 by terbium fluorescence.";
J. Biol. Chem. 260:9713-9719(1985).
[28]
CHROMATOGRAPHIC COMPARISON OF GAMMA-A AND GAMMA-B CHAINS.
PubMed=6933547; DOI=10.1073/pnas.77.9.5069;
Wolfenstein-Todel C., Mosesson M.W.;
"Human plasma fibrinogen heterogeneity: evidence for an extended
carboxyl-terminal sequence in a normal gamma chain variant (gamma').";
Proc. Natl. Acad. Sci. U.S.A. 77:5069-5073(1980).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[30]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[32]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[33]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[34]
GLYCOSYLATION AT ASN-78.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[35]
CLEAVAGE BY HEMENTIN AND PLASMIN.
PubMed=2143188;
Kirschbaum N.E., Budzynski A.Z.;
"A unique proteolytic fragment of human fibrinogen containing the A
alpha COOH-terminal domain of the native molecule.";
J. Biol. Chem. 265:13669-13676(1990).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[38]
PHOSPHORYLATION AT SER-68.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[39]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 169-433 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, AND SUBUNIT.
PubMed=9016719; DOI=10.1016/S0969-2126(97)00171-8;
Yee V.C., Pratt K.P., Cote H.C.F., le Trong I., Chung D.W.,
Davie E.W., Stenkamp R.E., Teller D.C.;
"Crystal structure of a 30 kDa C-terminal fragment from the gamma
chain of human fibrinogen.";
Structure 5:125-138(1997).
[40]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 169-433 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, AND SUBUNIT.
PubMed=9207064; DOI=10.1073/pnas.94.14.7176;
Pratt K.P., Cote H.C.F., Chung D.W., Stenkamp R.E., Davie E.W.;
"The primary fibrin polymerization pocket: three-dimensional structure
of a 30-kDa C-terminal gamma chain fragment complexed with the peptide
Gly-Pro-Arg-Pro.";
Proc. Natl. Acad. Sci. U.S.A. 94:7176-7181(1997).
[41]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 114-432 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, AND SUBUNIT.
PubMed=9333233; DOI=10.1038/38947;
Spraggon G., Everse S.J., Doolittle R.F.;
"Crystal structures of fragment D from human fibrinogen and its
crosslinked counterpart from fibrin.";
Nature 389:455-462(1997).
[42]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 114-432 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=9628725; DOI=10.1021/bi9804129;
Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F.;
"Crystal structure of fragment double-D from human fibrin with two
different bound ligands.";
Biochemistry 37:8637-8642(1998).
[43]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 114-432 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=10074346; DOI=10.1021/bi982626w;
Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F.;
"Conformational changes in fragments D and double-D from human
fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.";
Biochemistry 38:2941-2946(1999).
[44]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 27-433 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=19296670; DOI=10.1021/bi802205g;
Kollman J.M., Pandi L., Sawaya M.R., Riley M., Doolittle R.F.;
"Crystal structure of human fibrinogen.";
Biochemistry 48:3877-3886(2009).
[45]
VARIANT ASAHI THR-336.
PubMed=2496144; DOI=10.1172/JCI114056;
Yamazumi K., Shimura K., Terukina S., Takahashi N., Matsuda M.;
"A gamma methionine-310 to threonine substitution and consequent N-
glycosylation at gamma asparagine-308 identified in a congenital
dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen
Asahi.";
J. Clin. Invest. 83:1590-1597(1989).
[46]
VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3
TYR-356.
PubMed=1421174;
Mimuro J., Muramatsu S., Maekawa H., Sakata Y., Kaneko M.,
Yoshitake S., Okuma M., Ito Y., Takeda Y., Matsuda M.;
"Gene analyses of abnormal fibrinogens with a mutation in the gamma
chain.";
Int. J. Hematol. 56:129-134(1992).
[47]
INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN VAL-318.
PubMed=2257302;
Bantia S., Mane S.M., Bell W.R., Dang C.V.;
"Fibrinogen Baltimore I: polymerization defect associated with a gamma
292Gly-->Val (GGC-->GTC) mutation.";
Blood 76:2279-2283(1990).
[48]
VARIANT BALTIMORE-3 ILE-334.
PubMed=2328317;
Bantia S., Bell W.R., Dang C.V.;
"Polymerization defect of fibrinogen Baltimore III due to a gamma
Asn308-->Ile mutation.";
Blood 75:1659-1663(1990).
[49]
VARIANT BERN-1 LYS-363.
PubMed=8400260;
Steinmann C., Reber P., Jungo M., Laemmle B., Heinemann G.,
Wermuth B., Furlan M.;
"Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible
for defective fibrin monomer polymerization.";
Blood 82:2104-2108(1993).
[50]
VARIANT KYOTO-1 LYS-334.
