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Fibrinogen beta chain (Liver regeneration-related protein LRRG036/LRRG043/LRRG189) [Cleaved into: Fibrinopeptide B; Fibrinogen beta chain]

 FIBB_RAT                Reviewed;         479 AA.
P14480; Q5I0P7; Q7TME5;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-JUN-2018, entry version 148.
RecName: Full=Fibrinogen beta chain;
AltName: Full=Liver regeneration-related protein LRRG036/LRRG043/LRRG189;
Contains:
RecName: Full=Fibrinopeptide B;
Contains:
RecName: Full=Fibrinogen beta chain;
Flags: Precursor;
Name=Fgb; ORFNames=Ab1-181, Ab1-216, Ac1-581;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7841303;
Courtney M.A., Bunce L.A., Neroni L.A., Simpson-Haidaris P.J.;
"Cloning of the complete coding sequence of rat fibrinogen B beta
chain cDNA: interspecies conservation of fibrin beta 15-42 primary
structure.";
Blood Coagul. Fibrinolysis 5:487-496(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Xu C.S., Li W.Q., Li Y.C., Chang C.F., Chai L.Q., Yuan J.Y.,
Yang K.J., Yan H.M., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P.,
Wang G.P., Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
"Liver regeneration after PH.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
PubMed=6232608; DOI=10.1073/pnas.81.8.2313;
Fowlkes D.M., Mullis N.T., Comeau C.M., Crabtree G.R.;
"Potential basis for regulation of the coordinately expressed
fibrinogen genes: homology in the 5' flanking regions.";
Proc. Natl. Acad. Sci. U.S.A. 81:2313-2316(1984).
[5]
PROTEIN SEQUENCE OF 19-32 (ISOFORM 1).
Blombaeck B., Blombaeck M., Grondahl N.J.;
"Studies on fibrinopeptides from mammals.";
Acta Chem. Scand. 19:1789-1791(1965).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 183-479 (ISOFORMS 1/2).
PubMed=2673932; DOI=10.1016/0378-1119(89)90100-5;
Eastman E.M., Gilula N.B.;
"Cloning and characterization of a cDNA for the B beta chain of rat
fibrinogen: evolutionary conservation of translated and 3'-
untranslated sequences.";
Gene 79:151-158(1989).
[7]
PROTEIN SEQUENCE OF 151-167; 235-255 AND 415-424 (ISOFORMS 1/2), AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (DEC-2006) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 425-479 (ISOFORM 1).
STRAIN=Wistar; TISSUE=Liver;
PubMed=3817019; DOI=10.1016/0014-4827(87)90223-0;
Sobczak J., Lotti A.-M., Taroux P., Duguet M.;
"Molecular cloning of mRNA sequences transiently induced during rat
liver regeneration.";
Exp. Cell Res. 169:47-56(1987).
-!- FUNCTION: Cleaved by the protease thrombin to yield monomers
which, together with fibrinogen alpha (FGA) and fibrinogen gamma
(FGG), polymerize to form an insoluble fibrin matrix. Fibrin 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. 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 (By similarity). {ECO:0000250|UniProtKB:P02675}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14480-1; Sequence=Displayed;
Name=2;
IsoId=P14480-2; Sequence=VSP_022492, VSP_022493;
Note=No experimental confirmation available.;
-!- 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:0000250|UniProtKB:P02675}.
-!- 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.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U05675; AAA64866.1; -; mRNA.
EMBL; AY321323; AAP86255.1; -; mRNA.
EMBL; AY325147; AAP92548.1; -; mRNA.
EMBL; AY325153; AAP92554.1; -; mRNA.
EMBL; BC088102; AAH88102.1; -; mRNA.
EMBL; K01336; AAA98625.1; -; Genomic_DNA.
EMBL; M27220; AAA41160.1; -; mRNA.
EMBL; M35602; AAA41159.1; -; mRNA.
PIR; A05299; A05299.
PIR; I67595; I67595.
RefSeq; NP_064456.2; NM_020071.2. [P14480-1]
UniGene; Rn.11416; -.
