FIBG_MOUSE
ID FIBG_MOUSE Reviewed; 436 AA.
AC Q8VCM7; Q8WUR3; Q91ZP0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Fibrinogen gamma chain;
DE Flags: Precursor;
GN Name=Fgg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-352.
RA Murakawa M., Freeman M.W.;
RT "Mouse fibrinogen gamma-chain.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND MUTAGENESIS OF 432-GLN--VAL-436.
RX PubMed=19332769; DOI=10.1182/blood-2008-03-145821;
RA Yang H., Lang S., Zhai Z., Li L., Kahr W.H., Chen P., Brkic J.,
RA Spring C.M., Flick M.J., Degen J.L., Freedman J., Ni H.;
RT "Fibrinogen is required for maintenance of platelet intracellular and cell-
RT surface P-selectin expression.";
RL Blood 114:425-436(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta
CC (FGB), polymerizes to form an insoluble fibrin matrix (By similarity).
CC Fibrin has a major function in hemostasis as one of the primary
CC components of blood clots (By similarity). In addition, functions
CC during the early stages of wound repair to stabilize the lesion and
CC guide cell migration during re-epithelialization (By similarity). Was
CC originally thought to be essential for platelet aggregation, based on
CC in vitro studies using anticoagulated blood. However, subsequent
CC studies have shown that it is not absolutely required for thrombus
CC formation in vivo (By similarity). Enhances expression of SELP in
CC activated platelets via an ITGB3-dependent pathway (PubMed:19332769).
CC Maternal fibrinogen is essential for successful pregnancy (By
CC similarity). Fibrin deposition is also associated with infection, where
CC it protects against IFNG-mediated hemorrhage (By similarity). May also
CC facilitate the immune response via both innate and T-cell mediated
CC pathways (By similarity). {ECO:0000250|UniProtKB:E9PV24,
CC ECO:0000269|PubMed:19332769}.
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 (By similarity). {ECO:0000250|UniProtKB:P02679}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02679}.
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:0000250|UniProtKB:P02679}.
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 (By similarity). {ECO:0000250}.
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DR EMBL; BC019506; AAH19506.1; -; mRNA.
DR EMBL; BC019828; AAH19828.1; -; mRNA.
DR EMBL; AF413206; AAL02226.1; -; mRNA.
DR CCDS; CCDS38462.1; -.
DR RefSeq; NP_598623.1; NM_133862.2.
DR AlphaFoldDB; Q8VCM7; -.
DR SMR; Q8VCM7; -.
DR BioGRID; 221284; 12.
DR ComplexPortal; CPX-1916; Fibrinogen.
DR IntAct; Q8VCM7; 4.
DR STRING; 10090.ENSMUSP00000037018; -.
DR GlyGen; Q8VCM7; 1 site.
DR iPTMnet; Q8VCM7; -.
DR PhosphoSitePlus; Q8VCM7; -.
DR REPRODUCTION-2DPAGE; Q8VCM7; -.
DR CPTAC; non-CPTAC-3323; -.
DR CPTAC; non-CPTAC-3431; -.
DR jPOST; Q8VCM7; -.
DR MaxQB; Q8VCM7; -.
DR PaxDb; Q8VCM7; -.
DR PRIDE; Q8VCM7; -.
DR ProteomicsDB; 271696; -.
DR ABCD; Q8VCM7; 1 sequenced antibody.
DR Antibodypedia; 16774; 725 antibodies from 37 providers.
DR DNASU; 99571; -.
DR Ensembl; ENSMUST00000048486; ENSMUSP00000037018; ENSMUSG00000033860.
DR GeneID; 99571; -.
DR KEGG; mmu:99571; -.
DR UCSC; uc008ppe.1; mouse.
DR CTD; 2266; -.
DR MGI; MGI:95526; Fgg.
DR VEuPathDB; HostDB:ENSMUSG00000033860; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158467; -.
DR HOGENOM; CLU_038628_13_0_1; -.
DR InParanoid; Q8VCM7; -.
DR OMA; TYHNGMR; -.
DR PhylomeDB; Q8VCM7; -.
DR TreeFam; TF336658; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 99571; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8VCM7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VCM7; protein.
DR Bgee; ENSMUSG00000033860; Expressed in left lobe of liver and 74 other tissues.
DR ExpressionAtlas; Q8VCM7; baseline and differential.
DR Genevisible; Q8VCM7; MM.
DR GO; GO:0072562; C:blood microparticle; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005577; C:fibrinogen complex; ISO:MGI.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0042730; P:fibrinolysis; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISO:MGI.
DR GO; GO:0031639; P:plasminogen activation; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0051258; P:protein polymerization; ISO:MGI.
DR GO; GO:0009306; P:protein secretion; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
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 Adaptive immunity; Blood coagulation; Calcium; Coiled coil; Disulfide bond;
KW Glycoprotein; Hemostasis; Immunity; Innate immunity; Isopeptide bond;
KW Metal-binding; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..436
FT /note="Fibrinogen gamma chain"
FT /id="PRO_0000009100"
FT DOMAIN 169..415
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02680"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 34
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 44
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 48
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 160
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 164
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 178..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 351..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CROSSLNK 423
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-431)"
FT /evidence="ECO:0000250"
FT CROSSLNK 431
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-423)"
FT /evidence="ECO:0000250"
FT MUTAGEN 432..436
FT /note="Missing: Impairs induction of SELP in activated
FT platelets."
FT /evidence="ECO:0000269|PubMed:19332769"
SQ SEQUENCE 436 AA; 49391 MW; FF45A34B6C92143E CRC64;
MSWSLQPPSF LLCCLLLLFS PTGLAYVATR DNCCILDERF GSFCPTTCGI ADFLSSYQTD
VDNDLRTLED ILFRAENRTT EAKELIKAIQ VYYNPDQPPK PGMIDSATQK SKKMVEEIVK
YEALLLTHET SIRYLQEIYN SNNQKITNLK QKVAQLEAQC QEPCKDSVQI HDTTGKDCQE
IANKGAKESG LYFIRPLKAK QQFLVYCEID GSGNGWTVLQ KRIDGSLDFK KNWIQYKEGF
GHLSPTGTTE FWLGNEKIHL ISMQSTIPYA LRIQLKDWNG RTSTADYAMF RVGPESDKYR
LTYAYFIGGD AGDAFDGYDF GDDPSDKFFT SHNGMQFSTW DNDNDKFEGN CAEQDGSGWW
MNKCHAGHLN GVYHQGGTYS KSSTTNGFDD GIIWATWKSR WYSMKETTMK IIPFNRLSIG
EGQQHHMGGS KQAGDV