PubMed=2971046;
Yoshida N., Terukina S., Okuma M., Moroi M., Aoki N., Matsuda M.;
"Characterization of an apparently lower molecular weight gamma-chain
variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308
by lysine which causes accelerated cleavage of fragment D1 by plasmin
and the generation of a new plasmin cleavage site.";
J. Biol. Chem. 263:13848-13856(1988).
[51]
VARIANT KYOTO-3 TYR-356.
PubMed=2819242;
Terukina S., Yamazumi K., Okamoto K., Yamashita H., Ito Y.,
Matsuda M.;
"Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma
aspartic acid-330 to tyrosine substitution manifesting impaired fibrin
monomer polymerization.";
Blood 74:2681-2687(1989).
[52]
VARIANT DYSFIBRIN VAL-356.
PubMed=3708159;
Reber P., Furlan M., Rupp C., Kehl M., Henschen A., Mannucci P.M.,
Beck E.A.;
"Characterization of fibrinogen Milano I: amino acid exchange gamma
330 Asp-->Val impairs fibrin polymerization.";
Blood 67:1751-1756(1986).
[53]
VARIANT MILANO-5 CYS-301.
PubMed=7841300;
Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G.,
Wermuth B., Redaelli R., Baudo F., Furlan M.;
"Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275
Arg-->Cys substitution.";
Blood Coagul. Fibrinolysis 5:463-471(1994).
[54]
VARIANT MILANO-7 CYS-384.
PubMed=8080993;
Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G.,
Wermuth B., Redaelli R., Baudo F., Furlan M.;
"A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII
causes defective fibrin polymerization.";
Blood 84:1874-1880(1994).
[55]
VARIANT NAGOYA-1 ARG-355.
PubMed=2738036; DOI=10.1093/oxfordjournals.jbchem.a122601;
Miyata T., Furukawa K., Iwanaga S., Takamatsu J., Saito H.;
"Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the
gamma-chain that impairs the polymerization of fibrin monomer.";
J. Biochem. 105:10-14(1989).
[56]
VARIANT OSAKA-2 CYS-301.
PubMed=2971042;
Terukina S., Matsuda M., Hirata H., Takeda Y., Miyata T., Takao T.,
Shimonishi Y.;
"Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen,
'fibrinogen Osaka II'. Evidence for a unique solitary cystine
structure at the mutation site.";
J. Biol. Chem. 263:13579-13587(1988).
[57]
VARIANT OSAKA-3 HIS-301.
PubMed=1455400;
Yoshida N., Imoka S., Hirata H., Matsuda M., Asakura S.;
"Heterozygous abnormal fibrinogen Osaka III with the replacement of
gamma arginine-275 by histidine has an apparently higher molecular
weight gamma-chain variant.";
Thromb. Haemost. 68:534-538(1992).
[58]
VARIANT OSAKA-5 GLY-401.
PubMed=1733971;
Yoshida N., Hirata H., Morigami Y., Imaoka S., Matsuda M.,
Yamazumi K., Asakura S.;
"Characterization of an abnormal fibrinogen Osaka V with the
replacement of gamma-arginine 375 by glycine. The lack of high
affinity calcium binding to D-domains and the lack of protective
effect of calcium on fibrinolysis.";
J. Biol. Chem. 267:2753-2759(1992).
[59]
VARIANT PARIS-1 GLY-377 DELINS
VAL-MET-CYS-GLY-GLU-ALA-LEU-PRO-MET-LEU-LYS-ASP-PRO-CYS-TYR-SER.
PubMed=8470043;
Rosenberg J.B., Newman P.J., Mosesson M.W., Guillin M.-C.,
Amrani D.L.;
"Paris I dysfibrinogenemia: a point mutation in intron 8 results in
insertion of a 15 amino acid sequence in the fibrinogen gamma-chain.";
Thromb. Haemost. 69:217-220(1993).
[60]
VARIANT TOCHIGI CYS-301.
PubMed=3337908;
Yoshida N., Ota K., Moroi M., Matsuda M.;
"An apparently higher molecular weight gamma-chain variant in a new
congenital abnormal fibrinogen Tochigi characterized by the
replacement of gamma arginine-275 by cysteine.";
Blood 71:480-487(1988).
[61]
VARIANT VLISSINGEN 345-ASN-ASP-346 DEL.
PubMed=2071611;
Koopman J., Haverkate F., Briet E., Lord S.T.;
"A congenitally abnormal fibrinogen (Vlissingen) with a 6-base
deletion in the gamma-chain gene, causing defective calcium binding
and impaired fibrin polymerization.";
J. Biol. Chem. 266:13456-13461(1991).
[62]
VARIANT BERGAMO-2/ESSEN/HAIFA/PERUGIA HIS-301.
