FIBB_RAT
ID FIBB_RAT Reviewed; 479 AA.
AC P14480; Q5I0P7; Q7TME5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Fibrinogen beta chain;
DE AltName: Full=Liver regeneration-related protein LRRG036/LRRG043/LRRG189;
DE Contains:
DE RecName: Full=Fibrinopeptide B;
DE Contains:
DE RecName: Full=Fibrinogen beta chain;
DE Flags: Precursor;
GN Name=Fgb; ORFNames=Ab1-181, Ab1-216, Ac1-581;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7841303;
RA Courtney M.A., Bunce L.A., Neroni L.A., Simpson-Haidaris P.J.;
RT "Cloning of the complete coding sequence of rat fibrinogen B beta chain
RT cDNA: interspecies conservation of fibrin beta 15-42 primary structure.";
RL Blood Coagul. Fibrinolysis 5:487-496(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Xu C.S., Li W.Q., Li Y.C., Chang C.F., Chai L.Q., Yuan J.Y., Yang K.J.,
RA Yan H.M., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P., Wang G.P.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=6232608; DOI=10.1073/pnas.81.8.2313;
RA Fowlkes D.M., Mullis N.T., Comeau C.M., Crabtree G.R.;
RT "Potential basis for regulation of the coordinately expressed fibrinogen
RT genes: homology in the 5' flanking regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2313-2316(1984).
RN [5]
RP PROTEIN SEQUENCE OF 19-32 (ISOFORM 1).
RA Blombaeck B., Blombaeck M., Grondahl N.J.;
RT "Studies on fibrinopeptides from mammals.";
RL Acta Chem. Scand. 19:1789-1791(1965).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 183-479 (ISOFORMS 1/2).
RX PubMed=2673932; DOI=10.1016/0378-1119(89)90100-5;
RA Eastman E.M., Gilula N.B.;
RT "Cloning and characterization of a cDNA for the B beta chain of rat
RT fibrinogen: evolutionary conservation of translated and 3'-untranslated
RT sequences.";
RL Gene 79:151-158(1989).
RN [7]
RP PROTEIN SEQUENCE OF 151-167; 235-255 AND 415-424 (ISOFORMS 1/2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-479 (ISOFORM 1).
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=3817019; DOI=10.1016/0014-4827(87)90223-0;
RA Sobczak J., Lotti A.-M., Taroux P., Duguet M.;
RT "Molecular cloning of mRNA sequences transiently induced during rat liver
RT regeneration.";
RL Exp. Cell Res. 169:47-56(1987).
CC -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG),
CC polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC function in hemostasis as one of the primary components of blood clots.
CC In addition, functions during the early stages of wound repair to
CC stabilize the lesion and guide cell migration during re-
CC epithelialization. Was originally thought to be essential for platelet
CC aggregation, based on in vitro studies using anticoagulated blood.
CC However subsequent studies have shown that it is not absolutely
CC required for thrombus formation in vivo. Enhances expression of SELP in
CC activated platelets. Maternal fibrinogen is essential for successful
CC pregnancy. Fibrin deposition is also associated with infection, where
CC it protects against IFNG-mediated hemorrhage. May also facilitate the
CC antibacterial immune response via both innate and T-cell mediated
CC pathways. {ECO:0000250|UniProtKB:E9PV24}.
CC -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC head to head conformation with the N-termini in a small central domain
CC (By similarity). {ECO:0000250|UniProtKB:P02675}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P14480-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P14480-2; Sequence=VSP_022492, VSP_022493;
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: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.
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DR EMBL; U05675; AAA64866.1; -; mRNA.
DR EMBL; AY321323; AAP86255.1; -; mRNA.
DR EMBL; AY325147; AAP92548.1; -; mRNA.
DR EMBL; AY325153; AAP92554.1; -; mRNA.
DR EMBL; BC088102; AAH88102.1; -; mRNA.
DR EMBL; K01336; AAA98625.1; -; Genomic_DNA.
DR EMBL; M27220; AAA41160.1; -; mRNA.
DR EMBL; M35602; AAA41159.1; -; mRNA.
DR PIR; A05299; A05299.
DR PIR; I67595; I67595.
DR RefSeq; NP_064456.2; NM_020071.2. [P14480-1]
DR AlphaFoldDB; P14480; -.
DR SMR; P14480; -.
DR IntAct; P14480; 2.
