FIBB_MOUSE
ID FIBB_MOUSE Reviewed; 481 AA.
AC Q8K0E8; Q91ZP1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Fibrinogen beta chain;
DE Contains:
DE RecName: Full=Fibrinopeptide B;
DE Contains:
DE RecName: Full=Fibrinogen beta chain;
DE Flags: Precursor;
GN Name=Fgb;
OS 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;
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 234-469.
RA Murakawa M., Freeman M.W.;
RT "Mouse fibrinogen B-beta-chain.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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: Cleaved by the protease thrombin to yield monomers which,
CC together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG),
CC polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC function in hemostasis as one of the primary components of blood clots.
CC In addition, functions during the early stages of wound repair to
CC stabilize the lesion and guide cell migration during re-
CC epithelialization. Was originally thought to be essential for platelet
CC aggregation, based on in vitro studies using anticoagulated blood.
CC However, subsequent studies have shown that it is not absolutely
CC required for thrombus formation in vivo. Enhances expression of SELP in
CC activated platelets 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 immune response via both innate and
CC T-cell mediated pathways. {ECO:0000250|UniProtKB:E9PV24}.
CC -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC head to head conformation with the N-termini in a small central domain
CC (By similarity). {ECO:0000250|UniProtKB:P02675}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02675}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P02675}.
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. {ECO:0000250}.
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DR EMBL; BC031715; AAH31715.1; -; mRNA.
DR EMBL; AF413205; AAL02225.1; -; mRNA.
DR CCDS; CCDS17432.1; -.
DR RefSeq; NP_862897.1; NM_181849.3.
DR AlphaFoldDB; Q8K0E8; -.
DR SMR; Q8K0E8; -.
DR BioGRID; 225325; 13.
DR ComplexPortal; CPX-1916; Fibrinogen.
DR IntAct; Q8K0E8; 4.
DR STRING; 10090.ENSMUSP00000039472; -.
DR GlyConnect; 2312; 1 N-Linked glycan (1 site).
DR GlyGen; Q8K0E8; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8K0E8; -.
DR PhosphoSitePlus; Q8K0E8; -.
DR REPRODUCTION-2DPAGE; IPI00279079; -.
DR REPRODUCTION-2DPAGE; Q8K0E8; -.
DR CPTAC; non-CPTAC-3332; -.
DR jPOST; Q8K0E8; -.
DR MaxQB; Q8K0E8; -.
DR PaxDb; Q8K0E8; -.
DR PeptideAtlas; Q8K0E8; -.
DR PRIDE; Q8K0E8; -.
DR ProteomicsDB; 270990; -.
DR Antibodypedia; 855; 607 antibodies from 38 providers.
DR DNASU; 110135; -.
DR Ensembl; ENSMUST00000048246; ENSMUSP00000039472; ENSMUSG00000033831.
DR GeneID; 110135; -.
DR KEGG; mmu:110135; -.
DR UCSC; uc008pph.1; mouse.
DR CTD; 2244; -.
DR MGI; MGI:99501; Fgb.
DR VEuPathDB; HostDB:ENSMUSG00000033831; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158122; -.
DR HOGENOM; CLU_038628_13_0_1; -.
DR InParanoid; Q8K0E8; -.
DR OMA; VYPDAGG; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; Q8K0E8; -.
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-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR BioGRID-ORCS; 110135; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fgb; mouse.
DR PRO; PR:Q8K0E8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8K0E8; protein.
DR Bgee; ENSMUSG00000033831; Expressed in left lobe of liver and 65 other tissues.
DR ExpressionAtlas; Q8K0E8; baseline and differential.
DR Genevisible; Q8K0E8; 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:0005783; C:endoplasmic reticulum; 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:0051087; F:chaperone binding; ISO:MGI.
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:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
DR GO; GO:0042730; P:fibrinolysis; ISO:MGI.
DR GO; GO:0043152; P:induction of bacterial agglutination; 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: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: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; IPR037580; Fibrinogen_beta.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF332; PTHR19143:SF332; 1.
DR Pfam; PF08702; Fib_alpha; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SMART; SM01212; Fib_alpha; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Blood coagulation; Coiled coil; Disulfide bond;
KW Glycoprotein; Hemostasis; Immunity; Innate immunity; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT PEPTIDE 20..34
FT /note="Fibrinopeptide B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000009078"
FT CHAIN 35..481
FT /note="Fibrinogen beta chain"
FT /id="PRO_0000009077"
FT DOMAIN 222..478
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 22..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..37
FT /note="Beta-chain polymerization, binding distal domain of
FT another fibrin"
FT /evidence="ECO:0000250"
FT COILED 149..213
FT /evidence="ECO:0000255"
FT COMPBIAS 29..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 34..35
FT /note="Cleavage; by thrombin; to release fibrinopeptide B"
FT /evidence="ECO:0000250"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 213
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 217
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 221..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 231..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 414..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 481 AA; 54753 MW; 9902830CF708A155 CRC64;
MRHLWLLLLL CVFSVQTQAA DDDYDEPTDS LDARGHRPVD RRKEEPPSLR PAPPPISGGG
YRARPAKATA NQKKVERRPP DAGGCLHADT DMGVLCPTGC TLQQTLLNQE RPIKSSIAEL
NNNIQSVSDT SSVTFQYLTL LKDMWKKKQA QVKENENVIN EYSSILEDQR LYIDETVNDN
IPLNLRVLRS ILEDLRSKIQ KLESDISAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE
TSEMYLIQPD TSIKPYRVYC DMKTENGGWT VIQNRQDGSV DFGRKWDPYK KGFGNIATNE
DAKKYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT VQNEASKYQV
SVNKYKGTAG NALMDGASQL VGENRTMTIH NGMFFSTYDR DNDGWVTTDP RKQCSKEDGG
GWWYNRCHAA NPNGRYYWGG LYSWDMSKHG TDDGVVWMNW KGSWYSMRRM SMKIRPFFPQ
Q