PubMed=3563970;
Reber P., Furlan M., Henschen A., Kaudewitz H., Barbui T., Hilgard P.,
Nenci G.G., Berrettini M., Beck E.A.;
"Three abnormal fibrinogen variants with the same amino acid
substitution (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and
Perugia.";
Thromb. Haemost. 56:401-406(1986).
[63]
INVOLVEMENT IN DYSFIBRIN, AND VARIANT DYSFIBRIN HIS-301.
PubMed=2976995;
Yamazumi K., Terukina S., Onohara S., Matsuda M.;
"Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen
Saga' with an Arg-275 to His substitution.";
Thromb. Haemost. 60:476-480(1988).
[64]
VARIANT MILANO-12 ARG-191.
PubMed=11435303; DOI=10.1182/blood.V98.2.351;
Bolliger-Stucki B., Lord S.T., Furlan M.;
"Fibrinogen Milano XII: a dysfunctional variant containing 2 amino
acid substitutions, A-alpha R16C and gamma G165R.";
Blood 98:351-357(2001).
[65]
VARIANTS ARG-191 AND VAL-410.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[66]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[67]
VARIANT HILLSBOROUGH ASP-335.
PubMed=11986213; DOI=10.1182/blood.V99.10.3597;
Mullin J.L., Brennan S.O., Ganly P.S., George P.M.;
"Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with
impaired clotting.";
Blood 99:3597-3601(2002).
[68]
VARIANT DYSFIBRIN PRO-404.
PubMed=15632207; DOI=10.1182/blood-2004-04-1621;
Keller M.A., Martinez J., Baradet T.C., Nagaswami C., Chernysh I.N.,
Borowski M.K., Surrey S., Weisel J.W.;
"Fibrinogen Philadelphia, a hypodysfibrinogenemia characterized by
abnormal polymerization and fibrinogen hypercatabolism due to gamma
S378P mutation.";
Blood 105:3162-3168(2005).
[69]
INVOLVEMENT IN CAFBN; VARIANTS CAFBN PRO-303; HIS-327; ASP-345 AND
TRP-401, AND CHARACTERIZATION OF VARIANTS CAFBN PRO-303; HIS-327 AND
ASP-345.
PubMed=25427968; DOI=10.1160/TH14-07-0629;
Asselta R., Plate M., Robusto M., Borhany M., Guella I., Solda G.,
Afrasiabi A., Menegatti M., Shamsi T., Peyvandi F., Duga S.;
"Clinical and molecular characterisation of 21 patients affected by
quantitative fibrinogen deficiency.";
Thromb. Haemost. 113:567-576(2015).
-!- FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta
(FGB), polymerizes to form an insoluble fibrin matrix. Has a major
function in hemostasis as one of the primary components of blood
clots. In addition, functions during the early stages of wound
repair to stabilize the lesion and guide cell migration during re-
epithelialization. Was originally thought to be essential for
platelet aggregation, based on in vitro studies using
anticoagulated blood. However, subsequent studies have shown that
it is not absolutely required for thrombus formation in vivo.
Enhances expression of SELP in activated platelets via an ITGB3-
dependent pathway. Maternal fibrinogen is essential for successful
pregnancy. Fibrin deposition is also associated with infection,
where it protects against IFNG-mediated hemorrhage. May also
facilitate the antibacterial immune response via both innate and
T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
-!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3
non-identical chains (alpha, beta and gamma). The 2 heterotrimers
are in head to head conformation with the N-termini in a small
central domain. {ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:6860649,
ECO:0000269|PubMed:9016719, ECO:0000269|PubMed:9207064,
ECO:0000269|PubMed:9333233, ECO:0000269|PubMed:9628725}.
-!- INTERACTION:
P75358:gapA (xeno); NbExp=2; IntAct=EBI-1034422, EBI-2259469;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Gamma-B; Synonyms=Gamma';
IsoId=P02679-1; Sequence=Displayed;
Note=Present in about 10% of the fibrinogen molecules in plasma
but absent from those in the platelets.;
Name=Gamma-A;
IsoId=P02679-2; Sequence=VSP_001537;
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
{ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9628725}.
-!- DOMAIN: A long coiled coil structure formed by 3 polypeptide
chains connects the central nodule to the C-terminal domains
(distal nodules). The long C-terminal ends of the alpha chains
fold back, contributing a fourth strand to the coiled coil
structure. {ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9628725}.
-!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin,
which cleaves fibrinopeptides A and B from alpha and beta chains,
and thus exposes the N-terminal polymerization sites responsible
for the formation of the soft clot. The soft clot is converted
into the hard clot by factor XIIIA which catalyzes the epsilon-
(gamma-glutamyl)lysine cross-linking between gamma chains
(stronger) and between alpha chains (weaker) of different
monomers. {ECO:0000269|PubMed:2143188}.