DR STRING; 10116.ENSRNOP00000050663; -.
DR GlyGen; P14480; 1 site.
DR iPTMnet; P14480; -.
DR PhosphoSitePlus; P14480; -.
DR PRIDE; P14480; -.
DR Ensembl; ENSRNOT00000040708; ENSRNOP00000050663; ENSRNOG00000007092. [P14480-2]
DR GeneID; 24366; -.
DR KEGG; rno:24366; -.
DR UCSC; RGD:2604; rat. [P14480-1]
DR CTD; 2244; -.
DR RGD; 2604; Fgb.
DR VEuPathDB; HostDB:ENSRNOG00000007092; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000158122; -.
DR HOGENOM; CLU_038628_13_0_1; -.
DR InParanoid; P14480; -.
DR OMA; VYPDAGG; -.
DR OrthoDB; 357340at2759; -.
DR TreeFam; TF336658; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-354192; Integrin signaling.
DR Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR PRO; PR:P14480; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000007092; Expressed in liver and 17 other tissues.
DR Genevisible; P14480; RN.
DR GO; GO:0072562; C:blood microparticle; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005577; C:fibrinogen complex; ISO:RGD.
DR GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISO:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IEP:RGD.
DR GO; GO:0042730; P:fibrinolysis; ISO:RGD.
DR GO; GO:0043152; P:induction of bacterial agglutination; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:RGD.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0031639; P:plasminogen activation; ISO:RGD.
DR GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:RGD.
DR GO; GO:0051258; P:protein polymerization; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
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; Alternative splicing; Blood coagulation; Coiled coil;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
KW Immunity; Innate immunity; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT PEPTIDE 19..32
FT /note="Fibrinopeptide B"
FT /id="PRO_0000009086"
FT CHAIN 33..479
FT /note="Fibrinogen beta chain"
FT /id="PRO_0000009085"
FT DOMAIN 220..476
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 20..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..35
FT /note="Beta-chain polymerization, binding distal domain of
FT another fibrin"
FT /evidence="ECO:0000250"
FT COMPBIAS 27..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 32..33
FT /note="Cleavage; by thrombin; to release fibrinopeptide B"
FT /evidence="ECO:0000250"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 215
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 219..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 229..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 412..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 1..26
FT /note="MRHLWLLLLSVSLVQTQAATTDSDKV -> MSVPTRDTVITIHELVPNSSNS
FT KRK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_022492"
FT VAR_SEQ 463..479
FT /note="YSMRRMSMKIRPVFPQQ -> TPRQHLLLQRVPPQGSSVVMATCLHGTKCPE
FT SQLLDVHLNED (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_022493"
FT CONFLICT 28..30
FT /note="LSI -> ILS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="P -> A (in Ref. 1; AAA64866)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="S -> Y (in Ref. 1; AAA64866)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="I -> M (in Ref. 1; AAA64866 and 6; AAA41160)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="L -> Q (in Ref. 8; AAA41159)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="S -> T (in Ref. 8; AAA41159)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="S -> A (in Ref. 8; AAA41159)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="R -> K (in Ref. 8; AAA41159)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="V -> F (in Ref. 8; AAA41159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 54235 MW; 810698D9A65D0DE7 CRC64;
MRHLWLLLLS VSLVQTQAAT TDSDKVDLSI ARGHRPVDRR KEEPPSLRPA PPPISGGGYR
ARPAKVDAGQ KKVERKPPDA GGCVHGDGDM GVLCPTGCEL RQTLLNHERP IKNSIAELNS
NINSVSETSS VTFQYLTLLK DMWKKKQAQV KDNENVINEY SSILEDQKLY IDETVNDNIP
LNLRVLRSIL EDLRSKIQKL ESDISAQTEY CHTPCTVNCN IPVVSGKECE EIIRKGGETS
EMYLIQPDTS SKPYRVYCDM KTENGGWTVI QNRQDGSVDF GRKWDPYKKG FGNIATNEDT
KKYCGLPGEY WLGNDKISQL TRIGPTELLI EMEDWKGDKV KAHYGGFTVQ TEANKYQVSV
NKYKGTAGNA LMEGASQLVG ENRTMTIHNG MFFSTYDRDN DGWVTTDPRK QCSKEDGGGW
WYNRCHAANP NGRYYWGGLY SWDMSKHGTD DGVVWMNWKG SWYSMRRMSM KIRPVFPQQ