ProteinModelPortal; P14480; -.
SMR; P14480; -.
IntAct; P14480; 1.
iPTMnet; P14480; -.
PhosphoSitePlus; P14480; -.
PRIDE; P14480; -.
Ensembl; ENSRNOT00000009813; ENSRNOP00000009813; ENSRNOG00000007092. [P14480-1]
Ensembl; ENSRNOT00000040708; ENSRNOP00000050663; ENSRNOG00000007092. [P14480-2]
GeneID; 24366; -.
KEGG; rno:24366; -.
UCSC; RGD:2604; rat. [P14480-1]
CTD; 2244; -.
RGD; 2604; Fgb.
GeneTree; ENSGT00920000148942; -.
HOGENOM; HOG000059561; -.
HOVERGEN; HBG005707; -.
InParanoid; P14480; -.
KO; K03904; -.
OMA; TIHNGMF; -.
OrthoDB; EOG091G03M1; -.
TreeFam; TF336658; -.
Reactome; R-RNO-114608; Platelet degranulation.
Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-RNO-216083; Integrin cell surface interactions.
Reactome; R-RNO-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-RNO-5674135; MAP2K and MAPK activation.
PRO; PR:P14480; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000007092; -.
Genevisible; P14480; RN.
GO; GO:0072562; C:blood microparticle; IDA:RGD.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; IEA:Ensembl.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0044320; P:cellular response to leptin stimulus; IEP:RGD.
GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
GO; GO:0043152; P:induction of bacterial agglutination; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IEA:Ensembl.
GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0051258; P:protein polymerization; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
CDD; cd00087; FReD; 1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
InterPro; IPR037580; Fibrinogen_beta.
InterPro; IPR020837; Fibrinogen_CS.
PANTHER; PTHR19143:SF332; PTHR19143:SF332; 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;
Adaptive immunity; Alternative splicing; Blood coagulation;
Coiled coil; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemostasis; Immunity; Innate immunity;
Reference proteome; Secreted; Signal.
SIGNAL 1 18
PEPTIDE 19 32 Fibrinopeptide B.
/FTId=PRO_0000009086.
CHAIN 33 479 Fibrinogen beta chain.
/FTId=PRO_0000009085.
DOMAIN 220 476 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
REGION 33 35 Beta-chain polymerization, binding distal
domain of another fibrin. {ECO:0000250}.
SITE 32 33 Cleavage; by thrombin; to release
fibrinopeptide B. {ECO:0000250}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 211 211 Interchain (with alpha chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 215 215 Interchain (with gamma chain).
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 219 304 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 229 258 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 412 425 {ECO:0000255|PROSITE-ProRule:PRU00739}.
VAR_SEQ 1 26 MRHLWLLLLSVSLVQTQAATTDSDKV -> MSVPTRDTVIT
IHELVPNSSNSKRK (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_022492.
VAR_SEQ 463 479 YSMRRMSMKIRPVFPQQ -> TPRQHLLLQRVPPQGSSVVM
ATCLHGTKCPESQLLDVHLNED (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_022493.
CONFLICT 28 30 LSI -> ILS (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 95 95 P -> A (in Ref. 1; AAA64866).
{ECO:0000305}.
CONFLICT 126 126 S -> Y (in Ref. 1; AAA64866).
{ECO:0000305}.
CONFLICT 197 197 I -> M (in Ref. 1; AAA64866 and 6;
AAA41160). {ECO:0000305}.
CONFLICT 439 439 L -> Q (in Ref. 8; AAA41159).
{ECO:0000305}.
CONFLICT 441 441 S -> T (in Ref. 8; AAA41159).
{ECO:0000305}.
CONFLICT 445 445 S -> A (in Ref. 8; AAA41159).
{ECO:0000305}.
CONFLICT 467 467 R -> K (in Ref. 8; AAA41159).
{ECO:0000305}.
CONFLICT 475 475 V -> F (in Ref. 8; AAA41159).
{ECO:0000305}.
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


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