-!- PTM: Sulfation of C-terminal tyrosines increases affinity for
thrombin. {ECO:0000269|PubMed:11307817,
ECO:0000269|PubMed:1892842}.
-!- DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare
autosomal recessive disorder is characterized by bleeding that
varies from mild to severe and by complete absence or extremely
low levels of plasma and platelet fibrinogen.
{ECO:0000269|PubMed:25427968}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Patients
with congenital fibrinogen abnormalities can manifest different
clinical pictures. Some cases are clinically silent, some show a
tendency toward bleeding and some show a predisposition for
thrombosis with or without bleeding.
-!- DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A
disorder characterized by qualitative abnormalities
(dysfibrinogenemia) of the circulating fibrinogen. Affected
individuals are frequently asymptomatic, but some patients have
bleeding diathesis, thromboembolic complications, or both. In some
cases, dysfibrinogenemia is associated with low circulating
fibrinogen levels (hypodysfibrinogenemia).
{ECO:0000269|PubMed:15632207, ECO:0000269|PubMed:2257302,
ECO:0000269|PubMed:2976995, ECO:0000269|PubMed:3708159}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: The gamma-chain carries the main binding site for
the platelet receptor.
-!- WEB RESOURCE: Name=Wikipedia; Note=Fibrinogen entry;
URL="https://en.wikipedia.org/wiki/Fibrinogen";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/fgg/";
-----------------------------------------------------------------------
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EMBL; M10014; AAB59530.1; -; Genomic_DNA.
EMBL; M10014; AAB59531.1; -; Genomic_DNA.
EMBL; AF118092; AAF22036.1; -; mRNA.
EMBL; AF350254; AAK19751.2; -; Genomic_DNA.
EMBL; AF350254; AAK19752.2; -; Genomic_DNA.
EMBL; AK289422; BAF82111.1; -; mRNA.
EMBL; AK290824; BAF83513.1; -; mRNA.
EMBL; BT007081; AAP35744.1; -; mRNA.
EMBL; CH471056; EAX04917.1; -; Genomic_DNA.
EMBL; CH471056; EAX04919.1; -; Genomic_DNA.
EMBL; BC007044; AAH07044.1; -; mRNA.
EMBL; BC021674; AAH21674.1; -; mRNA.
EMBL; X51473; CAA35837.1; -; mRNA.
EMBL; X00086; CAA24944.1; -; mRNA.
EMBL; K02569; AAA52430.1; -; Genomic_DNA.
EMBL; K02569; AAA52431.1; -; Genomic_DNA.
CCDS; CCDS3788.1; -. [P02679-1]
CCDS; CCDS47153.1; -. [P02679-2]
PIR; A90470; FGHUG.
PIR; A90494; FGHUGB.
RefSeq; NP_000500.2; NM_000509.5. [P02679-2]
RefSeq; NP_068656.2; NM_021870.2. [P02679-1]
UniGene; Hs.727584; -.
PDB; 1DUG; X-ray; 1.80 A; A/B=424-433.
PDB; 1FIB; X-ray; 2.10 A; A=169-433.
PDB; 1FIC; X-ray; 2.50 A; A/B=169-433.
PDB; 1FID; X-ray; 2.10 A; A=169-433.
PDB; 1FZA; X-ray; 2.90 A; C/F=114-432.
PDB; 1FZB; X-ray; 2.90 A; C/F=114-432.
PDB; 1FZC; X-ray; 2.30 A; C/F=114-432.
PDB; 1FZE; X-ray; 3.00 A; C/F=114-432.
PDB; 1FZF; X-ray; 2.70 A; C/F=114-432.
PDB; 1FZG; X-ray; 2.50 A; C/F=114-432.
PDB; 1LT9; X-ray; 2.80 A; C/F=122-432.
PDB; 1LTJ; X-ray; 2.80 A; C/F=122-432.
PDB; 1N86; X-ray; 3.20 A; C/F=114-433.
PDB; 1N8E; X-ray; 4.50 A; C/F=114-433.
PDB; 1RE3; X-ray; 2.45 A; C/F=122-432.
PDB; 1RE4; X-ray; 2.70 A; C/F=122-432.
PDB; 1RF0; X-ray; 2.81 A; C/F=122-432.
PDB; 1RF1; X-ray; 2.53 A; C/F=122-432.
PDB; 2A45; X-ray; 3.65 A; I/L=27-71.
PDB; 2FFD; X-ray; 2.89 A; C/F=122-432.
PDB; 2FIB; X-ray; 2.01 A; A=169-433.
PDB; 2H43; X-ray; 2.70 A; C/F=115-433.
PDB; 2HLO; X-ray; 2.60 A; C/F=114-433.
PDB; 2HOD; X-ray; 2.90 A; C/F/I/L=115-433.
PDB; 2HPC; X-ray; 2.90 A; C/F/I/L=115-433.
PDB; 2HWL; X-ray; 2.40 A; P=439-452.
PDB; 2OYH; X-ray; 2.40 A; C/F=122-432.
PDB; 2OYI; X-ray; 2.70 A; C/F=122-432.
PDB; 2Q9I; X-ray; 2.80 A; C/F=114-433.
PDB; 2VDO; X-ray; 2.51 A; C=426-433.
PDB; 2VDP; X-ray; 2.80 A; C=428-433.
PDB; 2VDQ; X-ray; 2.59 A; C=426-433.
PDB; 2VDR; X-ray; 2.40 A; C=428-433.
PDB; 2VR3; X-ray; 1.95 A; C/D=425-433.
PDB; 2XNX; X-ray; 3.30 A; C/F/I/L=114-432.
PDB; 2XNY; X-ray; 7.50 A; C/F=114-432.
PDB; 2Y7L; X-ray; 1.49 A; B=421-433.
PDB; 2Z4E; X-ray; 2.70 A; C/F=114-433.
PDB; 3BVH; X-ray; 2.60 A; C/F=128-420.
PDB; 3E1I; X-ray; 2.30 A; C/F=114-432.
PDB; 3FIB; X-ray; 2.10 A; A=170-418.
PDB; 3GHG; X-ray; 2.90 A; C/F/I/L=27-433.
PDB; 3H32; X-ray; 3.60 A; C/F=121-433.
PDB; 3HUS; X-ray; 3.04 A; C/F=122-432.
PDB; 4B60; X-ray; 1.83 A; C/D=421-433.
PDBsum; 1DUG; -.
PDBsum; 1FIB; -.
PDBsum; 1FIC; -.
PDBsum; 1FID; -.
PDBsum; 1FZA; -.
PDBsum; 1FZB; -.
PDBsum; 1FZC; -.
PDBsum; 1FZE; -.
PDBsum; 1FZF; -.
PDBsum; 1FZG; -.
PDBsum; 1LT9; -.
PDBsum; 1LTJ; -.
PDBsum; 1N86; -.
PDBsum; 1N8E; -.
PDBsum; 1RE3; -.
PDBsum; 1RE4; -.
PDBsum; 1RF0; -.
PDBsum; 1RF1; -.
PDBsum; 2A45; -.
PDBsum; 2FFD; -.
PDBsum; 2FIB; -.
PDBsum; 2H43; -.
PDBsum; 2HLO; -.
PDBsum; 2HOD; -.
PDBsum; 2HPC; -.
PDBsum; 2HWL; -.
PDBsum; 2OYH; -.
PDBsum; 2OYI; -.
PDBsum; 2Q9I; -.
PDBsum; 2VDO; -.
PDBsum; 2VDP; -.
PDBsum; 2VDQ; -.
PDBsum; 2VDR; -.
PDBsum; 2VR3; -.
PDBsum; 2XNX; -.
PDBsum; 2XNY; -.
PDBsum; 2Y7L; -.
PDBsum; 2Z4E; -.
PDBsum; 3BVH; -.
PDBsum; 3E1I; -.
PDBsum; 3FIB; -.
PDBsum; 3GHG; -.
PDBsum; 3H32; -.
PDBsum; 3HUS; -.
PDBsum; 4B60; -.
ProteinModelPortal; P02679; -.
SMR; P02679; -.
BioGrid; 108557; 28.
ComplexPortal; CPX-1922; Fibrinogen.
CORUM; P02679; -.
DIP; DIP-29644N; -.
IntAct; P02679; 14.
STRING; 9606.ENSP00000336829; -.
ChEMBL; CHEMBL2364709; -.
DrugBank; DB00364; Sucralfate.
CarbonylDB; P02679; -.
GlyConnect; 157; -.
GlyConnect; 160; -.
iPTMnet; P02679; -.
PhosphoSitePlus; P02679; -.
UniCarbKB; P02679; -.
BioMuta; FGG; -.
DMDM; 20178280; -.
DOSAC-COBS-2DPAGE; P02679; -.
OGP; P02679; -.
REPRODUCTION-2DPAGE; IPI00219713; -.
REPRODUCTION-2DPAGE; P02679; -.
SWISS-2DPAGE; P02679; -.
MaxQB; P02679; -.
PaxDb; P02679; -.
PeptideAtlas; P02679; -.
PRIDE; P02679; -.
ProteomicsDB; 51545; -.
ProteomicsDB; 51546; -. [P02679-2]
DNASU; 2266; -.
Ensembl; ENST00000336098; ENSP00000336829; ENSG00000171557. [P02679-1]
Ensembl; ENST00000404648; ENSP00000384860; ENSG00000171557. [P02679-2]
GeneID; 2266; -.
KEGG; hsa:2266; -.
UCSC; uc003iog.4; human. [P02679-1]
CTD; 2266; -.
DisGeNET; 2266; -.
EuPathDB; HostDB:ENSG00000171557.16; -.
GeneCards; FGG; -.
HGNC; HGNC:3694; FGG.
HPA; CAB033120; -.
HPA; HPA027529; -.
MalaCards; FGG; -.
MIM; 134850; gene.
MIM; 202400; phenotype.
MIM; 616004; phenotype.
neXtProt; NX_P02679; -.
OpenTargets; ENSG00000171557; -.
Orphanet; 98880; Familial afibrinogenemia.
Orphanet; 98881; Familial dysfibrinogenemia.
Orphanet; 248408; Familial hypodysfibrinogenemia.
Orphanet; 101041; Familial hypofibrinogenemia.
PharmGKB; PA430; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00920000148942; -.
HOVERGEN; HBG099783; -.
InParanoid; P02679; -.
KO; K03905; -.
PhylomeDB; P02679; -.
TreeFam; TF336658; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P02679; -.
ChiTaRS; FGG; human.
EvolutionaryTrace; P02679; -.
GeneWiki; FGG; -.
GenomeRNAi; 2266; -.
PMAP-CutDB; P02679; -.
PRO; PR:P02679; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000171557; Expressed in 105 organ(s), highest expression level in liver.
CleanEx; HS_FGG; -.
ExpressionAtlas; P02679; baseline and differential.
Genevisible; P02679; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005577; C:fibrinogen complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031091; C:platelet alpha granule; IDA:BHF-UCL.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
GO; GO:0005198; F:structural molecule activity; IDA:BHF-UCL.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IDA:BHF-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0034622; P:cellular protein-containing complex assembly; IDA:BHF-UCL.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0036345; P:platelet maturation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0045921; P:positive regulation of exocytosis; IDA:BHF-UCL.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; NAS:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; IDA:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0051258; P:protein polymerization; IMP:BHF-UCL.
GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
CDD; cd00087; FReD; 1.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR020837; Fibrinogen_CS.
InterPro; IPR037581; Fibrinogen_gamma.
PANTHER; PTHR19143:SF338; PTHR19143:SF338; 1.
Pfam; PF08702; Fib_alpha; 1.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SMART; SM01212; Fib_alpha; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00514; FIBRINOGEN_C_1; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation; Calcium;
Coiled coil; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Hemostasis;
Isopeptide bond; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal; Sulfation.
SIGNAL 1 26 {ECO:0000269|PubMed:8509453,
ECO:0000269|Ref.9}.
CHAIN 27 453 Fibrinogen gamma chain.
/FTId=PRO_0000009099.
DOMAIN 170 416 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
REGION 400 422 Gamma-chain polymerization, binding amino
end of another fibrin alpha chain.
REGION 423 437 Platelet aggregation and Staphylococcus
clumping.
METAL 344 344 Calcium. {ECO:0000244|PDB:1FID,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9016719,
ECO:0000269|PubMed:9207064,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
METAL 346 346 Calcium. {ECO:0000244|PDB:1FID,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9016719,
ECO:0000269|PubMed:9207064,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
METAL 348 348 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1FID,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9016719,
ECO:0000269|PubMed:9207064,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
METAL 350 350 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1FID,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9016719,
ECO:0000269|PubMed:9207064,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
SITE 84 85 Cleavage; by plasmin; to break down
fibrin clots.
SITE 88 89 Cleavage; by plasmin; to break down
fibrin clots.
SITE 102 103 Cleavage; by hementin; to prevent blood
coagulation.
MOD_RES 68 68 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 444 444 Sulfotyrosine.
{ECO:0000269|PubMed:11307817}.
MOD_RES 448 448 Sulfotyrosine.
{ECO:0000269|PubMed:11307817}.
CARBOHYD 78 78 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine; in
variant Asahi.
DISULFID 34 34 Interchain (with C-35).
{ECO:0000244|PDB:3GHG,
ECO:0000269|PubMed:19296670}.
DISULFID 35 35 Interchain (with C-34).
{ECO:0000244|PDB:3GHG,
ECO:0000269|PubMed:19296670}.
DISULFID 45 45 Interchain (with C-110 in beta chain).
{ECO:0000305|PubMed:6575689}.
DISULFID 49 49 Interchain (with C-64 in alpha chain).
{ECO:0000305|PubMed:6575689}.
DISULFID 161 161 Interchain (with C-227 in beta chain).
{ECO:0000305|PubMed:6575689}.
DISULFID 165 165 Interchain (with C-180 in alpha chain).
{ECO:0000305|PubMed:6575689}.
DISULFID 179 208 {ECO:0000244|PDB:1FID,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9016719,
ECO:0000269|PubMed:9207064,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
DISULFID 352 365 {ECO:0000244|PDB:1FID,
ECO:0000269|PubMed:10074346,
ECO:0000269|PubMed:19296670,
ECO:0000269|PubMed:9016719,
ECO:0000269|PubMed:9207064,
ECO:0000269|PubMed:9333233,
ECO:0000269|PubMed:9628725}.
CROSSLNK 424 424 Isoglutamyl lysine isopeptide (Gln-Lys)
(interchain with K-432).
CROSSLNK 432 432 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-424).
VAR_SEQ 434 453 VRPEHPAETEYDSLYPEDDL -> AGDV (in isoform
Gamma-A). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2990550,
ECO:0000303|Ref.4, ECO:0000303|Ref.5}.
/FTId=VSP_001537.
VARIANT 77 77 E -> G (in dbSNP:rs11551835).
/FTId=VAR_049066.
VARIANT 140 140 Y -> H (in dbSNP:rs2066870).
{ECO:0000269|Ref.6}.
/FTId=VAR_033930.
VARIANT 191 191 G -> R (in Milano-12; dbSNP:rs6063).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11435303,
ECO:0000269|Ref.6}.
/FTId=VAR_014170.
VARIANT 301 301 R -> C (in Tochigi/Osaka-2/Milano-5/
Villajoyosa; dbSNP:rs121913087).
{ECO:0000269|PubMed:1421174,
ECO:0000269|PubMed:2971042,
ECO:0000269|PubMed:3337908,
ECO:0000269|PubMed:7654933,
ECO:0000269|PubMed:7841300}.
/FTId=VAR_002409.
VARIANT 301 301 R -> H (in DYSFIBRIN; fibrinogen Bergamo-
2/Essen/Haifa/Osaka-3/Perugia/Saga/
Barcelona-3/Barcelona-4;
dbSNP:rs121913088).
{ECO:0000269|PubMed:1455400,
ECO:0000269|PubMed:2976995,
ECO:0000269|PubMed:3563970,
ECO:0000269|PubMed:7654933}.
/FTId=VAR_002410.
VARIANT 303 303 T -> P (in CAFBN; hypofibrinogenemia;
heterozygous; no effect on fibrinogen
complex assembly; impaired fibrinogen
complex secretion).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072726.
VARIANT 318 318 G -> V (in DYSFIBRIN; fibrinogen
Baltimore-1; impaired polymerization;
dbSNP:rs121913089).
{ECO:0000269|PubMed:2257302}.
/FTId=VAR_002411.
VARIANT 327 327 D -> H (in CAFBN; hypofibrinogenemia;
heterozygous; no effect on fibrinogen
complex assembly; no effect on fibrinogen
complex secretion).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072727.
VARIANT 334 334 N -> I (in Baltimore-3; impaired
polymerization; dbSNP:rs121913090).
{ECO:0000269|PubMed:2328317}.
/FTId=VAR_002413.
VARIANT 334 334 N -> K (in Kyoto-1; causes accelerated
cleavage by plasmin).
{ECO:0000269|PubMed:1421174,
ECO:0000269|PubMed:2971046}.
/FTId=VAR_002412.
VARIANT 335 335 G -> D (in Hillsborough; prolonged
thrombin clotting time).
{ECO:0000269|PubMed:11986213}.
/FTId=VAR_015853.
VARIANT 336 336 M -> T (in Asahi; impaired
polymerization; dbSNP:rs121913091).
{ECO:0000269|PubMed:1421174,
ECO:0000269|PubMed:2496144}.
/FTId=VAR_002414.
VARIANT 345 346 Missing (in Vlissingen; defective calcium
binding and impaired polymerization).
{ECO:0000269|PubMed:2071611}.
/FTId=VAR_002415.
VARIANT 345 345 N -> D (in CAFBN; hypofibrinogenemia;
heterozygous; no effect on fibrinogen
complex assembly; decreased fibrinogen
complex secretion).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072728.
VARIANT 355 355 Q -> R (in Nagoya-1; impaired
polymerization; dbSNP:rs121913092).
{ECO:0000269|PubMed:2738036}.
/FTId=VAR_002416.
VARIANT 356 356 D -> V (in DYSFIBRIN; fibrinogen Milano-
1; impaired polymerization;
dbSNP:rs121913094).
{ECO:0000269|PubMed:3708159}.
/FTId=VAR_002418.
VARIANT 356 356 D -> Y (in Kyoto-3; impaired
polymerization; dbSNP:rs121913093).
{ECO:0000269|PubMed:1421174,
ECO:0000269|PubMed:2819242}.
/FTId=VAR_002417.
VARIANT 363 363 N -> K (in Bern-1; impaired
polymerization).
{ECO:0000269|PubMed:8400260}.
/FTId=VAR_002419.
VARIANT 377 377 G -> VMCGEALPMLKDPCYS (in Paris-1;
impaired polymerization).
{ECO:0000269|PubMed:8470043}.
/FTId=VAR_002420.
VARIANT 384 384 S -> C (in Milano-7; impaired
polymerization).
{ECO:0000269|PubMed:8080993}.
/FTId=VAR_002421.
VARIANT 401 401 R -> G (in Osaka-5; dbSNP:rs75848804).
{ECO:0000269|PubMed:1733971}.
/FTId=VAR_002422.
VARIANT 401 401 R -> W (in CAFBN; hypofibrinogenemia;
heterozygous; dbSNP:rs75848804).
{ECO:0000269|PubMed:25427968}.
/FTId=VAR_072729.
VARIANT 404 404 S -> P (in DYSFIBRIN; fibrinogen
Philadelphia; dbSNP:rs587777720).
{ECO:0000269|PubMed:15632207}.
/FTId=VAR_072621.
VARIANT 410 410 M -> V (in dbSNP:rs6061).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014171.
CONFLICT 114 114 K -> I (in Ref. 2; AAB59530/AAB59531).
{ECO:0000305}.
CONFLICT 435 435 R -> Y (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 448 448 Y -> R (in Ref. 15; AA sequence).
{ECO:0000305}.
HELIX 31 33 {ECO:0000244|PDB:3GHG}.
STRAND 34 36 {ECO:0000244|PDB:3GHG}.
STRAND 44 46 {ECO:0000244|PDB:3GHG}.
HELIX 49 94 {ECO:0000244|PDB:3GHG}.
TURN 96 98 {ECO:0000244|PDB:3GHG}.
TURN 115 118 {ECO:0000244|PDB:1FZA}.
TURN 119 122 {ECO:0000244|PDB:1FZB}.
TURN 124 128 {ECO:0000244|PDB:1FZC}.
HELIX 129 160 {ECO:0000244|PDB:1FZC}.
STRAND 161 163 {ECO:0000244|PDB:2HLO}.
STRAND 166 168 {ECO:0000244|PDB:1FZC}.
STRAND 171 178 {ECO:0000244|PDB:2FIB}.
HELIX 179 184 {ECO:0000244|PDB:2FIB}.
STRAND 191 195 {ECO:0000244|PDB:2FIB}.
TURN 198 200 {ECO:0000244|PDB:1FID}.
STRAND 204 210 {ECO:0000244|PDB:2FIB}.
STRAND 212 214 {ECO:0000244|PDB:2HOD}.
STRAND 216 226 {ECO:0000244|PDB:2FIB}.
HELIX 234 239 {ECO:0000244|PDB:2FIB}.
STRAND 241 244 {ECO:0000244|PDB:1FZC}.
STRAND 246 248 {ECO:0000244|PDB:1FZA}.
STRAND 252 254 {ECO:0000244|PDB:1RE3}.
HELIX 256 263 {ECO:0000244|PDB:2FIB}.
HELIX 265 267 {ECO:0000244|PDB:2FIB}.
STRAND 270 277 {ECO:0000244|PDB:2FIB}.
STRAND 279 281 {ECO:0000244|PDB:2OYI}.
STRAND 283 290 {ECO:0000244|PDB:2FIB}.
HELIX 296 298 {ECO:0000244|PDB:2FIB}.
STRAND 301 303 {ECO:0000244|PDB:3HUS}.
STRAND 305 309 {ECO:0000244|PDB:2FIB}.
HELIX 315 317 {ECO:0000244|PDB:2FIB}.
STRAND 322 324 {ECO:0000244|PDB:1FIB}.
HELIX 327 331 {ECO:0000244|PDB:2FIB}.
STRAND 341 343 {ECO:0000244|PDB:1FZA}.
STRAND 346 350 {ECO:0000244|PDB:2FIB}.
HELIX 352 356 {ECO:0000244|PDB:2FIB}.
STRAND 358 360 {ECO:0000244|PDB:2H43}.
STRAND 363 365 {ECO:0000244|PDB:2FIB}.
STRAND 367 369 {ECO:0000244|PDB:2FIB}.
STRAND 370 373 {ECO:0000244|PDB:2HOD}.
STRAND 376 379 {ECO:0000244|PDB:2H43}.
HELIX 382 384 {ECO:0000244|PDB:2FIB}.
STRAND 385 387 {ECO:0000244|PDB:1FIB}.
STRAND 392 395 {ECO:0000244|PDB:2FIB}.
TURN 396 398 {ECO:0000244|PDB:2FIB}.
STRAND 406 414 {ECO:0000244|PDB:2FIB}.
HELIX 415 417 {ECO:0000244|PDB:2FIB}.
STRAND 420 424 {ECO:0000244|PDB:1FID}.
STRAND 426 433 {ECO:0000244|PDB:4B60}.
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


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